{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,5,1]],"date-time":"2026-05-01T01:37:50Z","timestamp":1777599470495,"version":"3.51.4"},"reference-count":65,"publisher":"The Company of Biologists","issue":"5","license":[{"start":{"date-parts":[[2020,9,3]],"date-time":"2020-09-03T00:00:00Z","timestamp":1599091200000},"content-version":"vor","delay-in-days":2736,"URL":"http:\/\/creativecommons.org\/licenses\/by-nc-sa\/3.0"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"published-print":{"date-parts":[[2013,5,15]]},"abstract":"<jats:title>Summary<\/jats:title>\n               <jats:p>Reversible phosphorylation plays an important role as a mechanism of intracellular control in eukaryotes. PPP1, a major eukaryotic Ser\/Thr-protein phosphatase, acquires its specificity by interacting with different protein regulators, also known as PPP1 interacting proteins (PIPs). In the present work we characterized a physiologically relevant PIP in testis. Using a yeast two-hybrid screen with a human testis cDNA library, we identified a novel PIP of PPP1CC2 isoform, the T-complex testis expressed protein 1 domain containing 4 (TCTEX1D4) that has recently been described as a Tctex1 dynein light chain family member. The overlay assays confirm that TCTEX1D4 interacts with the different spliced isoforms of PPP1CC. Also, the binding domain occurs in the N-terminus, where a consensus PPP1 binding motif (PPP1BM) RVSF is present. The distribution of TCTEX1D4 in testis suggests its involvement in distinct functions, such as TGF\u03b2 signaling at the blood\u2013testis barrier and acrosome cap formation. Immunofluorescence in human ejaculated sperm shows that TCTEX1D4 is present in the flagellum and in the acrosome region of the head. Moreover, TCTEX1D4 and PPP1 co-localize in the microtubule organizing center (MTOC) and microtubules in cell cultures. Importantly, the TCTEX1D4 PPP1BM seems to be relevant for complex formation, for PPP1 retention in the MTOC and movement along microtubules.<\/jats:p>\n               <jats:p>These novel results open new avenues to possible roles of this dynein, together with PPP1. In essence TCTEX1D4\/PPP1C complex appears to be involved in microtubule dynamics, sperm motility, acrosome reaction and in the regulation of the blood\u2013testis barrier.<\/jats:p>","DOI":"10.1242\/bio.20131065","type":"journal-article","created":{"date-parts":[[2013,3,12]],"date-time":"2013-03-12T02:45:18Z","timestamp":1363056318000},"page":"453-465","source":"Crossref","is-referenced-by-count":18,"title":["TCTEX1D4, a novel protein phosphatase 1 interactor: connecting the phosphatase to the microtubule network"],"prefix":"10.1242","volume":"2","author":[{"given":"Lu\u00eds","family":"Korrodi-Greg\u00f3rio","sequence":"first","affiliation":[{"name":"Laboratory of Signal Transduction, Centre for Cell Biology, Biology Department, University of Aveiro, 3810-193 Aveiro, Portugal"}]},{"given":"Sandra I.","family":"Vieira","sequence":"additional","affiliation":[{"name":"Laboratory of Neurosciences, Centre for Cell Biology, Health Sciences Department and Biology Department, University of Aveiro, 3810-193 Aveiro, Portugal"}]},{"given":"Sara L. C.","family":"Esteves","sequence":"additional","affiliation":[{"name":"Laboratory of Signal Transduction, Centre for Cell Biology, Biology Department, University of Aveiro, 3810-193 Aveiro, Portugal"}]},{"given":"Joana V.","family":"Silva","sequence":"additional","affiliation":[{"name":"Laboratory of Signal Transduction, Centre for Cell Biology, Biology Department, University of Aveiro, 3810-193 Aveiro, Portugal"}]},{"given":"Maria Jo\u00e3o","family":"Freitas","sequence":"additional","affiliation":[{"name":"Laboratory of Signal Transduction, Centre for Cell Biology, Biology Department, University of Aveiro, 3810-193 Aveiro, Portugal"}]},{"given":"Ann-Kristin","family":"Brauns","sequence":"additional","affiliation":[{"name":"Department of Anatomy and Experimental Morphology, Center of Experimental Medicine, University Medical Center Hamburg-Eppendorf, D-20246 Hamburg, Germany"}]},{"given":"Georg","family":"Luers","sequence":"additional","affiliation":[{"name":"Department of Anatomy and Experimental Morphology, Center of Experimental Medicine, University Medical Center Hamburg-Eppendorf, D-20246 Hamburg, Germany"}]},{"given":"Joana","family":"Abrantes","sequence":"additional","affiliation":[{"name":"CIBIO-UP, Centro de Investiga\u00e7\u00e3o em Biodiversidade e Recursos Gen\u00e9ticos \u2013 Universidade do Porto, Campus Agr\u00e1rio de Vair\u00e3o, Rua Padre Armando Quintas, n\u00famero 7, 4485-661 Vair\u00e3o, Portugal"},{"name":"INSERM, U892, Universit\u00e9 de Nantes, 44007 Nantes, France"}]},{"given":"Pedro J.","family":"Esteves","sequence":"additional","affiliation":[{"name":"CIBIO-UP, Centro de Investiga\u00e7\u00e3o em Biodiversidade e Recursos Gen\u00e9ticos \u2013 Universidade do Porto, Campus Agr\u00e1rio de Vair\u00e3o, Rua Padre Armando Quintas, n\u00famero 7, 4485-661 Vair\u00e3o, Portugal"},{"name":"CITS, Centro de Investiga\u00e7\u00e3o em Tecnologias de Sa\u00fade, CESPU, 4585-116 Gandra, Portugal"}]},{"given":"Odete A. B.","family":"da Cruz e Silva","sequence":"additional","affiliation":[{"name":"Laboratory of Neurosciences, Centre for Cell Biology, Health Sciences Department and Biology Department, University of Aveiro, 3810-193 Aveiro, Portugal"}]},{"given":"Margarida","family":"Fardilha","sequence":"additional","affiliation":[{"name":"Laboratory of Signal Transduction, Centre for Cell Biology, Biology Department and Health Sciences Department, University of Aveiro, 3810-193 Aveiro, Portugal"}]},{"given":"Edgar F.","family":"da Cruz e Silva","sequence":"additional","affiliation":[{"name":"Laboratory of Signal Transduction, Centre for Cell Biology, Biology Department, University of Aveiro, 3810-193 Aveiro, Portugal"}]}],"member":"237","published-online":{"date-parts":[[2013,3,8]]},"reference":[{"key":"2021080923342907900_b1","doi-asserted-by":"publisher","first-page":"7187","DOI":"10.1073\/pnas.0401673101","article-title":"Phactrs 1\u20134: A family of protein phosphatase 1 and actin regulatory proteins.","volume":"101","author":"Allen","year":"2004","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"2021080923342907900_b2","doi-asserted-by":"publisher","first-page":"426","DOI":"10.1016\/S0968-0004(01)01836-9","article-title":"Combinatorial control of protein phosphatase-1.","volume":"26","author":"Bollen","year":"2001","journal-title":"Trends Biochem. Sci."},{"key":"2021080923342907900_b3","doi-asserted-by":"publisher","first-page":"187","DOI":"10.1042\/BJ20060600","article-title":"SARP, a new alternatively spliced protein phosphatase 1 and DNA interacting protein.","volume":"402","author":"Browne","year":"2007","journal-title":"Biochem. J."},{"key":"2021080923342907900_b4","doi-asserted-by":"publisher","first-page":"48002","DOI":"10.1074\/jbc.M208471200","article-title":"Protein phosphatase-1 binding to scd5p is important for regulation of actin organization and endocytosis in yeast.","volume":"277","author":"Chang","year":"2002","journal-title":"J. Biol. Chem."},{"key":"2021080923342907900_b5","doi-asserted-by":"crossref","first-page":"241","DOI":"10.1242\/jcs.115.2.241","article-title":"Protein phosphatase 1 \u2013 targeted in many directions.","volume":"115","author":"Cohen","year":"2002","journal-title":"J. Cell Sci."},{"key":"2021080923342907900_b6","doi-asserted-by":"crossref","first-page":"3375","DOI":"10.1523\/JNEUROSCI.15-05-03375.1995","article-title":"Differential expression of protein phosphatase 1 isoforms in mammalian brain.","volume":"15","author":"da Cruz e Silva","year":"1995","journal-title":"J. Neurosci."},{"key":"2021080923342907900_b7","doi-asserted-by":"publisher","first-page":"196","DOI":"10.1159\/000080986","article-title":"A model system to study intracellular trafficking and processing of the Alzheimer's amyloid precursor protein.","volume":"1","author":"da Cruz e Silva","year":"2004","journal-title":"Neurodegener. Dis."},{"key":"2021080923342907900_b8","doi-asserted-by":"publisher","first-page":"413","DOI":"10.1007\/s00418-011-0832-0","article-title":"Germ cells of male mice express genes for peroxisomal metabolic pathways implicated in the regulation of spermatogenesis and the protection against oxidative stress.","volume":"136","author":"Dastig","year":"2011","journal-title":"Histochem. Cell Biol."},{"key":"2021080923342907900_b9","doi-asserted-by":"publisher","first-page":"31107","DOI":"10.1074\/jbc.M803332200","article-title":"Targeting of hFis1 to peroxisomes is mediated by Pex19p.","volume":"283","author":"Delille","year":"2008","journal-title":"J. Biol. Chem."},{"key":"2021080923342907900_b10","doi-asserted-by":"publisher","first-page":"21666","DOI":"10.1074\/jbc.M313540200","article-title":"A novel Tctex2-related light chain is required for stability of inner dynein arm I1 and motor function in the Chlamydomonas flagellum.","volume":"279","author":"DiBella","year":"2004","journal-title":"J. Biol. Chem."},{"key":"2021080923342907900_b11","doi-asserted-by":"publisher","first-page":"5661","DOI":"10.1091\/mbc.E05-08-0732","article-title":"Differential light chain assembly influences outer arm dynein motor function.","volume":"16","author":"DiBella","year":"2005","journal-title":"Mol. Biol. Cell"},{"key":"2021080923342907900_b12","doi-asserted-by":"publisher","first-page":"468","DOI":"10.1196\/annals.1329.059","article-title":"Alternatively spliced protein variants as potential therapeutic targets for male infertility and contraception.","volume":"1030","author":"Fardilha","year":"2004","journal-title":"Ann. N. Y. Acad. Sci."},{"key":"2021080923342907900_b13","doi-asserted-by":"publisher","first-page":"196","DOI":"10.1196\/annals.1397.086","article-title":"Differential distribution of Alzheimer's amyloid precursor protein family variants in human sperm.","volume":"1096","author":"Fardilha","year":"2007","journal-title":"Ann. N. Y. Acad. Sci."},{"key":"2021080923342907900_b14","first-page":"39","article-title":"A import\u00e2ncia do mecanismo de \u201csplicing\u201d alternativo para a identifica\u00e7\u00e3o de novos alvos terap\u00eauticos. [Article in Portuguese].","volume":"25","author":"Fardilha","year":"2008","journal-title":"Acta Urol\u00f3gica"},{"key":"2021080923342907900_b15","doi-asserted-by":"publisher","first-page":"3996","DOI":"10.2174\/092986710793205363","article-title":"The physiological relevance of protein phosphatase 1 and its interacting proteins to health and disease.","volume":"17","author":"Fardilha","year":"2010","journal-title":"Curr. Med. Chem."},{"key":"2021080923342907900_b16","doi-asserted-by":"publisher","first-page":"466","DOI":"10.1093\/molehr\/gar004","article-title":"Protein phosphatase 1 complexes modulate sperm motility and present novel targets for male infertility.","volume":"17","author":"Fardilha","year":"2011","journal-title":"Mol. Hum. Reprod."},{"key":"2021080923342907900_b16a","doi-asserted-by":"publisher","first-page":"1403","DOI":"10.1016\/j.bcp.2011.02.018","article-title":"Identification of the human testis protein phosphatase 1 interactome.","volume":"82","author":"Fardilha","year":"2011","journal-title":"Biochem. Pharmacol."},{"key":"2021080923342907900_b18","doi-asserted-by":"publisher","first-page":"135","DOI":"10.1083\/jcb.147.1.135","article-title":"Cytoplasmic dynein is required for distinct aspects of Mtoc positioning, including centrosome separation, in the one cell stage Caenorhabditis elegans embryo.","volume":"147","author":"G\u00f6nczy","year":"1999","journal-title":"J. Cell Biol."},{"key":"2021080923342907900_b19","doi-asserted-by":"publisher","first-page":"1137","DOI":"10.1083\/jcb.140.5.1137","article-title":"Identification of the t complex-encoded cytoplasmic dynein light chain tctex1 in inner arm I1 supports the involvement of flagellar dyneins in meiotic drive.","volume":"140","author":"Harrison","year":"1998","journal-title":"J. Cell Biol."},{"key":"2021080923342907900_b20","doi-asserted-by":"publisher","first-page":"555","DOI":"10.1002\/(SICI)1521-1878(199807)20:7&lt;555::AID-BIES6&gt;3.0.CO;2-J","article-title":"Molecular mechanisms of male germ cell differentiation.","volume":"20","author":"Hecht","year":"1998","journal-title":"Bioessays"},{"key":"2021080923342907900_b21","doi-asserted-by":"publisher","first-page":"365","DOI":"10.1016\/j.chembiol.2009.02.012","article-title":"Docking motif-guided mapping of the interactome of protein phosphatase-1.","volume":"16","author":"Hendrickx","year":"2009","journal-title":"Chem. Biol."},{"key":"2021080923342907900_b22","doi-asserted-by":"publisher","first-page":"309","DOI":"10.2164\/jandrol.111.014167","article-title":"Control of messenger RNA fate by RNA-binding proteins: an emphasis on mammalian spermatogenesis.","volume":"33","author":"Idler","year":"2012","journal-title":"J. Androl."},{"key":"2021080923342907900_b23","doi-asserted-by":"publisher","first-page":"800","DOI":"10.1016\/S0006-291X(02)02303-3","article-title":"Dephosphorylation of Tctex2-related dynein light chain by type 2A protein phosphatase.","volume":"297","author":"Inaba","year":"2002","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"2021080923342907900_b24","doi-asserted-by":"publisher","first-page":"177","DOI":"10.1006\/bbrc.1999.0309","article-title":"Tctex2-related outer arm dynein light chain is phosphorylated at activation of sperm motility.","volume":"256","author":"Inaba","year":"1999","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"2021080923342907900_b25","doi-asserted-by":"publisher","first-page":"195","DOI":"10.1006\/jmbi.1999.3091","article-title":"Protein secondary structure prediction based on position-specific scoring matrices.","volume":"292","author":"Jones","year":"1999","journal-title":"J. Mol. Biol."},{"key":"2021080923342907900_b26","doi-asserted-by":"publisher","first-page":"594","DOI":"10.1016\/j.bbrc.2007.03.026","article-title":"Identification of phostensin, a PP1 F-actin cytoskeleton targeting subunit.","volume":"356","author":"Kao","year":"2007","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"2021080923342907900_b27","doi-asserted-by":"publisher","first-page":"32281","DOI":"10.1074\/jbc.271.50.32281","article-title":"The mouse t-complex-encoded protein Tctex-1 is a light chain of brain cytoplasmic dynein.","volume":"271","author":"King","year":"1996","journal-title":"J. Biol. Chem."},{"key":"2021080923342907900_b28","doi-asserted-by":"publisher","first-page":"5519","DOI":"10.1073\/pnas.90.12.5519","article-title":"A motility in the eukaryotic flagellum unrelated to flagellar beating.","volume":"90","author":"Kozminski","year":"1993","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"2021080923342907900_b29","doi-asserted-by":"publisher","first-page":"676","DOI":"10.1016\/j.bbrc.2009.07.086","article-title":"Phostensin caps to the pointed end of actin filaments and modulates actin dynamics.","volume":"387","author":"Lai","year":"2009","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"2021080923342907900_b30","doi-asserted-by":"publisher","first-page":"2947","DOI":"10.1093\/bioinformatics\/btm404","article-title":"Clustal W and Clustal X version 2.0.","volume":"23","author":"Larkin","year":"2007","journal-title":"Bioinformatics"},{"key":"2021080923342907900_b31","doi-asserted-by":"publisher","first-page":"313","DOI":"10.1677\/joe.1.06781","article-title":"Tumor necrosis factor \u03b1 reversibly disrupts the blood\u2013testis barrier and impairs Sertoli\u2013germ cell adhesion in the seminiferous epithelium of adult rat testes.","volume":"190","author":"Li","year":"2006","journal-title":"J. Endocrinol."},{"key":"2021080923342907900_b32","doi-asserted-by":"publisher","first-page":"12562","DOI":"10.1073\/pnas.1202316109","article-title":"Focal adhesion kinase-Tyr407 and -Tyr397 exhibit antagonistic effects on blood\u2013testis barrier dynamics in the rat.","volume":"109","author":"Lie","year":"2012","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"2021080923342907900_b33","doi-asserted-by":"publisher","first-page":"809","DOI":"10.1083\/jcb.201001006","article-title":"Regulated targeting of protein phosphatase 1 to the outer kinetochore by KNL1 opposes Aurora B kinase.","volume":"188","author":"Liu","year":"2010","journal-title":"J. Cell Biol."},{"key":"2021080923342907900_b34","doi-asserted-by":"publisher","first-page":"11205","DOI":"10.1074\/jbc.M611279200","article-title":"The DYNLT3 light chain directly links cytoplasmic dynein to a spindle checkpoint protein, Bub3.","volume":"282","author":"Lo","year":"2007","journal-title":"J. Biol. Chem."},{"key":"2021080923342907900_b35","doi-asserted-by":"publisher","first-page":"37069","DOI":"10.1074\/jbc.M608614200","article-title":"Identification of Tctex2\u03b2, a novel dynein light chain family member that interacts with different transforming growth factor-\u03b2 receptors.","volume":"281","author":"Meng","year":"2006","journal-title":"J. Biol. Chem."},{"key":"2021080923342907900_b36","doi-asserted-by":"publisher","first-page":"281","DOI":"10.1093\/emboj\/21.3.281","article-title":"Glycogen synthase kinase 3 phosphorylates kinesin light chains and negatively regulates kinesin-based motility.","volume":"21","author":"Morfini","year":"2002","journal-title":"EMBO J."},{"key":"2021080923342907900_b37","doi-asserted-by":"publisher","first-page":"2235","DOI":"10.1038\/sj.emboj.7600237","article-title":"A novel CDK5-dependent pathway for regulating GSK3 activity and kinesin-driven motility in neurons.","volume":"23","author":"Morfini","year":"2004","journal-title":"EMBO J."},{"key":"2021080923342907900_b38","doi-asserted-by":"publisher","first-page":"3396","DOI":"10.1073\/pnas.92.8.3396","article-title":"The alpha and gamma 1 isoforms of protein phosphatase 1 are highly and specifically concentrated in dendritic spines.","volume":"92","author":"Ouimet","year":"1995","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"2021080923342907900_b39","doi-asserted-by":"publisher","first-page":"1536","DOI":"10.1016\/S0960-9822(01)00475-4","article-title":"Cdc42, dynein, and dynactin regulate MTOC reorientation independent of Rho-regulated microtubule stabilization.","volume":"11","author":"Palazzo","year":"2001","journal-title":"Curr. Biol."},{"key":"2021080923342907900_b40","doi-asserted-by":"publisher","first-page":"1081","DOI":"10.1083\/jcb.137.5.1081","article-title":"A Chlamydomonas homologue of the putative murine t complex distorter Tctex-2 is an outer arm dynein light chain.","volume":"137","author":"Patel\u2013King","year":"1997","journal-title":"J. Cell Biol."},{"key":"2021080923342907900_b41","doi-asserted-by":"crossref","first-page":"3507","DOI":"10.1091\/mbc.10.10.3507","article-title":"LC2, the Chlamydomonas homologue of the t complex-encoded protein Tctex2, is essential for outer dynein arm assembly.","volume":"10","author":"Pazour","year":"1999","journal-title":"Mol. Biol. Cell"},{"key":"2021080923342907900_b42","doi-asserted-by":"publisher","first-page":"62","DOI":"10.1136\/jmg.2005.033001","article-title":"Identification of predicted human outer dynein arm genes: candidates for primary ciliary dyskinesia genes.","volume":"43","author":"Pazour","year":"2006","journal-title":"J. Med. Genet."},{"key":"2021080923342907900_b43","doi-asserted-by":"publisher","first-page":"3625","DOI":"10.1093\/nar\/gkg545","article-title":"ELM server: a new resource for investigating short functional sites in modular eukaryotic proteins.","volume":"31","author":"Puntervoll","year":"2003","journal-title":"Nucleic Acids Res."},{"key":"2021080923342907900_b44","doi-asserted-by":"publisher","first-page":"1065","DOI":"10.1016\/j.cub.2009.05.065","article-title":"Par3 and dynein associate to regulate local microtubule dynamics and centrosome orientation during migration.","volume":"19","author":"Schmoranzer","year":"2009","journal-title":"Curr. Biol."},{"key":"2021080923342907900_b45","doi-asserted-by":"publisher","first-page":"19639","DOI":"10.1074\/jbc.273.31.19639","article-title":"Localization of Tctex-1, a cytoplasmic dynein light chain, to the Golgi apparatus and evidence for dynein complex heterogeneity.","volume":"273","author":"Tai","year":"1998","journal-title":"J. Biol. Chem."},{"key":"2021080923342907900_b46","doi-asserted-by":"publisher","first-page":"877","DOI":"10.1016\/S0092-8674(00)80800-4","article-title":"Rhodopsin's carboxy-terminal cytoplasmic tail acts as a membrane receptor for cytoplasmic dynein by binding to the dynein light chain Tctex-1.","volume":"97","author":"Tai","year":"1999","journal-title":"Cell"},{"key":"2021080923342907900_b47","doi-asserted-by":"publisher","first-page":"2731","DOI":"10.1093\/molbev\/msr121","article-title":"MEGA5: molecular evolutionary genetics analysis using maximum likelihood, evolutionary distance, and maximum parsimony methods.","volume":"28","author":"Tamura","year":"2011","journal-title":"Mol. Biol. Evol."},{"key":"2021080923342907900_b48","doi-asserted-by":"publisher","first-page":"259","DOI":"10.2217\/14796694.5.2.259","article-title":"The TGF-\u03b2 paradox in human cancer: an update.","volume":"5","author":"Tian","year":"2009","journal-title":"Future Oncol."},{"key":"2021080923342907900_b49","doi-asserted-by":"publisher","first-page":"5537","DOI":"10.1093\/emboj\/16.18.5537","article-title":"Distinct roles of PP1 and PP2A-like phosphatases in control of microtubule dynamics during mitosis.","volume":"16","author":"Tournebize","year":"1997","journal-title":"EMBO J."},{"key":"2021080923342907900_b50","doi-asserted-by":"publisher","first-page":"10402","DOI":"10.1073\/pnas.0804102105","article-title":"Protein phosphatase 1 regulates the phosphorylation state of the polarity scaffold Par-3.","volume":"105","author":"Traweger","year":"2008","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"2021080923342907900_b51","doi-asserted-by":"publisher","first-page":"26171","DOI":"10.1074\/jbc.M102649200","article-title":"Cytoplasmic dynein intermediate chain phosphorylation regulates binding to dynactin.","volume":"276","author":"Vaughan","year":"2001","journal-title":"J. Biol. Chem."},{"key":"2021080923342907900_b52","doi-asserted-by":"publisher","first-page":"40","DOI":"10.1186\/1750-1326-5-40","article-title":"Retrieval of the Alzheimer's amyloid precursor protein from the endosome to the TGN is S655 phosphorylation state-dependent and retromer-mediated.","volume":"5","author":"Vieira","year":"2010","journal-title":"Mol. Neurodegener."},{"key":"2021080923342907900_b53","doi-asserted-by":"publisher","first-page":"709","DOI":"10.1095\/biolreprod54.3.709","article-title":"Sperm motility development in the epididymis is associated with decreased glycogen synthase kinase-3 and protein phosphatase 1 activity.","volume":"54","author":"Vijayaraghavan","year":"1996","journal-title":"Biol. Reprod."},{"key":"2021080923342907900_b54","doi-asserted-by":"publisher","first-page":"537","DOI":"10.1016\/j.molcel.2009.02.015","article-title":"From promiscuity to precision: protein phosphatases get a makeover.","volume":"33","author":"Virshup","year":"2009","journal-title":"Mol. Cell"},{"key":"2021080923342907900_b55","doi-asserted-by":"publisher","first-page":"377","DOI":"10.1042\/BJ20060758","article-title":"The translation initiation factor eIF2\u03b2 is an interactor of protein phosphatase-1.","volume":"400","author":"Wakula","year":"2006","journal-title":"Biochem. J."},{"key":"2021080923342907900_b56","doi-asserted-by":"publisher","first-page":"173","DOI":"10.1042\/BC20090091","article-title":"TLRR (lrrc67) interacts with PP1 and is associated with a cytoskeletal complex in the testis.","volume":"102","author":"Wang","year":"2010","journal-title":"Biol. Cell"},{"key":"2021080923342907900_b57","doi-asserted-by":"publisher","first-page":"819","DOI":"10.1083\/jcb.200804114","article-title":"Phosphorylation regulates targeting of cytoplasmic dynein to kinetochores during mitosis.","volume":"183","author":"Whyte","year":"2008","journal-title":"J. Cell Biol."},{"key":"2021080923342907900_b58","doi-asserted-by":"publisher","first-page":"569","DOI":"10.1002\/cm.20211","article-title":"Keeping an eye on I1: I1 dynein as a model for flagellar dynein assembly and regulation.","volume":"64","author":"Wirschell","year":"2007","journal-title":"Cell Motil. Cytoskeleton"},{"key":"2021080923342907900_b59","first-page":"4","article-title":"Collection and examination of human semen.","volume-title":"WHO Laboratory For Examination Of Human Semen And Sperm\u2013Cervical Mucus Interaction, 4th edition","author":"World Health Organization","year":"1999"},{"key":"2021080923342907900_b60","doi-asserted-by":"publisher","first-page":"26431","DOI":"10.1074\/jbc.M704969200","article-title":"Alternative splicing controls nuclear translocation of the cell cycle-regulated Nek2 kinase.","volume":"282","author":"Wu","year":"2007","journal-title":"J. Biol. Chem."},{"key":"2021080923342907900_b61","doi-asserted-by":"publisher","first-page":"321","DOI":"10.1016\/j.ydbio.2004.12.036","article-title":"TGF-\u03b23 regulates anchoring junction dynamics in the seminiferous epithelium of the rat testis via the Ras\/ERK signaling pathway: an in vivo study.","volume":"280","author":"Xia","year":"2005","journal-title":"Dev. Biol."},{"key":"2021080923342907900_b62","doi-asserted-by":"publisher","first-page":"469","DOI":"10.1016\/j.cytogfr.2005.05.007","article-title":"Cytokines and junction restructuring during spermatogenesis\u2014a lesson to learn from the testis.","volume":"16","author":"Xia","year":"2005","journal-title":"Cytokine Growth Factor Rev."},{"key":"2021080923342907900_b63","doi-asserted-by":"publisher","first-page":"16799","DOI":"10.1074\/jbc.M601618200","article-title":"Differential interactions between transforming growth factor-\u03b23\/T\u03b2R1, TAB1, and CD2AP disrupt blood-testis barrier and Sertoli-germ cell adhesion.","volume":"281","author":"Xia","year":"2006","journal-title":"J. Biol. Chem."},{"key":"2021080923342907900_b64","doi-asserted-by":"publisher","first-page":"48","DOI":"10.1016\/j.ydbio.2008.11.028","article-title":"TGF-\u03b23 and TNF\u03b1 perturb blood\u2013testis barrier (BTB) dynamics by accelerating the clathrin-mediated endocytosis of integral membrane proteins: a new concept of BTB regulation during spermatogenesis.","volume":"327","author":"Xia","year":"2009","journal-title":"Dev. Biol."},{"key":"2021080923342907900_b65","doi-asserted-by":"crossref","first-page":"91","DOI":"10.1242\/jcs.113.1.91","article-title":"Protein phosphatases PP1 and PP2A are located in distinct positions in the Chlamydomonas flagellar axoneme.","volume":"113","author":"Yang","year":"2000","journal-title":"J. Cell Sci."}],"container-title":["Biology Open"],"original-title":[],"language":"en","link":[{"URL":"http:\/\/journals.logists.com\/bio\/bio\/article-pdf\/2\/5\/453\/2098464\/bio-02-05-453.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"syndication"},{"URL":"http:\/\/journals.logists.com\/bio\/bio\/article-pdf\/2\/5\/453\/2098464\/bio-02-05-453.pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2021,8,10]],"date-time":"2021-08-10T00:20:10Z","timestamp":1628554810000},"score":1,"resource":{"primary":{"URL":"https:\/\/journals.biologists.com\/bio\/article\/2\/5\/453\/19834\/TCTEX1D4-a-novel-protein-phosphatase-1-interactor"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2013,3,8]]},"references-count":65,"journal-issue":{"issue":"5","published-print":{"date-parts":[[2013,5,15]]}},"URL":"https:\/\/doi.org\/10.1242\/bio.20131065","relation":{},"ISSN":["2046-6390"],"issn-type":[{"value":"2046-6390","type":"electronic"}],"subject":[],"published":{"date-parts":[[2013,3,8]]}}}