{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,21]],"date-time":"2026-09-21T22:36:21Z","timestamp":1790030181704,"version":"4.0.1"},"reference-count":138,"publisher":"American Association for the Advancement of Science (AAAS)","issue":"2","content-domain":{"domain":["www.science.org"],"crossmark-restriction":true},"short-container-title":["Sci. Adv."],"published-print":{"date-parts":[[2024,1,12]]},"abstract":"<jats:p>\n            Transcription factors play vital roles in neuron development; however, little is known about the role of these proteins in maintaining neuronal homeostasis. Here, we show that the transcription factor RREB1 (Ras-responsive element-binding protein 1) is essential for neuron survival in the mammalian brain. A spontaneous mouse mutation causing loss of a nervous system\u2013enriched\n            <jats:italic>Rreb1<\/jats:italic>\n            transcript is associated with progressive loss of cerebellar Purkinje cells and ataxia. Analysis of chromatin immunoprecipitation and sequencing, along with RNA sequencing data revealed dysregulation of RREB1 targets associated with the microtubule cytoskeleton. In agreement with the known role of microtubules in dendritic development, dendritic complexity was disrupted in\n            <jats:italic>Rreb1<\/jats:italic>\n            -deficient neurons. Analysis of sequencing data also suggested that RREB1 plays a role in the endomembrane system. Mutant Purkinje cells had fewer numbers of autophagosomes and lysosomes and contained P62- and ubiquitin-positive inclusions. Together, these studies demonstrate that RREB1 functions to maintain the microtubule network and proteostasis in mammalian neurons.\n          <\/jats:p>","DOI":"10.1126\/sciadv.adh3929","type":"journal-article","created":{"date-parts":[[2024,1,10]],"date-time":"2024-01-10T18:59:55Z","timestamp":1704913195000},"update-policy":"https:\/\/doi.org\/10.34133\/aaas_crossmark","source":"Crossref","is-referenced-by-count":15,"title":["RREB1 regulates neuronal proteostasis and the microtubule network"],"prefix":"10.1126","volume":"10","author":[{"ORCID":"https:\/\/orcid.org\/0000-0003-1653-1829","authenticated-orcid":true,"given":"Emily N.","family":"Griffin","sequence":"first","affiliation":[{"name":"Howard Hughes Medical Institute, Department of Cellular and Molecular Medicine, Department of Neurobiology, University of California, San Diego, La Jolla, CA 92093, USA."}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0009-0004-9331-9228","authenticated-orcid":true,"given":"Thomas","family":"Jucius","sequence":"additional","affiliation":[{"name":"Howard Hughes Medical Institute, Department of Cellular and Molecular Medicine, Department of Neurobiology, University of California, San Diego, La Jolla, CA 92093, USA."}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-3711-5322","authenticated-orcid":true,"given":"Su-Eon","family":"Sim","sequence":"additional","affiliation":[{"name":"Howard Hughes Medical Institute, Department of Cellular and Molecular Medicine, Department of Neurobiology, University of California, San Diego, La Jolla, CA 92093, USA."}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0009-0003-2008-5486","authenticated-orcid":true,"given":"Belinda S.","family":"Harris","sequence":"additional","affiliation":[{"name":"The Jackson Laboratory, Bar Harbor, ME 04609, USA."}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-4665-1007","authenticated-orcid":true,"given":"Sven","family":"Heinz","sequence":"additional","affiliation":[{"name":"Department of Medicine, University of California, San Diego, La Jolla, CA 92093, USA."}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-6740-593X","authenticated-orcid":true,"given":"Susan L.","family":"Ackerman","sequence":"additional","affiliation":[{"name":"Howard Hughes Medical Institute, Department of Cellular and Molecular Medicine, Department of Neurobiology, University of California, San Diego, La Jolla, CA 92093, USA."}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"221","reference":[{"key":"e_1_3_3_2_2","doi-asserted-by":"crossref","first-page":"6","DOI":"10.1186\/s40035-017-0077-5","article-title":"Protein misfolding in neurodegenerative diseases: Implications and strategies","volume":"6","author":"Sweeney P.","year":"2017","unstructured":"P. Sweeney, H. Park, M. Baumann, J. Dunlop, J. Frydman, R. Kopito, A. McCampbell, G. Leblanc, A. Venkateswaran, A. Nurmi, R. Hodgson, Protein misfolding in neurodegenerative diseases: Implications and strategies. Transl. Neurodegener. 6, 6 (2017).","journal-title":"Transl. Neurodegener."},{"key":"e_1_3_3_3_2","doi-asserted-by":"crossref","first-page":"83","DOI":"10.1016\/j.nbd.2018.05.012","article-title":"TFEB dysregulation as a driver of autophagy dysfunction in neurodegenerative disease: Molecular mechanisms, cellular processes, and emerging therapeutic opportunities","volume":"122","author":"Cortes C. J.","year":"2019","unstructured":"C. J. Cortes, A. R. La Spada, TFEB dysregulation as a driver of autophagy dysfunction in neurodegenerative disease: Molecular mechanisms, cellular processes, and emerging therapeutic opportunities. Neurobiol. Dis. 122, 83\u201393 (2019).","journal-title":"Neurobiol. Dis."},{"key":"e_1_3_3_4_2","doi-asserted-by":"crossref","first-page":"2355","DOI":"10.1084\/jem.20172158","article-title":"TFEB enhances astroglial uptake of extracellular tau species and reduces tau spreading","volume":"215","author":"Martini-Stoica H.","year":"2018","unstructured":"H. Martini-Stoica, A. L. Cole, D. B. Swartzlander, F. Chen, Y. W. Wan, L. Bajaj, D. A. Bader, V. M. Y. Lee, J. Q. Trojanowski, Z. Liu, M. Sardiello, H. Zheng, TFEB enhances astroglial uptake of extracellular tau species and reduces tau spreading. J. Exp. Med. 215, 2355\u20132377 (2018).","journal-title":"J. Exp. Med."},{"key":"e_1_3_3_5_2","doi-asserted-by":"crossref","first-page":"105855","DOI":"10.1016\/j.nbd.2022.105855","article-title":"TFEB in Alzheimer\u2019s disease: From molecular mechanisms to therapeutic implications","volume":"173","author":"Gu Z.","year":"2022","unstructured":"Z. Gu, H. Cao, C. Zuo, Y. Huang, J. Miao, Y. Song, Y. Yang, L. Zhu, F. Wang, TFEB in Alzheimer\u2019s disease: From molecular mechanisms to therapeutic implications. Neurobiol. Dis. 173, 105855 (2022).","journal-title":"Neurobiol. Dis."},{"key":"e_1_3_3_6_2","doi-asserted-by":"crossref","first-page":"761773","DOI":"10.3389\/fcell.2021.761773","article-title":"TFE3-mediated autophagy is involved in dopaminergic neurodegeneration in Parkinson\u2019s disease","volume":"9","author":"He X.","year":"2021","unstructured":"X. He, Y. Xie, Q. Zheng, Z. Zhang, S. Ma, J. Li, M. Li, Q. Huang, TFE3-mediated autophagy is involved in dopaminergic neurodegeneration in Parkinson\u2019s disease. Front. Cell Dev. Biol. 9, 761773 (2021).","journal-title":"Front. Cell Dev. Biol."},{"key":"e_1_3_3_7_2","doi-asserted-by":"crossref","first-page":"227","DOI":"10.1038\/modpathol.2015.153","article-title":"Genomic copy number analysis of a spectrum of blue nevi identifies recurrent aberrations of entire chromosomal arms in melanoma ex blue nevus","volume":"29","author":"Chan M. P.","year":"2016","unstructured":"M. P. Chan, A. A. Andea, P. W. Harms, A. B. Durham, R. M. Patel, M. Wang, P. Robichaud, G. J. Fisher, T. M. Johnson, D. R. Fullen, Genomic copy number analysis of a spectrum of blue nevi identifies recurrent aberrations of entire chromosomal arms in melanoma ex blue nevus. Mod. Pathol. 29, 227\u2013239 (2016).","journal-title":"Mod. Pathol."},{"key":"e_1_3_3_8_2","doi-asserted-by":"crossref","first-page":"1518","DOI":"10.1002\/pros.21368","article-title":"hZIP1 zinc transporter down-regulation in prostate cancer involves the overexpression of ras responsive element binding protein-1 (RREB-1)","volume":"71","author":"Zou J.","year":"2011","unstructured":"J. Zou, B. C. Milon, M. M. Desouki, L. C. Costello, R. B. Franklin, hZIP1 zinc transporter down-regulation in prostate cancer involves the overexpression of ras responsive element binding protein-1 (RREB-1). Prostate 71, 1518\u20131524 (2011).","journal-title":"Prostate"},{"key":"e_1_3_3_9_2","doi-asserted-by":"crossref","first-page":"695","DOI":"10.1097\/DAD.0000000000000567","article-title":"Blue nevus\u2013like metastasis of a cutaneous melanoma identified by fluorescence in situ hybridization","volume":"38","author":"Campa M.","year":"2016","unstructured":"M. Campa, M. Patel, P. Aubert, G. Hosler, D. Witheiler, Blue nevus\u2013like metastasis of a cutaneous melanoma identified by fluorescence in situ hybridization. Am. J. Dermatopathol. 38, 695\u2013697 (2016).","journal-title":"Am. J. Dermatopathol."},{"key":"e_1_3_3_10_2","doi-asserted-by":"crossref","first-page":"253","DOI":"10.1097\/DAD.0000000000000380","article-title":"Fluorescence in situ hybridization for melanoma diagnosis","volume":"38","author":"Ferrara G.","year":"2016","unstructured":"G. Ferrara, A. C. De Vanna, Fluorescence in situ hybridization for melanoma diagnosis. Am. J. Dermatopathol. 38, 253\u2013269 (2016).","journal-title":"Am. J. Dermatopathol."},{"key":"e_1_3_3_11_2","doi-asserted-by":"crossref","first-page":"169","DOI":"10.1111\/cup.14352","article-title":"A novel method to assess copy number variation in melanoma: Droplet digital PCR for precise quantitation of the RREB1 gene in FFPE melanocytic neoplasms, a proof-of-concept study","volume":"50","author":"O\u2019Hern K.","year":"2022","unstructured":"K. O\u2019Hern, R. Barney, M. Chambers, C. Baker, M. Stevanovic, G. J. Tsongalis, E. Hughes, A. Sriharan, A novel method to assess copy number variation in melanoma: Droplet digital PCR for precise quantitation of the RREB1 gene in FFPE melanocytic neoplasms, a proof-of-concept study. J. Cutan. Pathol. 50, 169\u2013177 (2022).","journal-title":"J. Cutan. Pathol."},{"key":"e_1_3_3_12_2","doi-asserted-by":"crossref","first-page":"1328","DOI":"10.5858\/arpa.2014-0307-CC","article-title":"Clear cell melanoma: A cutaneous clear cell malignancy","volume":"138","author":"Pletneva M. A.","year":"2014","unstructured":"M. A. Pletneva, A. Andea, N. Palanisamy, B. L. Betz, S. Carskadon, M. Wang, R. M. Patel, D. R. Fullen, P. W. Harms, Clear cell melanoma: A cutaneous clear cell malignancy. Arch. Pathol. Lab. Med. 138, 1328\u20131336 (2014).","journal-title":"Arch. Pathol. Lab. Med."},{"key":"e_1_3_3_13_2","doi-asserted-by":"crossref","first-page":"566","DOI":"10.1038\/s41586-019-1897-5","article-title":"TGF-\u03b2 orchestrates fibrogenic and developmental EMTs via the RAS effector RREB1","volume":"577","author":"Su J.","year":"2020","unstructured":"J. Su, S. M. Morgani, C. J. David, Q. Wang, E. E. Er, Y.-H. Huang, H. Basnet, Y. Zou, W. Shu, R. K. Soni, R. C. Hendrickson, A.-K. Hadjantonakis, J. Massagu\u00e9, TGF-\u03b2 orchestrates fibrogenic and developmental EMTs via the RAS effector RREB1. Nature 577, 566\u2013571 (2020).","journal-title":"Nature"},{"key":"e_1_3_3_14_2","doi-asserted-by":"crossref","first-page":"e64811","DOI":"10.7554\/eLife.64811","article-title":"The transcription factor Rreb1 regulates epithelial architecture, invasiveness, and vasculogenesis in early mouse embryos","volume":"10","author":"Morgani S. M.","year":"2021","unstructured":"S. M. Morgani, J. Su, J. Nichols, J. Massagu\u00e9, A.-K. Hadjantonakis, The transcription factor Rreb1 regulates epithelial architecture, invasiveness, and vasculogenesis in early mouse embryos. eLife 10, e64811 (2021).","journal-title":"eLife"},{"key":"e_1_3_3_15_2","doi-asserted-by":"crossref","first-page":"223","DOI":"10.1126\/science.2109351","article-title":"A promoter that drives transgene expression in cerebellar purkinje and retinal bipolar neurons","volume":"248","author":"Oberdick J.","year":"1990","unstructured":"J. Oberdick, R. J. Smeyne, J. R. Mann, S. Zackson, J. I. Morgan, A promoter that drives transgene expression in cerebellar purkinje and retinal bipolar neurons. Science 248, 223\u2013226 (1990).","journal-title":"Science"},{"key":"e_1_3_3_16_2","doi-asserted-by":"crossref","first-page":"259","DOI":"10.1128\/MCB.23.1.259-271.2003","article-title":"Novel transcriptional potentiation of BETA2\/NeuroD on the secretin gene promoter by the DNA-binding protein finb\/RREB-1","volume":"23","author":"Ray S. K.","year":"2003","unstructured":"S. K. Ray, J. Nishitani, M. W. Petry, M. Y. Fessing, A. B. Leiter, Novel transcriptional potentiation of BETA2\/NeuroD on the secretin gene promoter by the DNA-binding protein finb\/RREB-1. Mol. Cell. Biol. 23, 259\u2013271 (2003).","journal-title":"Mol. Cell. Biol."},{"key":"e_1_3_3_17_2","doi-asserted-by":"crossref","first-page":"13939","DOI":"10.1073\/pnas.0907143106","article-title":"Cell-type-specific isolation of ribosome-associated mRNA from complex tissues","volume":"106","author":"Sanz E.","year":"2009","unstructured":"E. Sanz, L. Yang, T. Su, D. R. Morris, G. S. McKnight, P. S. Amieux, Cell-type-specific isolation of ribosome-associated mRNA from complex tissues. Proc. Natl. Acad. Sci. U.S.A. 106, 13939\u201313944 (2009).","journal-title":"Proc. Natl. Acad. Sci. U.S.A."},{"key":"e_1_3_3_18_2","doi-asserted-by":"crossref","first-page":"4587","DOI":"10.1523\/JNEUROSCI.2757-14.2015","article-title":"Mutations in the microtubule-associated protein 1A (Map1a) gene cause Purkinje cell degeneration","volume":"35","author":"Liu Y.","year":"2015","unstructured":"Y. Liu, J. W. Lee, S. L. Ackerman, Mutations in the microtubule-associated protein 1A (Map1a) gene cause Purkinje cell degeneration. J. Neurosci. 35, 4587\u20134598 (2015).","journal-title":"J. Neurosci."},{"key":"e_1_3_3_19_2","doi-asserted-by":"crossref","first-page":"6018","DOI":"10.1007\/s12035-015-9508-4","article-title":"Microtubule-actin crosslinking factor 1 is required for dendritic arborization and axon outgrowth in the developing brain","volume":"53","author":"Ka M.","year":"2016","unstructured":"M. Ka, W.-Y. Kim, Microtubule-actin crosslinking factor 1 is required for dendritic arborization and axon outgrowth in the developing brain. Mol. Neurobiol. 53, 6018\u20136032 (2016).","journal-title":"Mol. Neurobiol."},{"key":"e_1_3_3_20_2","doi-asserted-by":"crossref","first-page":"2773","DOI":"10.1038\/s41467-018-05124-5","article-title":"APC2 controls dendrite development by promoting microtubule dynamics","volume":"9","author":"Kahn O. I.","year":"2018","unstructured":"O. I. Kahn, P. Sch\u00e4tzle, D. van de Willige, R. P. Tas, F. W. Lindhout, S. Portegies, L. C. Kapitein, C. C. Hoogenraad, APC2 controls dendrite development by promoting microtubule dynamics. Nat. Commun. 9, 2773 (2018).","journal-title":"Nat. Commun."},{"key":"e_1_3_3_21_2","doi-asserted-by":"crossref","first-page":"3","DOI":"10.1002\/path.2697","article-title":"Autophagy: Cellular and molecular mechanisms","volume":"221","author":"Glick D.","year":"2010","unstructured":"D. Glick, S. Barth, K. F. Macleod, Autophagy: Cellular and molecular mechanisms. J. Pathol. 221, 3\u201312 (2010).","journal-title":"J. Pathol."},{"key":"e_1_3_3_22_2","doi-asserted-by":"crossref","first-page":"e202102001","DOI":"10.1083\/jcb.202102001","article-title":"Lysosome biogenesis: Regulation and functions","volume":"220","author":"Yang C.","year":"2021","unstructured":"C. Yang, X. Wang, Lysosome biogenesis: Regulation and functions. J. Cell Biol. 220, e202102001 (2021).","journal-title":"J. Cell Biol."},{"key":"e_1_3_3_23_2","doi-asserted-by":"crossref","first-page":"17693","DOI":"10.1073\/pnas.1212786109","article-title":"Development of Purkinje cell degeneration in a knockin mouse model reveals lysosomal involvement in the pathogenesis of SCA6","volume":"109","author":"Unno T.","year":"2012","unstructured":"T. Unno, M. Wakamori, M. Koike, Y. Uchiyama, K. Ishikawa, H. Kubota, T. Yoshida, H. Sasakawa, C. Peters, H. Mizusawa, K. Watase, Development of Purkinje cell degeneration in a knockin mouse model reveals lysosomal involvement in the pathogenesis of SCA6. PNAS. 109, 17693\u201317698 (2012).","journal-title":"PNAS."},{"key":"e_1_3_3_24_2","first-page":"e21225","article-title":"Potential neuron-autonomous Purkinje cell degeneration by 2\u2032,3\u2032-cyclic nucleotide 3\u2032-phosphodiesterase promoter\/Cre-mediated autophagy impairments","volume":"35","author":"Jo Y. R.","year":"2021","unstructured":"Y. R. Jo, H. R. Kim, S. Y. Jang, H. Go, M. Song, D. K. Park, Y. Oh, J. Jo, Y. K. Shin, S. J. Lee, S. Cheon, H. K. Lee, K. E. Lee, Y. H. Kim, H. T. Park, Potential neuron-autonomous Purkinje cell degeneration by 2\u2032,3\u2032-cyclic nucleotide 3\u2032-phosphodiesterase promoter\/Cre-mediated autophagy impairments. FASEB J. 35, e21225 (2021).","journal-title":"FASEB J."},{"key":"e_1_3_3_25_2","doi-asserted-by":"crossref","first-page":"1586","DOI":"10.1016\/j.ajpath.2017.02.020","article-title":"Purkinje cells are more vulnerable to the specific depletion of cathepsin D than to that of Atg7","volume":"187","author":"Koike M.","year":"2017","unstructured":"M. Koike, M. Shibata, T. Sunabori, J. Yamaguchi, K. Sakimura, M. Komatsu, K. Tanaka, Y. Uchiyama, Purkinje cells are more vulnerable to the specific depletion of cathepsin D than to that of Atg7. Am. J. Pathol. 187, 1586\u20131600 (2017).","journal-title":"Am. J. Pathol."},{"key":"e_1_3_3_26_2","doi-asserted-by":"crossref","first-page":"11492","DOI":"10.1016\/S0021-9258(19)78150-2","article-title":"Molecular characterization of light chain 3. A microtubule binding subunit of MAP1A and MAP1B","volume":"269","author":"Mann S. S.","year":"1994","unstructured":"S. S. Mann, J. A. Hammarback, Molecular characterization of light chain 3. A microtubule binding subunit of MAP1A and MAP1B. J. Biol. Chem. 269, 11492\u201311497 (1994).","journal-title":"J. Biol. Chem."},{"key":"e_1_3_3_27_2","doi-asserted-by":"crossref","first-page":"711","DOI":"10.1242\/jcs.96.4.711","article-title":"Microtubule depolymerization inhibits transport of cathepsin D from the Golgi apparatus to lysosomes","volume":"96","author":"Scheel J.","year":"1990","unstructured":"J. Scheel, R. Matteoni, T. Ludwig, B. Hoflack, T. E. Kreis, Microtubule depolymerization inhibits transport of cathepsin D from the Golgi apparatus to lysosomes. J. Cell Sci. 96, 711\u2013720 (1990).","journal-title":"J. Cell Sci."},{"key":"e_1_3_3_28_2","doi-asserted-by":"crossref","first-page":"36303","DOI":"10.1074\/jbc.M607031200","article-title":"Microtubules support production of starvation-induced autophagosomes but not their targeting and fusion with lysosomes","volume":"281","author":"Fass E.","year":"2006","unstructured":"E. Fass, E. Shvets, I. Degani, K. Hirschberg, Z. Elazar, Microtubules support production of starvation-induced autophagosomes but not their targeting and fusion with lysosomes. J. Biol. Chem. 281, 36303\u201336316 (2006).","journal-title":"J. Biol. Chem."},{"key":"e_1_3_3_29_2","doi-asserted-by":"crossref","first-page":"458","DOI":"10.1002\/jcp.1041520304","article-title":"Cytoskeletal elements are required for the formation and maturation of autophagic vacuoles","volume":"152","author":"Aplin A.","year":"1992","unstructured":"A. Aplin, T. Jasionowski, D. L. Tuttle, S. E. Lenk, W. A. Dunn, Cytoskeletal elements are required for the formation and maturation of autophagic vacuoles. J. Cell. Physiol. 152, 458\u2013466 (1992).","journal-title":"J. Cell. Physiol."},{"key":"e_1_3_3_30_2","doi-asserted-by":"crossref","first-page":"129","DOI":"10.1111\/j.1600-0854.2005.00368.x","article-title":"Microtubules facilitate autophagosome formation and fusion of autophagosomes with endosomes","volume":"7","author":"K\u00f6chl R.","year":"2006","unstructured":"R. K\u00f6chl, X. W. Hu, E. Y. W. Chan, S. A. Tooze, Microtubules facilitate autophagosome formation and fusion of autophagosomes with endosomes. Traffic 7, 129\u2013145 (2006).","journal-title":"Traffic"},{"key":"e_1_3_3_31_2","doi-asserted-by":"crossref","first-page":"2541","DOI":"10.1016\/j.biocel.2004.02.003","article-title":"Microtubule disruption inhibits autophagosome-lysosome fusion: Implications for studying the roles of aggresomes in polyglutamine diseases","volume":"36","author":"Webb J. L.","year":"2004","unstructured":"J. L. Webb, B. Ravikumar, D. C. Rubinsztein, Microtubule disruption inhibits autophagosome-lysosome fusion: Implications for studying the roles of aggresomes in polyglutamine diseases. Int. J. Biochem. Cell Biol. 36, 2541\u20132550 (2004).","journal-title":"Int. J. Biochem. Cell Biol."},{"key":"e_1_3_3_32_2","doi-asserted-by":"crossref","first-page":"777","DOI":"10.1038\/nrm1739","article-title":"The cell biology of neurogenesis","volume":"6","author":"G\u00f6tz M.","year":"2005","unstructured":"M. G\u00f6tz, W. B. Huttner, The cell biology of neurogenesis. Nat. Rev. Mol. Cell Biol. 6, 777\u2013788 (2005).","journal-title":"Nat. Rev. Mol. Cell Biol."},{"key":"e_1_3_3_33_2","first-page":"a001800","article-title":"The growth cone cytoskeleton in axon outgrowth and guidance","volume":"3","author":"Dent E. W.","year":"2011","unstructured":"E. W. Dent, S. L. Gupton, F. B. Gertler, The growth cone cytoskeleton in axon outgrowth and guidance. Cold Spring Harb. Perspect. Biol. 3, a001800 (2011).","journal-title":"Cold Spring Harb. Perspect. Biol."},{"key":"e_1_3_3_34_2","doi-asserted-by":"crossref","first-page":"319","DOI":"10.1038\/nrn2631","article-title":"Microtubule assembly, organization and dynamics in axons and dendrites","volume":"10","author":"Conde C.","year":"2009","unstructured":"C. Conde, A. C\u00e1ceres, Microtubule assembly, organization and dynamics in axons and dendrites. Nat. Rev. Neurosci. 10, 319\u2013332 (2009).","journal-title":"Nat. Rev. Neurosci."},{"key":"e_1_3_3_35_2","doi-asserted-by":"crossref","first-page":"623","DOI":"10.1016\/j.tig.2007.09.003","article-title":"Genetic mechanisms underlying abnormal neuronal migration in classical lissencephaly","volume":"23","author":"Kerjan G.","year":"2007","unstructured":"G. Kerjan, J. G. Gleeson, Genetic mechanisms underlying abnormal neuronal migration in classical lissencephaly. Trends Genet. 23, 623\u2013630 (2007).","journal-title":"Trends Genet."},{"key":"e_1_3_3_36_2","doi-asserted-by":"crossref","first-page":"18","DOI":"10.1016\/j.nbd.2015.08.003","article-title":"Neuronal migration disorders: Focus on the cytoskeleton and epilepsy","volume":"92","author":"Stouffer M. A.","year":"2016","unstructured":"M. A. Stouffer, J. A. Golden, F. Francis, Neuronal migration disorders: Focus on the cytoskeleton and epilepsy. Neurobiol. Dis. 92, 18\u201345 (2016).","journal-title":"Neurobiol. Dis."},{"key":"e_1_3_3_37_2","doi-asserted-by":"crossref","first-page":"1820","DOI":"10.1016\/j.cub.2005.08.069","article-title":"Activity-driven dendritic remodeling requires microtubule-associated protein 1A","volume":"15","author":"Szebenyi G.","year":"2005","unstructured":"G. Szebenyi, F. Bollati, M. Bisbal, S. Sheridan, L. Faas, R. Wray, S. Haferkamp, S. Nguyen, A. Caceres, S. T. Brady, Activity-driven dendritic remodeling requires microtubule-associated protein 1A. Curr. Biol. 15, 1820\u20131826 (2005).","journal-title":"Curr. Biol."},{"key":"e_1_3_3_38_2","first-page":"1043","article-title":"Cortactin binding protein 2 increases microtubule stability and regulates dendritic arborization","volume":"32","author":"Shih P.-Y.","year":"2014","unstructured":"P.-Y. Shih, S.-P. Lee, Y.-K. Chen, Y.-P. Hsueh, Cortactin binding protein 2 increases microtubule stability and regulates dendritic arborization. J. Cell Sci. 32, 1043\u20131055 (2014).","journal-title":"J. Cell Sci."},{"key":"e_1_3_3_39_2","doi-asserted-by":"crossref","first-page":"20449","DOI":"10.1073\/pnas.1309958110","article-title":"Mechanism for the catastrophe-promoting activity of the microtubule destabilizer Op18\/stathmin","volume":"110","author":"Gupta K. K.","year":"2013","unstructured":"K. K. Gupta, C. Li, A. Duan, E. O. Alberico, O. V. Kim, M. S. Alber, H. V. Goodson, Mechanism for the catastrophe-promoting activity of the microtubule destabilizer Op18\/stathmin. PNAS. 110, 20449\u201320454 (2013).","journal-title":"PNAS."},{"key":"e_1_3_3_40_2","doi-asserted-by":"crossref","first-page":"16146","DOI":"10.1074\/jbc.M010637200","article-title":"Stathmin family proteins display specific molecular and tubulin binding properties","volume":"276","author":"Charbaut E.","year":"2001","unstructured":"E. Charbaut, P. A. Curmi, S. Ozon, S. Lachkar, V. Redeker, A. Sobel, Stathmin family proteins display specific molecular and tubulin binding properties. J. Biol. Chem. 276, 16146\u201316154 (2001).","journal-title":"J. Biol. Chem."},{"key":"e_1_3_3_41_2","doi-asserted-by":"crossref","first-page":"1447","DOI":"10.1242\/jcs.001461","article-title":"The microtubule destabilizer stathmin mediates the development of dendritic arbors in neuronal cells","volume":"120","author":"Ohkawa N.","year":"2007","unstructured":"N. Ohkawa, K. Fujitani, E. Tokunaga, S. Furuya, K. Inokuchi, The microtubule destabilizer stathmin mediates the development of dendritic arbors in neuronal cells. J. Cell Sci. 120, 1447\u20131456 (2007).","journal-title":"J. Cell Sci."},{"key":"e_1_3_3_42_2","doi-asserted-by":"crossref","first-page":"7387","DOI":"10.1523\/JNEUROSCI.1942-08.2008","article-title":"SCLIP is crucial for the formation and development of the Purkinje cell dendritic arbor","volume":"28","author":"Poulain F. E.","year":"2008","unstructured":"F. E. Poulain, S. Chauvin, R. Wehrl\u00e9, M. Desclaux, J. Mallet, G. Vodjdani, I. Dusart, A. Sobel, SCLIP is crucial for the formation and development of the Purkinje cell dendritic arbor. J. Neurosci. 28, 7387\u20137398 (2008).","journal-title":"J. Neurosci."},{"key":"e_1_3_3_43_2","doi-asserted-by":"crossref","first-page":"469","DOI":"10.1016\/S0002-9440(10)64866-3","article-title":"Stathmin-deficient mice develop an age-dependent axonopathy of the central and peripheral nervous systems","volume":"160","author":"Liedtke W.","year":"2002","unstructured":"W. Liedtke, E. E. Leman, R. E. W. Fyffe, C. S. Raine, U. K. Schubart, Stathmin-deficient mice develop an age-dependent axonopathy of the central and peripheral nervous systems. Am. J. Pathol. 160, 469\u2013480 (2002).","journal-title":"Am. J. Pathol."},{"key":"e_1_3_3_44_2","doi-asserted-by":"crossref","first-page":"180","DOI":"10.1038\/s41593-018-0293-z","article-title":"Premature polyadenylation-mediated loss of stathmin-2 is a hallmark of TDP-43-dependent neurodegeneration","volume":"22","author":"Melamed Z.","year":"2019","unstructured":"Z. Melamed, J. L\u00f3pez-Erauskin, M. W. Baughn, O. Zhang, K. Drenner, Y. Sun, F. Freyermuth, M. A. McMahon, M. S. Beccari, J. W. Artates, T. Ohkubo, M. Rodriguez, N. Lin, D. Wu, C. F. Bennett, F. Rigo, S. Da Cruz, J. Ravits, C. Lagier-Tourenne, D. W. Cleveland, Premature polyadenylation-mediated loss of stathmin-2 is a hallmark of TDP-43-dependent neurodegeneration. Nat. Neurosci. 22, 180\u2013190 (2019).","journal-title":"Nat. Neurosci."},{"key":"e_1_3_3_45_2","doi-asserted-by":"crossref","first-page":"5677","DOI":"10.1172\/JCI142854","article-title":"Stathmin-2: Adding another piece to the puzzle of TDP-43 proteinopathies and neurodegeneration","volume":"130","author":"Glass J. D.","year":"2020","unstructured":"J. D. Glass, Stathmin-2: Adding another piece to the puzzle of TDP-43 proteinopathies and neurodegeneration. J. Clin. Investig. 130, 5677\u20135680 (2020).","journal-title":"J. Clin. Investig."},{"key":"e_1_3_3_46_2","doi-asserted-by":"crossref","first-page":"4673","DOI":"10.1038\/s41467-020-18483-9","article-title":"Haploinsufficiency of RREB1 causes a Noonan-like RASopathy via epigenetic reprogramming of RAS-MAPK pathway genes","volume":"11","author":"Kent O. A.","year":"2020","unstructured":"O. A. Kent, M. Saha, E. Coyaud, H. E. Burston, N. Law, K. Dadson, S. Chen, E. M. Laurent, J. St-Germain, R. X. Sun, Y. Matsumoto, J. Cowen, A. Montgomery-Song, K. R. Brown, C. Ishak, J. La Rose, D. D. De Carvalho, H. H. He, B. Raught, F. Billia, P. Kannu, R. Rottapel, Haploinsufficiency of RREB1 causes a Noonan-like RASopathy via epigenetic reprogramming of RAS-MAPK pathway genes. Nat. Commun. 11, 4673 (2020).","journal-title":"Nat. Commun."},{"key":"e_1_3_3_47_2","doi-asserted-by":"crossref","first-page":"691","DOI":"10.4161\/auto.27749","article-title":"Seeing is believing","volume":"10","author":"Lin F.","year":"2014","unstructured":"F. Lin, Z. V. Wang, J. A. Hill, Seeing is believing. Autophagy 10, 691\u2013693 (2014).","journal-title":"Autophagy"},{"key":"e_1_3_3_48_2","doi-asserted-by":"crossref","first-page":"402","DOI":"10.1006\/meth.2001.1262","article-title":"Analysis of relative gene expression data using real-time quantitative PCR and the 2\u2212\u0394\u0394CT method","volume":"25","author":"Livak K. J.","year":"2001","unstructured":"K. J. Livak, T. D. Schmittgen, Analysis of relative gene expression data using real-time quantitative PCR and the 2\u2212\u0394\u0394CT method. Methods 25, 402\u2013408 (2001).","journal-title":"Methods"},{"key":"e_1_3_3_49_2","doi-asserted-by":"crossref","first-page":"100358","DOI":"10.1016\/j.xpro.2021.100358","article-title":"An optimized protocol for rapid, sensitive and robust on-bead ChIP-seq from primary cells","volume":"2","author":"Texari L.","year":"2021","unstructured":"L. Texari, N. J. Spann, T. D. Troutman, M. Sakai, J. S. Seidman, S. Heinz, An optimized protocol for rapid, sensitive and robust on-bead ChIP-seq from primary cells. STAR Protoc. 2, 100358 (2021).","journal-title":"STAR Protoc."},{"key":"e_1_3_3_50_2","doi-asserted-by":"crossref","first-page":"i884","DOI":"10.1093\/bioinformatics\/bty560","article-title":"fastp: An ultra-fast all-in-one FASTQ preprocessor","volume":"34","author":"Chen S.","year":"2018","unstructured":"S. Chen, Y. Zhou, Y. Chen, J. Gu, fastp: An ultra-fast all-in-one FASTQ preprocessor. Bioinformatics 34, i884\u2013i890 (2018).","journal-title":"Bioinformatics"},{"key":"e_1_3_3_51_2","doi-asserted-by":"crossref","first-page":"357","DOI":"10.1038\/nmeth.1923","article-title":"Fast gapped-read alignment with Bowtie 2","volume":"9","author":"Langmead B.","year":"2012","unstructured":"B. Langmead, S. L. Salzberg, Fast gapped-read alignment with Bowtie 2. Nat. Methods 9, 357\u2013359 (2012).","journal-title":"Nat. Methods"},{"key":"e_1_3_3_52_2","doi-asserted-by":"crossref","first-page":"923","DOI":"10.1093\/bioinformatics\/btt656","article-title":"featureCounts: An efficient general purpose program for assigning sequence reads to genomic features","volume":"30","author":"Liao Y.","year":"2014","unstructured":"Y. Liao, G. K. Smyth, W. Shi, featureCounts: An efficient general purpose program for assigning sequence reads to genomic features. Bioinformatics 30, 923\u2013930 (2014).","journal-title":"Bioinformatics"},{"key":"e_1_3_3_53_2","doi-asserted-by":"crossref","first-page":"550","DOI":"10.1186\/s13059-014-0550-8","article-title":"Moderated estimation of fold change and dispersion for RNA-seq data with DESeq2","volume":"15","author":"Love M. I.","year":"2014","unstructured":"M. I. Love, W. Huber, S. Anders, Moderated estimation of fold change and dispersion for RNA-seq data with DESeq2. Genome Biol. 15, 550 (2014).","journal-title":"Genome Biol."},{"key":"e_1_3_3_54_2","doi-asserted-by":"crossref","first-page":"2628","DOI":"10.1093\/bioinformatics\/btz931","article-title":"ShinyGO: A graphical gene-set enrichment tool for animals and plants","volume":"36","author":"Ge S. X.","year":"2020","unstructured":"S. X. Ge, D. Jung, R. Yao, ShinyGO: A graphical gene-set enrichment tool for animals and plants. Bioinformatics 36, 2628\u20132629 (2020).","journal-title":"Bioinformatics"},{"key":"e_1_3_3_55_2","doi-asserted-by":"crossref","first-page":"2032","DOI":"10.1093\/bioinformatics\/btv098","article-title":"Sambamba: Fast processing of NGS alignment formats","volume":"31","author":"Tarasov A.","year":"2015","unstructured":"A. Tarasov, A. J. Vilella, E. Cuppen, I. J. Nijman, P. Prins, Sambamba: Fast processing of NGS alignment formats. Bioinformatics 31, 2032\u20132034 (2015).","journal-title":"Bioinformatics"},{"key":"e_1_3_3_56_2","doi-asserted-by":"crossref","first-page":"R137","DOI":"10.1186\/gb-2008-9-9-r137","article-title":"Model-based analysis of ChIP-seq (MACS)","volume":"9","author":"Zhang Y.","year":"2008","unstructured":"Y. Zhang, T. Liu, C. A. Meyer, J. Eeckhoute, D. S. Johnson, B. E. Bernstein, C. Nusbaum, R. M. Myers, M. Brown, W. Li, X. S. Liu, Model-based analysis of ChIP-seq (MACS). Genome Biol. 9, R137 (2008).","journal-title":"Genome Biol."},{"key":"e_1_3_3_57_2","doi-asserted-by":"crossref","first-page":"576","DOI":"10.1016\/j.molcel.2010.05.004","article-title":"Simple combinations of lineage-determining transcription factors prime cis-regulatory elements required for macrophage and B cell identities","volume":"38","author":"Heinz S.","year":"2010","unstructured":"S. Heinz, C. Benner, N. Spann, E. Bertolino, Y. C. Lin, P. Laslo, J. X. Cheng, C. Murre, H. Singh, C. K. Glass, Simple combinations of lineage-determining transcription factors prime cis-regulatory elements required for macrophage and B cell identities. Mol. Cell 38, 576\u2013589 (2010).","journal-title":"Mol. Cell"},{"key":"e_1_3_3_58_2","doi-asserted-by":"crossref","first-page":"644","DOI":"10.3892\/ijo.2017.4047","article-title":"Autophagy plays an important role in stemness mediation and the novel dual function of EIG121 in both autophagy and stemness regulation of endometrial carcinoma JEC cells","volume":"51","author":"Ran X.","year":"2017","unstructured":"X. Ran, P. Zhou, K. Zhang, Autophagy plays an important role in stemness mediation and the novel dual function of EIG121 in both autophagy and stemness regulation of endometrial carcinoma JEC cells. Int. J. Oncol. 51, 644\u2013656 (2017).","journal-title":"Int. J. Oncol."},{"key":"e_1_3_3_59_2","doi-asserted-by":"crossref","first-page":"e32","DOI":"10.1038\/cddis.2010.9","article-title":"The novel estrogen-induced gene EIG121 regulates autophagy and promotes cell survival under stress","volume":"1","author":"Deng L.","year":"2010","unstructured":"L. Deng, J. Feng, R. R. Broaddus, The novel estrogen-induced gene EIG121 regulates autophagy and promotes cell survival under stress. Cell Death Dis. 1, e32\u2013e32 (2010).","journal-title":"Cell Death Dis."},{"key":"e_1_3_3_60_2","doi-asserted-by":"crossref","first-page":"161","DOI":"10.1096\/fj.201901626R","article-title":"Fas-apoptotic inhibitory molecule 2 localizes to the lysosome and facilitates autophagosome-lysosome fusion through the LC3 interaction region motif\u2013dependent interaction with LC3","volume":"34","author":"Hong C. J.","year":"2020","unstructured":"C. J. Hong, J. Yeon, B. K. Yeo, H. Woo, H. An, W. Heo, K. Kim, S. Yu, Fas-apoptotic inhibitory molecule 2 localizes to the lysosome and facilitates autophagosome-lysosome fusion through the LC3 interaction region motif\u2013dependent interaction with LC3. FASEB J. 34, 161\u2013179 (2020).","journal-title":"FASEB J."},{"key":"e_1_3_3_61_2","doi-asserted-by":"crossref","first-page":"6997","DOI":"10.1038\/s41598-018-25485-7","article-title":"CPT1C promotes human mesenchymal stem cells survival under glucose deprivation through the modulation of autophagy","volume":"8","author":"Roa-Mansergas X.","year":"2018","unstructured":"X. Roa-Mansergas, R. Fad\u00f3, M. Atari, J. F. Mir, H. Muley, D. Serra, N. Casals, CPT1C promotes human mesenchymal stem cells survival under glucose deprivation through the modulation of autophagy. Sci. Rep. 8, 6997 (2018).","journal-title":"Sci. Rep."},{"key":"e_1_3_3_62_2","doi-asserted-by":"crossref","first-page":"229","DOI":"10.1042\/BJ20081973","article-title":"TVP23interacts genetically with the yeast SNAREVTI1and functions in retrograde transport from the early endosome to the late Golgi","volume":"419","author":"Stein I. S.","year":"2009","unstructured":"I. S. Stein, A. Gottfried, J. Zimmermann, G. Fischer von Mollard, TVP23interacts genetically with the yeast SNAREVTI1and functions in retrograde transport from the early endosome to the late Golgi. Biochem. J. 419, 229\u2013236 (2009).","journal-title":"Biochem. J."},{"key":"e_1_3_3_63_2","doi-asserted-by":"crossref","first-page":"1574","DOI":"10.1080\/15548627.2018.1463120","article-title":"TRIM37 deficiency induces autophagy through deregulating the MTORC1-TFEB axis","volume":"14","author":"Wang W.","year":"2018","unstructured":"W. Wang, Z. Xia, J.-C. Farr\u00e9, S. Subramani, TRIM37 deficiency induces autophagy through deregulating the MTORC1-TFEB axis. Autophagy 14, 1574\u20131585 (2018).","journal-title":"Autophagy"},{"key":"e_1_3_3_64_2","doi-asserted-by":"crossref","first-page":"140","DOI":"10.1016\/j.mcn.2012.11.008","article-title":"The role of autophagy in Nmnat-mediated protection against hypoxia-induced dendrite degeneration","volume":"52","author":"Wen Y.","year":"2013","unstructured":"Y. Wen, R. G. Zhai, M. D. Kim, The role of autophagy in Nmnat-mediated protection against hypoxia-induced dendrite degeneration. Mol. Cell. Neurosci. 52, 140\u2013151 (2013).","journal-title":"Mol. Cell. Neurosci."},{"key":"e_1_3_3_65_2","doi-asserted-by":"crossref","first-page":"171","DOI":"10.1016\/j.devcel.2016.06.012","article-title":"KIF1A\/UNC-104 transports ATG-9 to regulate neurodevelopment and autophagy at synapses","volume":"38","author":"Stavoe A. K. H.","year":"2016","unstructured":"A. K. H. Stavoe, S. E. Hill, D. H. Hall, D. A. Col\u00f3n-Ramos, KIF1A\/UNC-104 transports ATG-9 to regulate neurodevelopment and autophagy at synapses. Dev. Cell 38, 171\u2013185 (2016).","journal-title":"Dev. Cell"},{"key":"e_1_3_3_66_2","doi-asserted-by":"crossref","first-page":"573372","DOI":"10.3389\/fphys.2020.573372","article-title":"Natural killer lytic-associated molecule (NKLAM): An E3 ubiquitin ligase with an integral role in innate immunity","volume":"11","author":"Lawrence D. W.","year":"2020","unstructured":"D. W. Lawrence, P. A. Willard, A. M. Cochran, E. C. Matchett, J. Kornbluth, Natural killer lytic-associated molecule (NKLAM): An E3 ubiquitin ligase with an integral role in innate immunity. Front. Physiol. 11, 573372 (2020).","journal-title":"Front. Physiol."},{"key":"e_1_3_3_67_2","doi-asserted-by":"crossref","first-page":"1154","DOI":"10.1128\/EC.00115-12","article-title":"The mitochondrial Dnm1-Like fission component is required for lga2 -induced mitophagy but dispensable for starvation-induced mitophagy in ustilago maydis","volume":"11","author":"Nieto-Jacobo F.","year":"2012","unstructured":"F. Nieto-Jacobo, D. Pasch, C. W. Basse, The mitochondrial Dnm1-Like fission component is required for lga2 -induced mitophagy but dispensable for starvation-induced mitophagy in ustilago maydis. Eukaryot. Cell 11, 1154\u20131166 (2012).","journal-title":"Eukaryot. Cell"},{"key":"e_1_3_3_68_2","doi-asserted-by":"crossref","first-page":"689","DOI":"10.1080\/15548627.2016.1151580","article-title":"Mitophagy receptor FUNDC1 regulates mitochondrial dynamics and mitophagy","volume":"12","author":"Chen M.","year":"2016","unstructured":"M. Chen, Z. Chen, Y. Wang, Z. Tan, C. Zhu, Y. Li, Z. Han, L. Chen, R. Gao, L. Liu, Q. Chen, Mitophagy receptor FUNDC1 regulates mitochondrial dynamics and mitophagy. Autophagy 12, 689\u2013702 (2016).","journal-title":"Autophagy"},{"key":"e_1_3_3_69_2","doi-asserted-by":"crossref","first-page":"1470","DOI":"10.1080\/15548627.2019.1609864","article-title":"The MTORC1-mediated autophagy is regulated by the FBXW7-SHOC2-RPTOR axis","volume":"15","author":"Xie C.-M.","year":"2019","unstructured":"C.-M. Xie, Y. Sun, The MTORC1-mediated autophagy is regulated by the FBXW7-SHOC2-RPTOR axis. Autophagy 15, 1470\u20131472 (2019).","journal-title":"Autophagy"},{"key":"e_1_3_3_70_2","doi-asserted-by":"crossref","first-page":"3259","DOI":"10.1111\/odi.14325","article-title":"FBXW7 affects autophagy through MCL1 in oral squamous cell carcinoma","volume":"29","author":"Sun Y.","year":"2022","unstructured":"Y. Sun, W. Nie, B. Qiu, Q. Yang, H. Zhao, FBXW7 affects autophagy through MCL1 in oral squamous cell carcinoma. Oral Dis. 29, 3259\u20133267 (2022).","journal-title":"Oral Dis."},{"key":"e_1_3_3_71_2","doi-asserted-by":"crossref","first-page":"2168","DOI":"10.1128\/MCB.00170-16","article-title":"Novel Grb14-mediated cross talk between insulin and p62\/Nrf2 pathways regulates liver lipogenesis and selective insulin resistance","volume":"36","author":"Popineau L.","year":"2016","unstructured":"L. Popineau, L. Morzyglod, N. Carr\u00e9, M. Ca\u00fczac, P. Bossard, C. Prip-Buus, V. Lenoir, B. Ragazzon, V. Fauveau, L. Robert, S. Guilmeau, C. Postic, M. Komatsu, F. Canonne-Hergaux, H. Guillou, A.-F. Burnol, Novel Grb14-mediated cross talk between insulin and p62\/Nrf2 pathways regulates liver lipogenesis and selective insulin resistance. Mol. Cell. Biol. 36, 2168\u20132181 (2016).","journal-title":"Mol. Cell. Biol."},{"key":"e_1_3_3_72_2","doi-asserted-by":"crossref","first-page":"3828","DOI":"10.1038\/ncomms4828","article-title":"Mutation in VPS35 associated with Parkinson\u2019s disease impairs WASH complex association and inhibits autophagy","volume":"5","author":"Zavodszky E.","year":"2014","unstructured":"E. Zavodszky, M. N. J. Seaman, K. Moreau, M. Jimenez-Sanchez, S. Y. Breusegem, M. E. Harbour, D. C. Rubinsztein, Mutation in VPS35 associated with Parkinson\u2019s disease impairs WASH complex association and inhibits autophagy. Nat. Commun. 5, 3828 (2014).","journal-title":"Nat. Commun."},{"key":"e_1_3_3_73_2","doi-asserted-by":"crossref","first-page":"245","DOI":"10.1136\/jmedgenet-2019-106213","article-title":"Biallelic VPS35L pathogenic variants cause 3C\/Ritscher-Schinzel-like syndrome through dysfunction of retriever complex","volume":"57","author":"Kato K.","year":"2020","unstructured":"K. Kato, Y. Oka, H. Muramatsu, F. F. Vasilev, T. Otomo, H. Oishi, Y. Kawano, H. Kidokoro, Y. Nakazawa, T. Ogi, Y. Takahashi, S. Saitoh, Biallelic VPS35L pathogenic variants cause 3C\/Ritscher-Schinzel-like syndrome through dysfunction of retriever complex. J. Med. Genet. 57, 245\u2013253 (2020).","journal-title":"J. Med. Genet."},{"key":"e_1_3_3_74_2","doi-asserted-by":"crossref","first-page":"25652","DOI":"10.18632\/oncotarget.8357","article-title":"Tumor suppressor Spred2 interaction with LC3 promotes autophagosome maturation and induces autophagy-dependent cell death","volume":"7","author":"Jiang K.","year":"2016","unstructured":"K. Jiang, M. Liu, G. Lin, B. Mao, W. Cheng, H. Liu, J. Gal, H. Zhu, Z. Yuan, W. Deng, Q. Liu, P. Gong, X. Bi, S. Meng, Tumor suppressor Spred2 interaction with LC3 promotes autophagosome maturation and induces autophagy-dependent cell death. Oncotarget 7, 25652\u201325667 (2016).","journal-title":"Oncotarget"},{"key":"e_1_3_3_75_2","doi-asserted-by":"crossref","first-page":"13","DOI":"10.1016\/j.yjmcc.2019.01.023","article-title":"SPRED2 deficiency elicits cardiac arrhythmias and premature death via impaired autophagy","volume":"129","author":"Ullrich M.","year":"2019","unstructured":"M. Ullrich, B. A\u00dfmus, A. M. Augustin, H. H\u00e4bich, M. Abe\u00dfer, J. Martin Machado, F. Werner, R. Erkens, A.-P. Arias-Loza, S. Umbenhauer, H. Wagner, P. M. Benz, A. Unger, W. A. Linke, S. Frantz, H. A. Baba, M. Kuhn, K. Schuh, SPRED2 deficiency elicits cardiac arrhythmias and premature death via impaired autophagy. J. Mol. Cell. Cardiol. 129, 13\u201326 (2019).","journal-title":"J. Mol. Cell. Cardiol."},{"key":"e_1_3_3_76_2","first-page":"963689720962460","article-title":"miR-19 promotes cell proliferation, invasion, migration, and emt by inhibiting SPRED2-mediated autophagy in osteosarcoma cells","volume":"29","author":"Xie C.","year":"2020","unstructured":"C. Xie, S. Liu, B. Wu, Y. Zhao, B. Chen, J. Guo, S. Qiu, Y. Cao, miR-19 promotes cell proliferation, invasion, migration, and emt by inhibiting SPRED2-mediated autophagy in osteosarcoma cells. Cell Transplant. 29, 963689720962460 (2020).","journal-title":"Cell Transplant."},{"key":"e_1_3_3_77_2","doi-asserted-by":"crossref","first-page":"1093","DOI":"10.1016\/j.bbrc.2019.04.134","article-title":"p62\/mTOR\/LXR\u03b1 pathway inhibits cholesterol efflux mediated by ABCA1 and ABCG1 during autophagy blockage","volume":"514","author":"Liang X.","year":"2019","unstructured":"X. Liang, C. Wang, Y. Sun, W. Song, J. Lin, J. Li, X. Guan, p62\/mTOR\/LXR\u03b1 pathway inhibits cholesterol efflux mediated by ABCA1 and ABCG1 during autophagy blockage. Biochem. Biophys. Res. Commun. 514, 1093\u20131100 (2019).","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"e_1_3_3_78_2","doi-asserted-by":"crossref","first-page":"483","DOI":"10.1038\/s41556-022-00869-0","article-title":"Aggresome assembly at the centrosome is driven by CP110\u2013CEP97\u2013CEP290 and centriolar satellites","volume":"24","author":"Prosser S. L.","year":"2022","unstructured":"S. L. Prosser, J. Tkach, L. Gheiratmand, J. Kim, B. Raught, C. G. Morrison, L. Pelletier, Aggresome assembly at the centrosome is driven by CP110\u2013CEP97\u2013CEP290 and centriolar satellites. Nat. Cell Biol. 24, 483\u2013496 (2022).","journal-title":"Nat. Cell Biol."},{"key":"e_1_3_3_79_2","doi-asserted-by":"crossref","first-page":"2199","DOI":"10.1016\/S0024-3205(03)00092-4","article-title":"Increased intracellular calcium activates serum and glucocorticoid-inducible kinase 1 (SGK1) through a calmodulin-calcium calmodulin dependent kinase kinase pathway in Chinese hamster ovary cells","volume":"72","author":"Imai S.","year":"2003","unstructured":"S. Imai, N. Okayama, M. Shimizu, M. Itoh, Increased intracellular calcium activates serum and glucocorticoid-inducible kinase 1 (SGK1) through a calmodulin-calcium calmodulin dependent kinase kinase pathway in Chinese hamster ovary cells. Life Sci. 72, 2199\u20132209 (2003).","journal-title":"Life Sci."},{"key":"e_1_3_3_80_2","doi-asserted-by":"crossref","first-page":"251","DOI":"10.1182\/blood-2011-06-359976","article-title":"The serum- and glucocorticoid-inducible kinase 1 (SGK1) influences platelet calcium signaling and function by regulation of Orai1 expression in megakaryocytes","volume":"119","author":"Borst O.","year":"2012","unstructured":"O. Borst, E.-M. Schmidt, P. M\u00fcnzer, T. Sch\u00f6nberger, S. T. Towhid, M. Elvers, C. Leibrock, E. Schmid, A. Eylenstein, D. Kuhl, A. E. May, M. Gawaz, F. Lang, The serum- and glucocorticoid-inducible kinase 1 (SGK1) influences platelet calcium signaling and function by regulation of Orai1 expression in megakaryocytes. Blood 119, 251\u2013261 (2012).","journal-title":"Blood"},{"key":"e_1_3_3_81_2","doi-asserted-by":"crossref","first-page":"1855","DOI":"10.1042\/BST20210538","article-title":"Ion channels as convergence points in the pathology of pulmonary arterial hypertension","volume":"49","author":"Jouen-Tachoire T. R. H.","year":"2021","unstructured":"T. R. H. Jouen-Tachoire, S. J. Tucker, P. Tammaro, Ion channels as convergence points in the pathology of pulmonary arterial hypertension. Biochem. Soc. Trans. 49, 1855\u20131865 (2021).","journal-title":"Biochem. Soc. Trans."},{"key":"e_1_3_3_82_2","doi-asserted-by":"crossref","first-page":"825","DOI":"10.1016\/j.bbrc.2009.01.177","article-title":"Membrane targeting of the EF-hand containing calcium-sensing proteins CaBP7 and CaBP8","volume":"380","author":"McCue H. V.","year":"2009","unstructured":"H. V. McCue, R. D. Burgoyne, L. P. Haynes, Membrane targeting of the EF-hand containing calcium-sensing proteins CaBP7 and CaBP8. Biochem. Biophys. Res. Commun. 380, 825\u2013831 (2009).","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"e_1_3_3_83_2","doi-asserted-by":"crossref","first-page":"1247","DOI":"10.1074\/jbc.275.2.1247","article-title":"Five members of a novel Ca2+\u2212binding protein (CABP) subfamily with similarity to calmodulin","volume":"275","author":"Haeseleer F.","year":"2000","unstructured":"F. Haeseleer, I. Sokal, C. L. M. J. Verlinde, H. Erdjument-Bromage, P. Tempst, A. N. Pronin, J. L. Benovic, R. N. Fariss, K. Palczewski, Five members of a novel Ca2+\u2212binding protein (CABP) subfamily with similarity to calmodulin. J. Biol. Chem. 275, 1247\u20131260 (2000).","journal-title":"J. Biol. Chem."},{"key":"e_1_3_3_84_2","doi-asserted-by":"crossref","first-page":"24303","DOI":"10.1016\/S0021-9258(20)80526-2","article-title":"Structure and function of C-CAM1. The first immunoglobulin domain is required for intercellular adhesion","volume":"268","author":"Cheung P. H.","year":"1993","unstructured":"P. H. Cheung, W. Luo, Y. Qiu, X. Zhang, K. Earley, P. Millirons, S. H. Lin, Structure and function of C-CAM1. The first immunoglobulin domain is required for intercellular adhesion. J. Biol. Chem. 268, 24303\u201324310 (1993).","journal-title":"J. Biol. Chem."},{"key":"e_1_3_3_85_2","doi-asserted-by":"crossref","first-page":"1697","DOI":"10.1038\/sj.onc.1200999","article-title":"Suppression of tumorigenicity of breast cancer cells by an epithelial cell adhesion molecule (C-CAM1): The adhesion and growth suppression are mediated by different domains","volume":"14","author":"Luo W.","year":"1997","unstructured":"W. Luo, C. G. Wood, K. Earley, M.-C. Hung, S.-H. Lin, Suppression of tumorigenicity of breast cancer cells by an epithelial cell adhesion molecule (C-CAM1): The adhesion and growth suppression are mediated by different domains. Oncogene 14, 1697\u20131704 (1997).","journal-title":"Oncogene"},{"key":"e_1_3_3_86_2","doi-asserted-by":"crossref","first-page":"1387","DOI":"10.1002\/jnr.22315","article-title":"Analysis of the expression and function of BRINP family genes during neuronal differentiation in mouse embryonic stem cell-derived neural stem cells","volume":"88","author":"Terashima M.","year":"2010","unstructured":"M. Terashima, M. Kobayashi, M. Motomiya, N. Inoue, T. Yoshida, H. Okano, N. Iwasaki, A. Minami, I. Matsuoka, Analysis of the expression and function of BRINP family genes during neuronal differentiation in mouse embryonic stem cell-derived neural stem cells. J. Neurosci. Res. 88, 1387\u20131393 (2010).","journal-title":"J. Neurosci. Res."},{"key":"e_1_3_3_87_2","doi-asserted-by":"crossref","first-page":"22","DOI":"10.1186\/s13229-016-0079-7","article-title":"Brinp1\u2212\/\u2212 mice exhibit autism-like behaviour, altered memory, hyperactivity and increased parvalbumin-positive cortical interneuron density","volume":"7","author":"Berkowicz S. R.","year":"2016","unstructured":"S. R. Berkowicz, T. J. Featherby, Z. Qu, A. Giousoh, N. A. Borg, J. I. Heng, J. C. Whisstock, P. I. Bird, Brinp1\u2212\/\u2212 mice exhibit autism-like behaviour, altered memory, hyperactivity and increased parvalbumin-positive cortical interneuron density. Mol. Autism. 7, 22 (2016).","journal-title":"Mol. Autism."},{"key":"e_1_3_3_88_2","doi-asserted-by":"crossref","first-page":"103420","DOI":"10.1016\/j.mcn.2019.103420","article-title":"Deficits in developmental neurogenesis and dendritic spine maturation in mice lacking the serine protease inhibitor neuroserpin","volume":"102","author":"Hermann M.","year":"2020","unstructured":"M. Hermann, R. Reumann, K. Schostak, D. Kement, M. Gelderblom, C. Bernreuther, R. Frischknecht, A. Schipanski, S. Marik, S. Krasemann, D. Sepulveda-Falla, M. Schweizer, T. Magnus, M. Glatzel, G. Galliciotti, Deficits in developmental neurogenesis and dendritic spine maturation in mice lacking the serine protease inhibitor neuroserpin. Mol. Cell. Neurosci. 102, 103420 (2020).","journal-title":"Mol. Cell. Neurosci."},{"key":"e_1_3_3_89_2","doi-asserted-by":"crossref","first-page":"650","DOI":"10.1101\/lm.045864.117","article-title":"The serine protease inhibitor neuroserpin is required for normal synaptic plasticity and regulates learning and social behavior","volume":"24","author":"Reumann R.","year":"2017","unstructured":"R. Reumann, R. Vierk, L. Zhou, F. Gries, V. Kraus, J. Mienert, E. Romswinkel, F. Morellini, I. Ferrer, C. Nicolini, M. Fahnestock, G. Rune, M. Glatzel, G. Galliciotti, The serine protease inhibitor neuroserpin is required for normal synaptic plasticity and regulates learning and social behavior. Learn. Mem. 24, 650\u2013659 (2017).","journal-title":"Learn. Mem."},{"key":"e_1_3_3_90_2","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1016\/j.gep.2012.08.001","article-title":"Expression of the tetraspanin family members Tspan3, Tspan4, Tspan5 and Tspan7 during Xenopus laevis embryonic development","volume":"13","author":"Kashef J.","year":"2013","unstructured":"J. Kashef, T. Diana, M. Oelgeschl\u00e4ger, I. Nazarenko, Expression of the tetraspanin family members Tspan3, Tspan4, Tspan5 and Tspan7 during Xenopus laevis embryonic development. Gene Expr. Patterns 13, 1\u201311 (2013).","journal-title":"Gene Expr. Patterns"},{"key":"e_1_3_3_91_2","doi-asserted-by":"crossref","first-page":"15182","DOI":"10.1074\/jbc.M600265200","article-title":"Calcyon, a novel partner of clathrin light chain, stimulates clathrin-mediated endocytosis","volume":"281","author":"Xiao J.","year":"2006","unstructured":"J. Xiao, R. Dai, L. Negyessy, C. Bergson, Calcyon, a novel partner of clathrin light chain, stimulates clathrin-mediated endocytosis. J. Biol. Chem. 281, 15182\u201315193 (2006).","journal-title":"J. Biol. Chem."},{"key":"e_1_3_3_92_2","doi-asserted-by":"crossref","first-page":"1547","DOI":"10.1097\/WNR.0b013e3282f03f51","article-title":"Intracellular dynamics of calcyon, a neuron-specific vesicular protein","volume":"18","author":"Kruusm\u00e4gi M.","year":"2007","unstructured":"M. Kruusm\u00e4gi, S. Zelenin, H. Brismar, L. Scott, Intracellular dynamics of calcyon, a neuron-specific vesicular protein. Neuroreport 18, 1547\u20131551 (2007).","journal-title":"Neuroreport"},{"key":"e_1_3_3_93_2","doi-asserted-by":"crossref","first-page":"41","DOI":"10.1186\/s13041-019-0464-1","article-title":"SGIP1\u03b1 functions as a selective endocytic adaptor for the internalization of synaptotagmin 1 at synapses","volume":"12","author":"Lee S.-E.","year":"2019","unstructured":"S.-E. Lee, S. Jeong, U. Lee, S. Chang, SGIP1\u03b1 functions as a selective endocytic adaptor for the internalization of synaptotagmin 1 at synapses. Mol. Brain 12, 41 (2019).","journal-title":"Mol. Brain"},{"key":"e_1_3_3_94_2","doi-asserted-by":"crossref","first-page":"26481","DOI":"10.1074\/jbc.M703815200","article-title":"SGIP1\u03b1 is an endocytic protein that directly interacts with phospholipids and Eps15","volume":"282","author":"Uezu A.","year":"2007","unstructured":"A. Uezu, A. Horiuchi, K. Kanda, N. Kikuchi, K. Umeda, K. Tsujita, S. Suetsugu, N. Araki, H. Yamamoto, T. Takenawa, H. Nakanishi, SGIP1\u03b1 is an endocytic protein that directly interacts with phospholipids and Eps15. J. Biol. Chem. 282, 26481\u201326489 (2007).","journal-title":"J. Biol. Chem."},{"key":"e_1_3_3_95_2","doi-asserted-by":"crossref","first-page":"e1001670","DOI":"10.1371\/journal.pbio.1001670","article-title":"NECAP 1 regulates AP-2 interactions to control vesicle size, number, and cargo during clathrin-mediated endocytosis","volume":"11","author":"Ritter B.","year":"2013","unstructured":"B. Ritter, S. Murphy, H. Dokainish, M. Girard, M. V. Gudheti, G. Kozlov, M. Halin, J. Philie, E. M. Jorgensen, K. Gehring, P. S. McPherson, NECAP 1 regulates AP-2 interactions to control vesicle size, number, and cargo during clathrin-mediated endocytosis. PLoS Biol. 11, e1001670 (2013).","journal-title":"PLoS Biol."},{"key":"e_1_3_3_96_2","doi-asserted-by":"crossref","first-page":"109","DOI":"10.1016\/S0009-3084(99)00023-7","article-title":"Diacylglycerol kinase in the central nervous system\u2014Molecular heterogeneity and gene expression","volume":"98","author":"Goto K.","year":"1999","unstructured":"K. Goto, H. Kondo, Diacylglycerol kinase in the central nervous system\u2014Molecular heterogeneity and gene expression. Chem. Phys. Lipids 98, 109\u2013117 (1999).","journal-title":"Chem. Phys. Lipids"},{"key":"e_1_3_3_97_2","doi-asserted-by":"crossref","first-page":"113","DOI":"10.1042\/BJ20101357","article-title":"The endoplasmic reticulum sulfhydryl oxidase Ero1\u03b2 drives efficient oxidative protein folding with loose regulation","volume":"434","author":"Wang L.","year":"2011","unstructured":"L. Wang, L. Zhu, C. C. Wang, The endoplasmic reticulum sulfhydryl oxidase Ero1\u03b2 drives efficient oxidative protein folding with loose regulation. Biochem. J. 434, 113\u2013121 (2011).","journal-title":"Biochem. J."},{"key":"e_1_3_3_98_2","doi-asserted-by":"crossref","first-page":"23685","DOI":"10.1074\/jbc.M003061200","article-title":"Endoplasmic reticulum oxidoreductin 1-L\u03b2 (ERO1-L\u03b2), a human gene induced in the course of the unfolded protein response","volume":"275","author":"Pagani M.","year":"2000","unstructured":"M. Pagani, M. Fabbri, C. Benedetti, A. Fassio, S. Pilati, N. J. Bulleid, A. Cabibbo, R. Sitia, Endoplasmic reticulum oxidoreductin 1-L\u03b2 (ERO1-L\u03b2), a human gene induced in the course of the unfolded protein response. J. Biol. Chem. 275, 23685\u201323692 (2000).","journal-title":"J. Biol. Chem."},{"key":"e_1_3_3_99_2","doi-asserted-by":"crossref","first-page":"296","DOI":"10.1016\/j.ajhg.2018.06.011","article-title":"Mutations in LNPK, encoding the endoplasmic reticulum junction stabilizer lunapark, cause a recessive neurodevelopmental syndrome","volume":"103","author":"Breuss M. W.","year":"2018","unstructured":"M. W. Breuss, A. Nguyen, Q. Song, T. Nguyen, V. Stanley, K. N. James, D. Musaev, G. Chai, S. A. Wirth, P. Anzenberg, R. D. George, A. Johansen, S. Ali, M. Zia-ur-Rehman, T. Sultan, M. S. Zaki, J. G. Gleeson, Mutations in LNPK, encoding the endoplasmic reticulum junction stabilizer lunapark, cause a recessive neurodevelopmental syndrome. Am. J. Hum. Genet. 103, 296\u2013304 (2018).","journal-title":"Am. J. Hum. Genet."},{"key":"e_1_3_3_100_2","doi-asserted-by":"crossref","first-page":"237","DOI":"10.1093\/jb\/mvi124","article-title":"Molecular cloning and expression of human ST6GalNAc III: Restricted tissue distribution and substrate specificity","volume":"138","author":"Tsuchida A.","year":"2005","unstructured":"A. Tsuchida, M. Ogiso, Y. Nakamura, M. Kiso, K. Furukawa, K. Furukawa, Molecular cloning and expression of human ST6GalNAc III: Restricted tissue distribution and substrate specificity. J. Biochem. 138, 237\u2013243 (2005).","journal-title":"J. Biochem."},{"key":"e_1_3_3_101_2","doi-asserted-by":"crossref","first-page":"1059","DOI":"10.1002\/pros.22826","article-title":"Increased expression of GCNT1 is associated with altered O-glycosylation of PSA, PAP, and MUC1 in human prostate cancers","volume":"74","author":"Chen Z.","year":"2014","unstructured":"Z. Chen, Z. G. Gulzar, C. A. St. Hill, B. Walcheck, J. D. Brooks, Increased expression of GCNT1 is associated with altered O-glycosylation of PSA, PAP, and MUC1 in human prostate cancers. Prostate 74, 1059\u20131067 (2014).","journal-title":"Prostate"},{"key":"e_1_3_3_102_2","doi-asserted-by":"crossref","first-page":"1674","DOI":"10.4049\/jimmunol.1901194","article-title":"GCNT1-mediated O-glycosylation of the sialomucin CD43 is a sensitive indicator of notch signaling in activated T cells","volume":"204","author":"Perkey E.","year":"2020","unstructured":"E. Perkey, D. Maurice De Sousa, L. Carrington, J. Chung, A. Dils, D. Granadier, U. Koch, F. Radtke, B. Ludewig, B. R. Blazar, C. W. Siebel, T. V. Brennan, J. Nolz, N. Labrecque, I. Maillard, GCNT1-mediated O-glycosylation of the sialomucin CD43 is a sensitive indicator of notch signaling in activated T cells. J. Immunol. 204, 1674\u20131688 (2020).","journal-title":"J. Immunol."},{"key":"e_1_3_3_103_2","doi-asserted-by":"crossref","first-page":"602","DOI":"10.1093\/glycob\/cwr179","article-title":"Characterization of ppGalNAc-T18, a member of the vertebrate-specific Y subfamily of UDP-N-acetyl-\u03b1-D-galactosamine:polypeptide N-acetylgalactosaminyltransferases","volume":"22","author":"Li X.","year":"2012","unstructured":"X. Li, J. Wang, W. Li, Y. Xu, D. Shao, Y. Xie, W. Xie, T. Kubota, H. Narimatsu, Y. Zhang, Characterization of ppGalNAc-T18, a member of the vertebrate-specific Y subfamily of UDP-N-acetyl-\u03b1-D-galactosamine:polypeptide N-acetylgalactosaminyltransferases. Glycobiology 22, 602\u2013615 (2012).","journal-title":"Glycobiology"},{"key":"e_1_3_3_104_2","doi-asserted-by":"crossref","first-page":"389","DOI":"10.1242\/jcs.037051","article-title":"EHD3 regulates early-endosome-to-Golgi transport and preserves Golgi morphology","volume":"122","author":"Naslavsky N.","year":"2009","unstructured":"N. Naslavsky, J. McKenzie, N. Altan-Bonnet, D. Sheff, S. Caplan, EHD3 regulates early-endosome-to-Golgi transport and preserves Golgi morphology. J. Cell Sci. 122, 389\u2013400 (2009).","journal-title":"J. Cell Sci."},{"key":"e_1_3_3_105_2","doi-asserted-by":"crossref","first-page":"13465","DOI":"10.1074\/jbc.M116.716407","article-title":"EHD3 protein is required for tubular recycling endosome stabilization, and an asparagine-glutamic acid residue pair within its Eps15 homology (EH) domain dictates its selective binding to NPF peptides","volume":"291","author":"Bahl K.","year":"2016","unstructured":"K. Bahl, S. Xie, G. Spagnol, P. Sorgen, N. Naslavsky, S. Caplan, EHD3 protein is required for tubular recycling endosome stabilization, and an asparagine-glutamic acid residue pair within its Eps15 homology (EH) domain dictates its selective binding to NPF peptides. J. Biol. Chem. 291, 13465\u201313478 (2016).","journal-title":"J. Biol. Chem."},{"key":"e_1_3_3_106_2","doi-asserted-by":"crossref","first-page":"70","DOI":"10.1016\/j.gene.2005.07.029","article-title":"The gene repertoire and the common evolutionary history of glutamate, pheromone (V2R), taste(1) and other related G protein-coupled receptors","volume":"362","author":"Bjarnad\u00f3ttir T. K.","year":"2005","unstructured":"T. K. Bjarnad\u00f3ttir, R. Fredriksson, H. B. Schi\u00f6th, The gene repertoire and the common evolutionary history of glutamate, pheromone (V2R), taste(1) and other related G protein-coupled receptors. Gene 362, 70\u201384 (2005).","journal-title":"Gene"},{"key":"e_1_3_3_107_2","doi-asserted-by":"crossref","first-page":"854556","DOI":"10.3389\/fnmol.2022.854556","article-title":"Sema6D regulates zebrafish vascular patterning and motor neuronal axon growth in spinal cord","volume":"15","author":"Sheng J.","year":"2022","unstructured":"J. Sheng, J. Xu, K. Geng, D. Liu, Sema6D regulates zebrafish vascular patterning and motor neuronal axon growth in spinal cord. Front Mol Neurosci. 15, 854556 (2022).","journal-title":"Front Mol Neurosci."},{"key":"e_1_3_3_108_2","doi-asserted-by":"crossref","first-page":"ar133","DOI":"10.1091\/mbc.E22-08-0336","article-title":"KAP is the neuronal organelle adaptor for kinesin-2 KIF3AB and KIF3AC","volume":"33","author":"Garbouchian A.","year":"2022","unstructured":"A. Garbouchian, A. C. Montgomery, S. P. Gilbert, M. Bentley, KAP is the neuronal organelle adaptor for kinesin-2 KIF3AB and KIF3AC. Mol. Biol. Cell 33, ar133 (2022).","journal-title":"Mol. Biol. Cell"},{"key":"e_1_3_3_109_2","first-page":"8443","article-title":"Cloning and characterization of KAP3: A novel kinesin superfamily-associated protein of KIF3A\/3B (microtubule\/axonal transport\/motor protein)","volume":"93","author":"Yamazaki H.","year":"1996","unstructured":"H. Yamazaki, T. Nakata, Y. Okada, N. Hirokawa, Cloning and characterization of KAP3: A novel kinesin superfamily-associated protein of KIF3A\/3B (microtubule\/axonal transport\/motor protein). Cell Biol. 93, 8443\u20138448 (1996).","journal-title":"Cell Biol."},{"key":"e_1_3_3_110_2","doi-asserted-by":"crossref","first-page":"466","DOI":"10.1124\/pr.119.018762","article-title":"Monocarboxylate transporters (SLC16): Function, regulation, and role in health and disease","volume":"72","author":"Felmlee M. A.","year":"2020","unstructured":"M. A. Felmlee, R. S. Jones, V. Rodriguez-Cruz, K. E. Follman, M. E. Morris, Monocarboxylate transporters (SLC16): Function, regulation, and role in health and disease. Pharmacol. Rev. 72, 466\u2013485 (2020).","journal-title":"Pharmacol. Rev."},{"key":"e_1_3_3_111_2","doi-asserted-by":"crossref","first-page":"1037","DOI":"10.1016\/S0896-6273(00)81049-1","article-title":"Caspr2, a new member of the neurexin superfamily, is localized at the juxtaparanodes of myelinated axons and associates with k channels","volume":"24","author":"Poliak S.","year":"1999","unstructured":"S. Poliak, L. Gollan, R. Martinez, A. Custer, S. Einheber, J. L. Salzer, J. S. Trimmer, P. Shrager, E. Peles, Caspr2, a new member of the neurexin superfamily, is localized at the juxtaparanodes of myelinated axons and associates with k channels. Neuron 24, 1037\u20131047 (1999).","journal-title":"Neuron"},{"key":"e_1_3_3_112_2","doi-asserted-by":"crossref","first-page":"780","DOI":"10.1016\/j.biopsych.2023.03.014","article-title":"Loss of CNTNAP2 alters human cortical excitatory neuron differentiation and neural network development","volume":"94","author":"St George-Hyslop F.","year":"2023","unstructured":"F. St George-Hyslop, M. Haneklaus, T. Kivisild, F. J. Livesey, Loss of CNTNAP2 alters human cortical excitatory neuron differentiation and neural network development. Biol. Psychiatry 94, 780\u2013791 (2023).","journal-title":"Biol. Psychiatry"},{"key":"e_1_3_3_113_2","doi-asserted-by":"crossref","first-page":"7","DOI":"10.1159\/000371594","article-title":"Connecting the CNTNAP2 networks with neurodevelopmental disorders","volume":"6","author":"Poot M.","year":"2015","unstructured":"M. Poot, Connecting the CNTNAP2 networks with neurodevelopmental disorders. Mol Syndromol. 6, 7\u201322 (2015).","journal-title":"Mol Syndromol."},{"key":"e_1_3_3_114_2","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1155\/2019\/2054783","article-title":"Cend1, a story with many tales: From regulation of cell cycle progression\/exit of neural stem cells to brain structure and function","volume":"2019","author":"Gaitanou M.","year":"2019","unstructured":"M. Gaitanou, K. Segklia, R. Matsas, Cend1, a story with many tales: From regulation of cell cycle progression\/exit of neural stem cells to brain structure and function. Stem Cells Int. 2019, 1\u201316 (2019).","journal-title":"Stem Cells Int."},{"key":"e_1_3_3_115_2","first-page":"1823","article-title":"TGF-b-induced profibrotic signaling is regulated in part by the WNT receptor Frizzled-8","volume":"30","author":"Spanjer A. I. R.","year":"2016","unstructured":"A. I. R. Spanjer, H. A. Baarsma, L. M. Oostenbrink, S. R. Jansen, C. C. Kuipers, M. Lindner, D. S. Postma, H. Meurs, I. H. Heijink, R. Gosens, M. K\u00f6nigshoff, A. M. Fachkliniken, TGF-b-induced profibrotic signaling is regulated in part by the WNT receptor Frizzled-8. J (Basel). 30, 1823\u20131835 (2016).","journal-title":"J (Basel)."},{"key":"e_1_3_3_116_2","doi-asserted-by":"crossref","first-page":"145","DOI":"10.1016\/S0925-4773(98)00076-8","article-title":"A role for xenopus Frizzled 8 in dorsal development","volume":"74","author":"Itoh K.","year":"1998","unstructured":"K. Itoh, J. Jacob, S. Y. Sokol, A role for xenopus Frizzled 8 in dorsal development. Mech. Dev. 74, 145\u2013157 (1998).","journal-title":"Mech. Dev."},{"key":"e_1_3_3_117_2","doi-asserted-by":"crossref","first-page":"2687","DOI":"10.1242\/dev.125.14.2687","article-title":"Frizzled-8 is expressed in the Spemann organizer and plays a role in early morphogenesis","volume":"125","author":"Deardorff M. A.","year":"1998","unstructured":"M. A. Deardorff, C. Tan, L. J. Conrad, P. S. Klein, Frizzled-8 is expressed in the Spemann organizer and plays a role in early morphogenesis. Development 125, 2687\u20132700 (1998).","journal-title":"Development"},{"key":"e_1_3_3_118_2","doi-asserted-by":"crossref","first-page":"249","DOI":"10.1042\/bj3550249","article-title":"Cellular functions of phosphatidylinositol 3-phosphate and FYVE domain proteins","volume":"355","author":"Gillooly D. J.","year":"2001","unstructured":"D. J. Gillooly, A. Simonsen, H. Stenmark, Cellular functions of phosphatidylinositol 3-phosphate and FYVE domain proteins. Biochem. J. 355, 249\u2013258 (2001).","journal-title":"Biochem. J."},{"key":"e_1_3_3_119_2","doi-asserted-by":"crossref","first-page":"63","DOI":"10.3389\/fcell.2020.00063","article-title":"CDP-diacylglycerol synthases (CDS): Gateway to phosphatidylinositol and cardiolipin synthesis","volume":"8","author":"Blunsom N. J.","year":"2020","unstructured":"N. J. Blunsom, S. Cockcroft, CDP-diacylglycerol synthases (CDS): Gateway to phosphatidylinositol and cardiolipin synthesis. Front. Cell Dev. Biol. 8, 63 (2020).","journal-title":"Front. Cell Dev. Biol."},{"key":"e_1_3_3_120_2","doi-asserted-by":"crossref","first-page":"83","DOI":"10.1177\/1535370219828195","article-title":"TYRO3: A potential therapeutic target in cancer","volume":"244","author":"Hsu P.-L.","year":"2019","unstructured":"P.-L. Hsu, J. Jou, S.-J. Tsai, TYRO3: A potential therapeutic target in cancer. Exp. Biol. Med. 244, 83\u201399 (2019).","journal-title":"Exp. Biol. Med."},{"key":"e_1_3_3_121_2","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1016\/j.pneurobio.2014.09.002","article-title":"Neuronal stathmins: A family of phosphoproteins cooperating for neuronal development, plasticity and regeneration","volume":"126","author":"Chauvin S.","year":"2015","unstructured":"S. Chauvin, A. Sobel, Neuronal stathmins: A family of phosphoproteins cooperating for neuronal development, plasticity and regeneration. Prog. Neurobiol. 126, 1\u201318 (2015).","journal-title":"Prog. Neurobiol."},{"key":"e_1_3_3_122_2","doi-asserted-by":"crossref","first-page":"392","DOI":"10.1016\/j.yexcr.2003.11.024","article-title":"LIM kinase 1, a key regulator of actin dynamics, is widely expressed in embryonic and adult tissues","volume":"294","author":"Foletta V. C.","year":"2004","unstructured":"V. C. Foletta, N. Moussi, P. D. Sarmiere, J. R. Bamburg, O. Bernard, LIM kinase 1, a key regulator of actin dynamics, is widely expressed in embryonic and adult tissues. Exp. Cell Res. 294, 392\u2013405 (2004).","journal-title":"Exp. Cell Res."},{"key":"e_1_3_3_123_2","doi-asserted-by":"crossref","first-page":"358","DOI":"10.3390\/cells9020358","article-title":"Much more than a Scaffold: Cytoskeletal proteins in neurological disorders","volume":"9","author":"Mu\u00f1oz-Lasso D. C.","year":"2020","unstructured":"D. C. Mu\u00f1oz-Lasso, C. Rom\u00e1-Mateo, F. V. Pallard\u00f3, P. Gonzalez-Cabo, Much more than a Scaffold: Cytoskeletal proteins in neurological disorders. Cell 9, 358 (2020).","journal-title":"Cell"},{"key":"e_1_3_3_124_2","first-page":"1","article-title":"Functional roles of ST8SIA3-mediated sialylation of striatal dopamine D2 and adenosine A2A receptors","volume":"9","author":"Lin C. Y.","year":"2019","unstructured":"C. Y. Lin, H. L. Lai, H. M. Chen, J. J. Siew, C. Te Hsiao, H. C. Chang, K. S. Liao, S. C. Tsai, C. Y. Wu, K. Kitajima, C. Sato, K. H. Khoo, Y. Chern, Functional roles of ST8SIA3-mediated sialylation of striatal dopamine D2 and adenosine A2A receptors. Transl. Psychiatry 9, 1\u201313 (2019).","journal-title":"Transl. Psychiatry"},{"key":"e_1_3_3_125_2","first-page":"2359","article-title":"The intrinsic relationship between structure and function of the sialyltransferase ST8Sia family members","volume":"17","author":"Huang R.-B.","year":"2017","unstructured":"R.-B. Huang, D. Cheng, S.-M. Liao, B. Lu, Q.-Y. Wang, N.-Z. Xie, F. A. Troy II, G.-P. Zhou, The intrinsic relationship between structure and function of the sialyltransferase ST8Sia family members. Curr. Top. Med. Chem. 17, 2359\u20132369 (2017).","journal-title":"Curr. Top. Med. Chem."},{"key":"e_1_3_3_126_2","doi-asserted-by":"crossref","first-page":"713","DOI":"10.1016\/j.apsb.2018.07.009","article-title":"Ganglioside GD3 synthase (GD3S), a novel cancer drug target","volume":"8","author":"Liu J.","year":"2018","unstructured":"J. Liu, X. Zheng, X. Pang, L. Li, J. Wang, C. Yang, G. Du, Ganglioside GD3 synthase (GD3S), a novel cancer drug target. Acta Pharm. Sin. 8, 713\u2013720 (2018).","journal-title":"Acta Pharm. Sin."},{"key":"e_1_3_3_127_2","doi-asserted-by":"crossref","first-page":"1289","DOI":"10.1093\/glycob\/cws103","article-title":"Biosynthesis of the major brain gangliosides GD1a and GT1b","volume":"22","author":"Sturgill E. R.","year":"2012","unstructured":"E. R. Sturgill, K. Aoki, P. Hh Lopez, D. Colacurcio, K. Vajn, I. Lorenzini, S. Maji\u0107, W. H. Yang, M. Heffer, M. Tiemeyer, J. D. Marth, R. L. Schnaar, Biosynthesis of the major brain gangliosides GD1a and GT1b. Glycobiology 22, 1289\u20131301 (2012).","journal-title":"Glycobiology"},{"key":"e_1_3_3_128_2","doi-asserted-by":"crossref","first-page":"3040","DOI":"10.1096\/fj.15-270983","article-title":"Sialylation regulates brain structure and function","volume":"29","author":"Yoo S. W.","year":"2015","unstructured":"S. W. Yoo, M. G. Motari, K. Susuki, J. Prendergast, A. Mountney, A. Hurtado, R. L. Schnaar, Sialylation regulates brain structure and function. FASEB J. 29, 3040\u20133053 (2015).","journal-title":"FASEB J."},{"key":"e_1_3_3_129_2","doi-asserted-by":"crossref","first-page":"5170","DOI":"10.1074\/jbc.274.8.5170","article-title":"Multiple isoforms of heparan sulfate d-glucosaminyl 3-O-sulfotransferase: Isolation, characterization, and expression of human cdnas and identification of distinct genomic loci","volume":"274","author":"Shworak N. W.","year":"1999","unstructured":"N. W. Shworak, J. Liu, L. M. Petros, L. Zhang, M. Kobayashi, N. G. Copeland, N. A. Jenkins, R. D. Rosenberg, Multiple isoforms of heparan sulfate d-glucosaminyl 3-O-sulfotransferase: Isolation, characterization, and expression of human cdnas and identification of distinct genomic loci. J. Biol. Chem. 274, 5170\u20135184 (1999).","journal-title":"J. Biol. Chem."},{"key":"e_1_3_3_130_2","doi-asserted-by":"crossref","first-page":"443","DOI":"10.1007\/978-1-0716-1398-6_35","article-title":"Regulation of 3-O-sulfation of heparan sulfate during transition from the na\u00efve to the primed state in mouse embryonic stem cells","volume":"2303","author":"Ota H.","year":"2022","unstructured":"H. Ota, S. Nishihara, Regulation of 3-O-sulfation of heparan sulfate during transition from the na\u00efve to the primed state in mouse embryonic stem cells. Methods Mol. Biol. 2303, 443\u2013452 (2022).","journal-title":"Methods Mol. Biol."},{"key":"e_1_3_3_131_2","doi-asserted-by":"crossref","first-page":"7297","DOI":"10.1073\/pnas.1501627112","article-title":"Overlapping functions of stonin 2 and SV2 in sorting of the calcium sensor synaptotagmin 1 to synaptic vesicles","volume":"112","author":"Kaempf N.","year":"2015","unstructured":"N. Kaempf, G. Kochlamazashvili, D. Puchkov, T. Maritzen, S. M. Bajjalieh, N. L. Kononenko, V. Haucke, Overlapping functions of stonin 2 and SV2 in sorting of the calcium sensor synaptotagmin 1 to synaptic vesicles. Proc. Natl. Acad. Sci. U.S.A. 112, 7297\u20137302 (2015).","journal-title":"Proc. Natl. Acad. Sci. U.S.A."},{"key":"e_1_3_3_132_2","doi-asserted-by":"crossref","first-page":"960","DOI":"10.1152\/ajpcell.00259.2010","article-title":"SV2 regulates neurotransmitter release via multiple mechanisms","volume":"299","author":"Nowack A.","year":"2010","unstructured":"A. Nowack, J. Yao, K. L. Custer, S. M. Bajjalieh, SV2 regulates neurotransmitter release via multiple mechanisms. Am. J. Physiol. Cell Physiol. 299, 960\u2013967 (2010).","journal-title":"Am. J. Physiol. Cell Physiol."},{"key":"e_1_3_3_133_2","first-page":"251","article-title":"VAMP subfamilies identified by specific R-SNARE motifs","volume":"96","author":"Rossi V.","year":"2004","unstructured":"V. Rossi, R. Picco, M. Vacca, M. D\u2019Esposito, M. D\u2019Urso, T. Galli, F. Filippini, VAMP subfamilies identified by specific R-SNARE motifs. Biol. Cell 96, 251\u2013256 (2004).","journal-title":"Biol. Cell"},{"key":"e_1_3_3_134_2","first-page":"305","article-title":"Amphiphysin I and regulation of synaptic vesicle endocytosis","volume":"63","author":"Wu Y.","year":"2009","unstructured":"Y. Wu, H. Matsui, K. Tomizawa, Amphiphysin I and regulation of synaptic vesicle endocytosis. Acta Med. Okayama 63, 305\u2013323 (2009).","journal-title":"Acta Med. Okayama"},{"key":"e_1_3_3_135_2","doi-asserted-by":"crossref","first-page":"331","DOI":"10.1073\/pnas.93.1.331","article-title":"A role of amphiphysin in synaptic vesicle endocytosis suggested by its binding to dynamin in nerve terminals","volume":"93","author":"David C.","year":"1996","unstructured":"C. David, P. S. McPherson, O. Mundigl, P. De Camilli, A role of amphiphysin in synaptic vesicle endocytosis suggested by its binding to dynamin in nerve terminals. PNAS. 93, 331\u2013335 (1996).","journal-title":"PNAS."},{"key":"e_1_3_3_136_2","doi-asserted-by":"crossref","first-page":"187218","DOI":"10.3389\/fnsyn.2016.00007","article-title":"SNAP-25, a known presynaptic protein with emerging postsynaptic functions","volume":"8","author":"Antonucci F.","year":"2016","unstructured":"F. Antonucci, I. Corradini, G. Fossati, R. Tomasoni, E. Menna, M. Matteoli, SNAP-25, a known presynaptic protein with emerging postsynaptic functions. Front Synaptic Neurosci. 8, 187218 (2016).","journal-title":"Front Synaptic Neurosci."},{"key":"e_1_3_3_137_2","doi-asserted-by":"crossref","first-page":"18893","DOI":"10.1074\/jbc.274.27.18893","article-title":"Synaptogyrins regulate Ca2+\u2212dependent exocytosis in PC12 Cells","volume":"274","author":"Sugita S.","year":"1999","unstructured":"S. Sugita, R. Janz, T. C. S\u00fcdhof, Synaptogyrins regulate Ca2+\u2212dependent exocytosis in PC12 Cells. J. Biol. Chem. 274, 18893\u201318901 (1999).","journal-title":"J. Biol. Chem."},{"key":"e_1_3_3_138_2","doi-asserted-by":"crossref","first-page":"14417","DOI":"10.1523\/JNEUROSCI.1236-13.2013","article-title":"Synaptotagmin interaction with SNAP-25 governs vesicle docking, priming, and fusion triggering","volume":"33","author":"Mohrmann R.","year":"2013","unstructured":"R. Mohrmann, H. de Wit, E. Connell, P. S. Pinheiro, C. Leese, D. Bruns, B. Davletov, M. Verhage, J. B. S\u00f8rensen, Synaptotagmin interaction with SNAP-25 governs vesicle docking, priming, and fusion triggering. J. Neurosci. 33, 14417\u201314430 (2013).","journal-title":"J. Neurosci."},{"key":"e_1_3_3_139_2","doi-asserted-by":"crossref","first-page":"1964","DOI":"10.1212\/WNL.0000000000002185","article-title":"Electrophysiologic features of SYT2 mutations causing a treatable neuromuscular syndrome","volume":"85","author":"Whittaker R. G.","year":"2015","unstructured":"R. G. Whittaker, D. N. Herrmann, B. Bansagi, B. A. S. Hasan, R. M. Lofra, E. L. Logigian, J. E. Sowden, J. L. Almodovar, J. T. Littleton, S. Zuchner, R. Horvath, H. Lochm\u00fcller, Electrophysiologic features of SYT2 mutations causing a treatable neuromuscular syndrome. Neurology 85, 1964\u20131971 (2015).","journal-title":"Neurology"}],"container-title":["Science Advances"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/www.science.org\/doi\/pdf\/10.1126\/sciadv.adh3929","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2024,5,16]],"date-time":"2024-05-16T20:07:24Z","timestamp":1715890044000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.science.org\/doi\/10.1126\/sciadv.adh3929"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2024,1,12]]},"references-count":138,"journal-issue":{"issue":"2","published-print":{"date-parts":[[2024,1,12]]}},"alternative-id":["10.1126\/sciadv.adh3929"],"URL":"https:\/\/doi.org\/10.1126\/sciadv.adh3929","relation":{},"ISSN":["2375-2548"],"issn-type":[{"value":"2375-2548","type":"electronic"}],"subject":[],"published":{"date-parts":[[2024,1,12]]},"assertion":[{"value":"2023-03-02","order":0,"name":"received","label":"Received","group":{"name":"publication_history","label":"Publication History"}},{"value":"2023-12-12","order":1,"name":"accepted","label":"Accepted","group":{"name":"publication_history","label":"Publication History"}},{"value":"2024-01-10","order":2,"name":"published","label":"Published","group":{"name":"publication_history","label":"Publication History"}}],"article-number":"eadh3929"}}