{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,6]],"date-time":"2026-10-06T16:22:13Z","timestamp":1791303733042,"version":"4.1.0"},"reference-count":36,"publisher":"Springer Science and Business Media LLC","issue":"6","license":[{"start":{"date-parts":[[2006,5,14]],"date-time":"2006-05-14T00:00:00Z","timestamp":1147564800000},"content-version":"tdm","delay-in-days":0,"URL":"http:\/\/www.springer.com\/tdm"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Nat Neurosci"],"published-print":{"date-parts":[[2006,6]]},"DOI":"10.1038\/nn1702","type":"journal-article","created":{"date-parts":[[2006,5,14]],"date-time":"2006-05-14T13:27:22Z","timestamp":1147613242000},"page":"824-831","source":"Crossref","is-referenced-by-count":302,"title":["Palmitoylation of huntingtin by HIP14is essential for its trafficking and function"],"prefix":"10.1038","volume":"9","author":[{"given":"Anat","family":"Yanai","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Kun","family":"Huang","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Rujun","family":"Kang","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Roshni R","family":"Singaraja","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Pamela","family":"Arstikaitis","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Lu","family":"Gan","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Paul C","family":"Orban","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Asher","family":"Mullard","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Catherine M","family":"Cowan","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Lynn A","family":"Raymond","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Renaldo C","family":"Drisdel","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"William N","family":"Green","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Brinda","family":"Ravikumar","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"David C","family":"Rubinsztein","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Alaa","family":"El-Husseini","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Michael R","family":"Hayden","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"297","published-online":{"date-parts":[[2006,5,14]]},"reference":[{"key":"BFnn1702_CR1","doi-asserted-by":"publisher","first-page":"159","DOI":"10.1083\/jcb.148.1.159","volume":"148","author":"AE El-Husseini","year":"2000","unstructured":"El-Husseini, A.E. et al. Dual palmitoylation of PSD-95 mediates its vesiculotubular sorting, postsynaptic targeting, and ion channel clustering. J. Cell Biol. 148, 159\u2013172 (2000).","journal-title":"J. Cell Biol."},{"key":"BFnn1702_CR2","doi-asserted-by":"publisher","first-page":"791","DOI":"10.1038\/nrn940","volume":"3","author":"A El-Husseini","year":"2002","unstructured":"El-Husseini, A. & Bredt, D.S. Protein palmitoylation: a regulator of neuronal development and function. Nat. Rev. Neurosci. 3, 791\u2013802 (2002).","journal-title":"Nat. Rev. Neurosci."},{"key":"BFnn1702_CR3","doi-asserted-by":"publisher","first-page":"527","DOI":"10.1016\/j.conb.2005.08.001","volume":"15","author":"K Huang","year":"2005","unstructured":"Huang, K. & El-Husseini, A. Modulation of neuronal protein trafficking and function by palmitoylation. Curr. Opin. Neurobiol. 15, 527\u2013535 (2005).","journal-title":"Curr. Opin. Neurobiol."},{"key":"BFnn1702_CR4","doi-asserted-by":"publisher","first-page":"977","DOI":"10.1016\/j.neuron.2004.11.027","volume":"44","author":"K Huang","year":"2004","unstructured":"Huang, K. et al. Huntingtin-interacting protein HIP14 is a palmitoyl transferase involved in palmitoylation and trafficking of multiple neuronal proteins. Neuron 44, 977\u2013986 (2004).","journal-title":"Neuron"},{"key":"BFnn1702_CR5","doi-asserted-by":"crossref","unstructured":"The Huntington's Disease Collaborative Research Group. A novel gene containing a trinucleotide repeat that is expanded and unstable on Huntington's disease chromosomes. Cell 72, 971\u2013983 (1993).","DOI":"10.1016\/0092-8674(93)90585-E"},{"key":"BFnn1702_CR6","doi-asserted-by":"publisher","first-page":"1097","DOI":"10.1083\/jcb.141.5.1097","volume":"141","author":"AS Hackam","year":"1998","unstructured":"Hackam, A.S. et al. The influence of huntingtin protein size on nuclear localization and cellular toxicity. J. Cell Biol. 141, 1097\u20131105 (1998).","journal-title":"J. Cell Biol."},{"key":"BFnn1702_CR7","doi-asserted-by":"publisher","first-page":"633","DOI":"10.1093\/hmg\/11.6.633","volume":"11","author":"VC Wheeler","year":"2002","unstructured":"Wheeler, V.C. et al. Early phenotypes that presage late-onset neurodegenerative disease allow testing of modifiers in Hdh CAG knock-in mice. Hum. Mol. Genet. 11, 633\u2013640 (2002).","journal-title":"Hum. Mol. Genet."},{"key":"BFnn1702_CR8","doi-asserted-by":"publisher","first-page":"3823","DOI":"10.1093\/hmg\/ddi407","volume":"14","author":"JM Van Raamsdonk","year":"2005","unstructured":"Van Raamsdonk, J.M., Murphy, Z., Slow, E.J., Leavitt, B.R. & Hayden, M.R. Selective degeneration and nuclear localization of mutant huntingtin in the YAC128 mouse model of Huntington disease. Hum. Mol. Genet. 14, 3823\u20133835 (2005).","journal-title":"Hum. Mol. Genet."},{"key":"BFnn1702_CR9","doi-asserted-by":"publisher","first-page":"34","DOI":"10.1006\/exnr.1998.6832","volume":"152","author":"J Velier","year":"1998","unstructured":"Velier, J. et al. Wild-type and mutant huntingtins function in vesicle trafficking in the secretory and endocytic pathways. Exp. Neurol. 152, 34\u201340 (1998).","journal-title":"Exp. Neurol."},{"key":"BFnn1702_CR10","doi-asserted-by":"publisher","first-page":"1075","DOI":"10.1016\/0896-6273(95)90346-1","volume":"14","author":"M DiFiglia","year":"1995","unstructured":"DiFiglia, M. et al. Huntingtin is a cytoplasmic protein associated with vesicles in human and rat brain neurons. Neuron 14, 1075\u20131081 (1995).","journal-title":"Neuron"},{"key":"BFnn1702_CR11","doi-asserted-by":"publisher","first-page":"36464","DOI":"10.1074\/jbc.M503672200","volume":"280","author":"KB Kegel","year":"2005","unstructured":"Kegel, K.B. et al. Huntingtin associates with acidic phospholipids at the plasma membrane. J. Biol. Chem. 280, 36464\u201336473 (2005).","journal-title":"J. Biol. Chem."},{"key":"BFnn1702_CR12","doi-asserted-by":"publisher","first-page":"19385","DOI":"10.1074\/jbc.271.32.19385","volume":"271","author":"MA Kalchman","year":"1996","unstructured":"Kalchman, M.A. et al. Huntingtin is ubiquitinated and interacts with a specific ubiquitin-conjugating enzyme. J. Biol. Chem. 271, 19385\u201319394 (1996).","journal-title":"J. Biol. Chem."},{"key":"BFnn1702_CR13","doi-asserted-by":"publisher","first-page":"100","DOI":"10.1126\/science.1092194","volume":"304","author":"JS Steffan","year":"2004","unstructured":"Steffan, J.S. et al. SUMO modification of Huntingtin and Huntington's disease pathology. Science 304, 100\u2013104 (2004).","journal-title":"Science"},{"key":"BFnn1702_CR14","doi-asserted-by":"publisher","first-page":"831","DOI":"10.1016\/S1534-5807(02)00188-0","volume":"2","author":"S Humbert","year":"2002","unstructured":"Humbert, S. et al. The IGF-1\/Akt pathway is neuroprotective in Huntington's disease and involves Huntingtin phosphorylation by Akt. Dev. Cell 2, 831\u2013837 (2002).","journal-title":"Dev. Cell"},{"key":"BFnn1702_CR15","doi-asserted-by":"publisher","first-page":"1569","DOI":"10.1093\/hmg\/ddi165","volume":"14","author":"SC Warby","year":"2005","unstructured":"Warby, S.C. et al. Huntingtin phosphorylation on serine 421 is significantly reduced in the striatum and by polyglutamine expansion in vivo. Hum. Mol. Genet. 14, 1569\u20131577 (2005).","journal-title":"Hum. Mol. Genet."},{"key":"BFnn1702_CR16","doi-asserted-by":"publisher","first-page":"524","DOI":"10.1016\/S0962-8924(00)01852-3","volume":"10","author":"RR Kopito","year":"2000","unstructured":"Kopito, R.R. Aggresomes, inclusion bodies and protein aggregation. Trends Cell Biol. 10, 524\u2013530 (2000).","journal-title":"Trends Cell Biol."},{"key":"BFnn1702_CR17","doi-asserted-by":"publisher","first-page":"1393","DOI":"10.1091\/mbc.12.5.1393","volume":"12","author":"S Waelter","year":"2001","unstructured":"Waelter, S. et al. Accumulation of mutant huntingtin fragments in aggresome-like inclusion bodies as a result of insufficient protein degradation. Mol. Biol. Cell 12, 1393\u20131407 (2001).","journal-title":"Mol. Biol. Cell"},{"key":"BFnn1702_CR18","doi-asserted-by":"publisher","first-page":"1137","DOI":"10.1093\/hmg\/11.9.1137","volume":"11","author":"A Wyttenbach","year":"2002","unstructured":"Wyttenbach, A. et al. Heat shock protein 27 prevents cellular polyglutamine toxicity and suppresses the increase of reactive oxygen species caused by huntingtin. Hum. Mol. Genet. 11, 1137\u20131151 (2002).","journal-title":"Hum. Mol. Genet."},{"key":"BFnn1702_CR19","doi-asserted-by":"publisher","first-page":"604","DOI":"10.1002\/ana.410420411","volume":"42","author":"E Sapp","year":"1997","unstructured":"Sapp, E. et al. Huntingtin localization in brains of normal and Huntington's disease patients. Ann. Neurol. 42, 604\u2013612 (1997).","journal-title":"Ann. Neurol."},{"key":"BFnn1702_CR20","doi-asserted-by":"publisher","first-page":"849","DOI":"10.1016\/S0896-6273(02)00615-3","volume":"33","author":"MM Zeron","year":"2002","unstructured":"Zeron, M.M. et al. Increased sensitivity to N-methyl-D-aspartate receptor-mediated excitotoxicity in a mouse model of Huntington's disease. Neuron 33, 849\u2013860 (2002).","journal-title":"Neuron"},{"key":"BFnn1702_CR21","doi-asserted-by":"publisher","first-page":"2815","DOI":"10.1093\/hmg\/11.23.2815","volume":"11","author":"RR Singaraja","year":"2002","unstructured":"Singaraja, R.R. et al. HIP14, a novel ankyrin domain-containing protein, links huntingtin to intracellular trafficking and endocytosis. Hum. Mol. Genet. 11, 2815\u20132828 (2002).","journal-title":"Hum. Mol. Genet."},{"key":"BFnn1702_CR22","doi-asserted-by":"publisher","first-page":"1555","DOI":"10.1093\/hmg\/ddg169","volume":"12","author":"EJ Slow","year":"2003","unstructured":"Slow, E.J. et al. Selective striatal neuronal loss in a YAC128 mouse model of Huntington disease. Hum. Mol. Genet. 12, 1555\u20131567 (2003).","journal-title":"Hum. Mol. Genet."},{"key":"BFnn1702_CR23","doi-asserted-by":"publisher","first-page":"276","DOI":"10.2144\/04362RR02","volume":"36","author":"RC Drisdel","year":"2004","unstructured":"Drisdel, R.C. & Green, W.N. Labeling and quantifying sites of protein palmitoylation. Biotechniques 36, 276\u2013285 (2004).","journal-title":"Biotechniques"},{"key":"BFnn1702_CR24","doi-asserted-by":"publisher","first-page":"10502","DOI":"10.1523\/JNEUROSCI.3315-04.2004","volume":"24","author":"RC Drisdel","year":"2004","unstructured":"Drisdel, R.C., Manzana, E. & Green, W.N. The role of palmitoylation in functional expression of nicotinic alpha7 receptors. J. Neurosci. 24, 10502\u201310510 (2004).","journal-title":"J. Neurosci."},{"key":"BFnn1702_CR25","doi-asserted-by":"publisher","first-page":"849","DOI":"10.1016\/S0092-8674(02)00683-9","volume":"108","author":"A El-Husseini","year":"2002","unstructured":"El-Husseini, A. et al. Synaptic strength regulated by palmitate cycling on PSD-95. Cell 108, 849\u2013863 (2002).","journal-title":"Cell"},{"key":"BFnn1702_CR26","first-page":"203","volume":"146","author":"S Rakhilin","year":"1999","unstructured":"Rakhilin, S. et al. Alpha-bungarotoxin receptors contain alpha7 subunits in two different disulfide-bonded conformations. J. Cell Biol. 146, 203\u2013218 (1999).","journal-title":"J. Cell Biol."},{"key":"BFnn1702_CR27","doi-asserted-by":"publisher","first-page":"1746","DOI":"10.1126\/science.1105654","volume":"307","author":"O Rocks","year":"2005","unstructured":"Rocks, O. et al. An acylation cycle regulates localization and activity of palmitoylated Ras isoforms. Science 307, 1746\u20131752 (2005).","journal-title":"Science"},{"key":"BFnn1702_CR28","doi-asserted-by":"publisher","first-page":"623","DOI":"10.1083\/jcb.200502007","volume":"169","author":"RM Drenan","year":"2005","unstructured":"Drenan, R.M. et al. Palmitoylation regulates plasma membrane-nuclear shuttling of R7BP, a novel membrane anchor for the RGS7 family. J. Cell Biol. 169, 623\u2013633 (2005).","journal-title":"J. Cell Biol."},{"key":"BFnn1702_CR29","doi-asserted-by":"publisher","first-page":"9418","DOI":"10.1523\/JNEUROSCI.23-28-09418.2003","volume":"23","author":"RJ Ferrante","year":"2003","unstructured":"Ferrante, R.J. et al. Histone deacetylase inhibition by sodium butyrate chemotherapy ameliorates the neurodegenerative phenotype in Huntington's disease mice. J. Neurosci. 23, 9418\u20139427 (2003).","journal-title":"J. Neurosci."},{"key":"BFnn1702_CR30","doi-asserted-by":"publisher","first-page":"873","DOI":"10.1038\/sj.cdd.4401093","volume":"9","author":"PG Mastroberardino","year":"2002","unstructured":"Mastroberardino, P.G. et al. 'Tissue' transglutaminase ablation reduces neuronal death and prolongs survival in a mouse model of Huntington's disease. Cell Death Differ. 9, 873\u2013880 (2002).","journal-title":"Cell Death Differ."},{"key":"BFnn1702_CR31","doi-asserted-by":"publisher","first-page":"11402","DOI":"10.1073\/pnas.0503634102","volume":"102","author":"EJ Slow","year":"2005","unstructured":"Slow, E.J. et al. Absence of behavioral abnormalities and neurodegeneration in vivo despite widespread neuronal huntingtin inclusions. Proc. Natl. Acad. Sci. USA 102, 11402\u201311407 (2005).","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"BFnn1702_CR32","doi-asserted-by":"publisher","first-page":"805","DOI":"10.1038\/nature02998","volume":"431","author":"M Arrasate","year":"2004","unstructured":"Arrasate, M., Mitra, S., Schweitzer, E.S., Segal, M.R. & Finkbeiner, S. Inclusion body formation reduces levels of mutant huntingtin and the risk of neuronal death. Nature 431, 805\u2013810 (2004).","journal-title":"Nature"},{"key":"BFnn1702_CR33","doi-asserted-by":"publisher","first-page":"27456","DOI":"10.1074\/jbc.272.43.27456","volume":"272","author":"AA Soyombo","year":"1997","unstructured":"Soyombo, A.A. & Hofmann, S.L. Molecular cloning and expression of palmitoyl-protein thioesterase 2 (PPT2), a homolog of lysosomal palmitoyl-protein thioesterase with a distinct substrate specificity. J. Biol. Chem. 272, 27456\u201327463 (1997).","journal-title":"J. Biol. Chem."},{"key":"BFnn1702_CR34","doi-asserted-by":"publisher","first-page":"15831","DOI":"10.1074\/jbc.271.26.15831","volume":"271","author":"LA Verkruyse","year":"1996","unstructured":"Verkruyse, L.A. & Hofmann, S.L. Lysosomal targeting of palmitoyl-protein thioesterase. J. Biol. Chem. 271, 15831\u201315836 (1996).","journal-title":"J. Biol. Chem."},{"key":"BFnn1702_CR35","doi-asserted-by":"publisher","first-page":"9158","DOI":"10.1074\/jbc.273.15.9158","volume":"273","author":"CL Wellington","year":"1998","unstructured":"Wellington, C.L. et al. Caspase cleavage of gene products associated with triplet expansion disorders generates truncated fragments containing the polyglutamine tract. J. Biol. Chem. 273, 9158\u20139167 (1998).","journal-title":"J. Biol. Chem."},{"key":"BFnn1702_CR36","doi-asserted-by":"publisher","first-page":"593","DOI":"10.1016\/S0076-6879(06)06046-0","volume":"406","author":"J Janas","year":"2006","unstructured":"Janas, J., Skowronski, J. & Van, A.L. Lentiviral delivery of RNAi in hippocampal neurons. Methods Enzymol. 406, 593\u2013605 (2006).","journal-title":"Methods Enzymol."}],"container-title":["Nature Neuroscience"],"original-title":[],"language":"en","link":[{"URL":"http:\/\/www.nature.com\/articles\/nn1702.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"text-mining"},{"URL":"http:\/\/www.nature.com\/articles\/nn1702","content-type":"text\/html","content-version":"vor","intended-application":"text-mining"},{"URL":"http:\/\/www.nature.com\/articles\/nn1702.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2023,5,18]],"date-time":"2023-05-18T19:57:33Z","timestamp":1684439853000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.nature.com\/articles\/nn1702"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2006,5,14]]},"references-count":36,"journal-issue":{"issue":"6","published-print":{"date-parts":[[2006,6]]}},"alternative-id":["BFnn1702"],"URL":"https:\/\/doi.org\/10.1038\/nn1702","relation":{},"ISSN":["1097-6256","1546-1726"],"issn-type":[{"value":"1097-6256","type":"print"},{"value":"1546-1726","type":"electronic"}],"subject":[],"published":{"date-parts":[[2006,5,14]]}}}