{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,5,8]],"date-time":"2026-05-08T21:40:48Z","timestamp":1778276448654,"version":"3.51.4"},"reference-count":98,"publisher":"Elsevier BV","issue":"10","license":[{"start":{"date-parts":[[2011,10,1]],"date-time":"2011-10-01T00:00:00Z","timestamp":1317427200000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2011,10,1]],"date-time":"2011-10-01T00:00:00Z","timestamp":1317427200000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/legal\/tdmrep-license"},{"start":{"date-parts":[[2013,7,18]],"date-time":"2013-07-18T00:00:00Z","timestamp":1374105600000},"content-version":"vor","delay-in-days":656,"URL":"http:\/\/www.elsevier.com\/open-access\/userlicense\/1.0\/"},{"start":{"date-parts":[[2011,10,1]],"date-time":"2011-10-01T00:00:00Z","timestamp":1317427200000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-017"},{"start":{"date-parts":[[2011,10,1]],"date-time":"2011-10-01T00:00:00Z","timestamp":1317427200000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-037"},{"start":{"date-parts":[[2011,10,1]],"date-time":"2011-10-01T00:00:00Z","timestamp":1317427200000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-012"},{"start":{"date-parts":[[2011,10,1]],"date-time":"2011-10-01T00:00:00Z","timestamp":1317427200000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-029"},{"start":{"date-parts":[[2011,10,1]],"date-time":"2011-10-01T00:00:00Z","timestamp":1317427200000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-004"}],"funder":[{"name":"The National Kidney Research Fund (now Kidney Research UK)"},{"name":"The Wellcome Trust, NIDDK","award":["R01 DK50141"],"award-info":[{"award-number":["R01 DK50141"]}]},{"DOI":"10.13039\/100001296","name":"PKD Foundation","doi-asserted-by":"crossref","award":["12(A-C)2R"],"award-info":[{"award-number":["12(A-C)2R"]}],"id":[{"id":"10.13039\/100001296","id-type":"DOI","asserted-by":"crossref"}]},{"name":"NIH","award":["DK P0162345"],"award-info":[{"award-number":["DK P0162345"]}]},{"name":"NIH-NCI","award":["5R24 CA095823-04"],"award-info":[{"award-number":["5R24 CA095823-04"]}]},{"name":"NSF Major Research Instrumentation","award":["DBI-9724504"],"award-info":[{"award-number":["DBI-9724504"]}]},{"name":"NIH shared instrumentation","award":["1 S10 RR0 9145-01"],"award-info":[{"award-number":["1 S10 RR0 9145-01"]}]}],"content-domain":{"domain":["elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease"],"published-print":{"date-parts":[[2011,10]]},"DOI":"10.1016\/j.bbadis.2010.11.006","type":"journal-article","created":{"date-parts":[[2010,11,30]],"date-time":"2010-11-30T06:01:41Z","timestamp":1291096901000},"page":"1225-1238","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":17,"title":["Receptor protein tyrosine phosphatases are novel components of a polycystin complex"],"prefix":"10.1016","volume":"1812","author":[{"given":"Catherine A.","family":"Boucher","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Heather H.","family":"Ward","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Ruth L.","family":"Case","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Katie S.","family":"Thurston","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Xiaohong","family":"Li","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Andrew","family":"Needham","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Elsa","family":"Romero","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Deborah","family":"Hyink","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Seema","family":"Qamar","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Tamara","family":"Roitbak","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Samantha","family":"Powell","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Christopher","family":"Ward","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Patricia D.","family":"Wilson","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Angela","family":"Wandinger-Ness","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Richard N.","family":"Sandford","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"78","reference":[{"key":"10.1016\/j.bbadis.2010.11.006_bb0005","doi-asserted-by":"crossref","first-page":"467","DOI":"10.1016\/S0888-7543(11)80001-7","article-title":"Autosomal dominant polycystic kidney disease: localization of the second gene to chromosome 4q13-q23","volume":"18","author":"Kimberling","year":"1993","journal-title":"Genomics"},{"key":"10.1016\/j.bbadis.2010.11.006_bb0010","doi-asserted-by":"crossref","first-page":"359","DOI":"10.1038\/ng1293-359","article-title":"Chromosome 4 localization of a second gene for autosomal dominant polycystic kidney disease","volume":"5","author":"Peters","year":"1993","journal-title":"Nat. Genet."},{"key":"10.1016\/j.bbadis.2010.11.006_bb0015","first-page":"925","article-title":"Identification of a locus which shows no genetic recombination with the autosomal dominant polycystic kidney disease gene on chromosome 16","volume":"46","author":"Germino","year":"1990","journal-title":"Am. J. Hum. Genet."},{"key":"10.1016\/j.bbadis.2010.11.006_bb0020","doi-asserted-by":"crossref","first-page":"150","DOI":"10.1016\/0888-7543(88)90146-2","article-title":"Regional localization of the autosomal dominant polycystic kidney disease locus","volume":"3","author":"Reeders","year":"1988","journal-title":"Genomics"},{"key":"10.1016\/j.bbadis.2010.11.006_bb0025","doi-asserted-by":"crossref","first-page":"129","DOI":"10.1038\/ng1076","article-title":"Polycystins 1 and 2 mediate mechanosensation in the primary cilium of kidney cells","volume":"33","author":"Nauli","year":"2003","journal-title":"Nat. Genet."},{"key":"10.1016\/j.bbadis.2010.11.006_bb0030","doi-asserted-by":"crossref","first-page":"F930","DOI":"10.1152\/ajprenal.00285.2006","article-title":"Human ADPKD primary cyst epithelial cells with a novel, single codon deletion in the PKD1 gene exhibit defective ciliary polycystin localization and loss of flow-induced Ca2+ signaling","volume":"292","author":"Xu","year":"2007","journal-title":"Am. J. Physiol. Ren. Physiol."},{"key":"10.1016\/j.bbadis.2010.11.006_bb0035","doi-asserted-by":"crossref","first-page":"2724","DOI":"10.1681\/ASN.2004110913","article-title":"Increased activity of activator protein-1 transcription factor components ATF2, c-Jun, and c-Fos in human and mouse autosomal dominant polycystic kidney disease","volume":"16","author":"Le","year":"2005","journal-title":"J. Am. Soc. Nephrol."},{"key":"10.1016\/j.bbadis.2010.11.006_bb0040","doi-asserted-by":"crossref","first-page":"19566","DOI":"10.1074\/jbc.M201875200","article-title":"Polycystin-1 activation of c-Jun N-terminal kinase and AP-1 is mediated by heterotrimeric G proteins","volume":"277","author":"Parnell","year":"2002","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bbadis.2010.11.006_bb0045","doi-asserted-by":"crossref","first-page":"1267","DOI":"10.1016\/S1097-2765(00)00123-4","article-title":"Polycystin-1, the gene product of PKD1, induces resistance to apoptosis and spontaneous tubulogenesis in MDCK cells","volume":"6","author":"Boletta","year":"2000","journal-title":"Mol. Cell"},{"key":"10.1016\/j.bbadis.2010.11.006_bb0050","doi-asserted-by":"crossref","first-page":"481","DOI":"10.1172\/JCI0212867","article-title":"The polycystin-1 C-terminal fragment triggers branching morphogenesis and migration of tubular kidney epithelial cells","volume":"109","author":"Nickel","year":"2002","journal-title":"J. Clin. Invest."},{"key":"10.1016\/j.bbadis.2010.11.006_bb0055","doi-asserted-by":"crossref","first-page":"151","DOI":"10.1038\/ng0695-151","article-title":"The polycystic kidney disease 1 (PKD1) gene encodes a novel protein with multiple cell recognition domains","volume":"10","author":"Hughes","year":"1995","journal-title":"Nat. Genet."},{"key":"10.1016\/j.bbadis.2010.11.006_bb0060","doi-asserted-by":"crossref","first-page":"21","DOI":"10.1016\/S0925-4439(00)00079-X","article-title":"Modification of the composition of polycystin-1 multiprotein complexes by calcium and tyrosine phosphorylation","volume":"1535","author":"Geng","year":"2000","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1016\/j.bbadis.2010.11.006_bb0065","doi-asserted-by":"crossref","first-page":"356","DOI":"10.1006\/bbrc.1999.0780","article-title":"Identification of phosphorylation sites in the PKD1-encoded protein C-terminal domain","volume":"259","author":"Li","year":"1999","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"10.1016\/j.bbadis.2010.11.006_bb0070","doi-asserted-by":"crossref","first-page":"1483","DOI":"10.1093\/hmg\/6.9.1483","article-title":"Comparative analysis of the polycystic kidney disease 1 (PKD1) gene reveals an integral membrane glycoprotein with multiple evolutionary conserved domains","volume":"6","author":"Sandford","year":"1997","journal-title":"Hum. Mol. Genet."},{"key":"10.1016\/j.bbadis.2010.11.006_bb0075","doi-asserted-by":"crossref","first-page":"179","DOI":"10.1038\/ng0697-179","article-title":"PKD1 interacts with PKD2 through a probable coiled-coil domain","volume":"16","author":"Qian","year":"1997","journal-title":"Nat. Genet."},{"key":"10.1016\/j.bbadis.2010.11.006_bb0080","first-page":"1311","article-title":"The PKD1 gene product, \u201cpolycystin-1,\u201d is a tyrosine-phosphorylated protein that colocalizes with alpha2beta1-integrin in focal clusters in adherent renal epithelia","volume":"79","author":"Wilson","year":"1999","journal-title":"Lab. Invest."},{"key":"10.1016\/j.bbadis.2010.11.006_bb0085","doi-asserted-by":"crossref","first-page":"297","DOI":"10.1093\/emboj\/18.2.297","article-title":"The structure of a PKD domain from polycystin-1: implications for polycystic kidney disease","volume":"18","author":"Bycroft","year":"1999","journal-title":"EMBO J."},{"key":"10.1016\/j.bbadis.2010.11.006_bb0090","doi-asserted-by":"crossref","first-page":"861","DOI":"10.1016\/j.jmb.2005.04.008","article-title":"The remarkable mechanical strength of polycystin-1 supports a direct role in mechanotransduction","volume":"349","author":"Forman","year":"2005","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.bbadis.2010.11.006_bb0095","doi-asserted-by":"crossref","first-page":"1421","DOI":"10.1053\/ajkd.2001.29282","article-title":"Biochemical characterization of bona fide polycystin-1 in vitro and in vivo","volume":"38","author":"Boletta","year":"2001","journal-title":"Am. J. Kidney Dis."},{"key":"10.1016\/j.bbadis.2010.11.006_bb0100","doi-asserted-by":"crossref","first-page":"12174","DOI":"10.1073\/pnas.211191098","article-title":"Cardiovascular, skeletal, and renal defects in mice with a targeted disruption of the Pkd1 gene","volume":"98","author":"Boulter","year":"2001","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.bbadis.2010.11.006_bb0105","doi-asserted-by":"crossref","first-page":"179","DOI":"10.1016\/S0925-4773(00)00257-4","article-title":"Distinct and common developmental expression patterns of the murine Pkd2 and Pkd1 genes","volume":"93","author":"Guillaume","year":"2000","journal-title":"Mech. Dev."},{"key":"10.1016\/j.bbadis.2010.11.006_bb0110","doi-asserted-by":"crossref","first-page":"219","DOI":"10.1016\/j.yexcr.2003.08.019","article-title":"Altered distribution and co-localization of polycystin-2 with polycystin-1 in MDCK cells after wounding stress","volume":"292","author":"Scheffers","year":"2004","journal-title":"Exp. Cell Res."},{"key":"10.1016\/j.bbadis.2010.11.006_bb0115","doi-asserted-by":"crossref","first-page":"F1153","DOI":"10.1152\/ajprenal.00008.2005","article-title":"Mispolarization of desmosomal proteins and altered intercellular adhesion in autosomal dominant polycystic kidney disease","volume":"288","author":"Silberberg","year":"2005","journal-title":"Am. J. Physiol. Ren. Physiol."},{"key":"10.1016\/j.bbadis.2010.11.006_bb0120","doi-asserted-by":"crossref","first-page":"151","DOI":"10.1056\/NEJMra022161","article-title":"Polycystic kidney disease","volume":"350","author":"Wilson","year":"2004","journal-title":"N. Engl. J. Med."},{"key":"10.1016\/j.bbadis.2010.11.006_bb0125","doi-asserted-by":"crossref","first-page":"990","DOI":"10.1038\/35050128","article-title":"Co-assembly of polycystin-1 and -2 produces unique cation-permeable currents","volume":"408","author":"Hanaoka","year":"2000","journal-title":"Nature"},{"key":"10.1016\/j.bbadis.2010.11.006_bb0130","doi-asserted-by":"crossref","first-page":"124","DOI":"10.1042\/BST0350124","article-title":"TRP channels and kidney disease: lessons from polycystic kidney disease","volume":"35","author":"Qamar","year":"2007","journal-title":"Biochem. Soc. Trans."},{"key":"10.1016\/j.bbadis.2010.11.006_bb0135","doi-asserted-by":"crossref","first-page":"441","DOI":"10.1038\/nrneph.2009.100","article-title":"The role of transient receptor potential channels in kidney disease","volume":"5","author":"Woudenberg-Vrenken","year":"2009","journal-title":"Nat. Rev. Nephrol."},{"key":"10.1016\/j.bbadis.2010.11.006_bb0140","doi-asserted-by":"crossref","first-page":"1459","DOI":"10.1172\/JCI5111","article-title":"Polycystin-1, the PKD1 gene product, is in a complex containing E-cadherin and the catenins","volume":"104","author":"Huan","year":"1999","journal-title":"J. Clin. Invest."},{"key":"10.1016\/j.bbadis.2010.11.006_bb0145","doi-asserted-by":"crossref","first-page":"1334","DOI":"10.1091\/mbc.e03-05-0296","article-title":"A polycystin-1 multiprotein complex is disrupted in polycystic kidney disease cells","volume":"15","author":"Roitbak","year":"2004","journal-title":"Mol. Biol. Cell"},{"key":"10.1016\/j.bbadis.2010.11.006_bb0150","doi-asserted-by":"crossref","first-page":"2508","DOI":"10.1097\/01.ASN.0000029587.47950.25","article-title":"The polycystic kidney disease proteins, polycystin-1, polycystin-2, polaris, and cystin, are co-localized in renal cilia","volume":"13","author":"Yoder","year":"2002","journal-title":"J. Am. Soc. Nephrol."},{"key":"10.1016\/j.bbadis.2010.11.006_bb0155","doi-asserted-by":"crossref","first-page":"2743","DOI":"10.1093\/hmg\/9.18.2743","article-title":"Polycystin-1, the product of the polycystic kidney disease 1 gene, co-localizes with desmosomes in MDCK cells","volume":"9","author":"Scheffers","year":"2000","journal-title":"Hum. Mol. Genet."},{"key":"10.1016\/j.bbadis.2010.11.006_bb0160","doi-asserted-by":"crossref","first-page":"10173","DOI":"10.1074\/jbc.274.15.10173","article-title":"Phosphorylation and free pool of beta-catenin are regulated by tyrosine kinases and tyrosine phosphatases during epithelial cell migration","volume":"274","author":"Muller","year":"1999","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bbadis.2010.11.006_bb0165","doi-asserted-by":"crossref","first-page":"1733","DOI":"10.1002\/j.1460-2075.1992.tb05225.x","article-title":"The effect of tyrosine-specific protein phosphorylation on the assembly of adherens-type junctions","volume":"11","author":"Volberg","year":"1992","journal-title":"EMBO J."},{"key":"10.1016\/j.bbadis.2010.11.006_bb0170","doi-asserted-by":"crossref","first-page":"29","DOI":"10.1042\/BJ20050645","article-title":"A polycystin multiprotein complex constitutes a cholesterol-containing signalling microdomain in human kidney epithelia","volume":"392","author":"Roitbak","year":"2005","journal-title":"Biochem. J."},{"key":"10.1016\/j.bbadis.2010.11.006_bb0175","doi-asserted-by":"crossref","first-page":"8285","DOI":"10.1128\/MCB.25.18.8285-8298.2005","article-title":"PKD2 functions as an epidermal growth factor-activated plasma membrane channel","volume":"25","author":"Ma","year":"2005","journal-title":"Mol. Cell. Biol."},{"key":"10.1016\/j.bbadis.2010.11.006_bb0180","doi-asserted-by":"crossref","first-page":"C487","DOI":"10.1152\/ajpcell.1995.269.2.C487","article-title":"Abnormal polarization of EGF receptors and autocrine stimulation of cyst epithelial growth in human ADPKD","volume":"269","author":"Du","year":"1995","journal-title":"Am. J. Physiol."},{"key":"10.1016\/j.bbadis.2010.11.006_bb0185","first-page":"F387","article-title":"Functional activity of epidermal growth factor receptors in autosomal recessive polycystic kidney disease","volume":"275","author":"Sweeney","year":"1998","journal-title":"Am. J. Physiol."},{"key":"10.1016\/j.bbadis.2010.11.006_bb0190","doi-asserted-by":"crossref","first-page":"647","DOI":"10.1016\/j.bbadis.2006.04.006","article-title":"Inhibition of HER-2(neu\/ErbB2) restores normal function and structure to polycystic kidney disease (PKD) epithelia","volume":"1762","author":"Wilson","year":"2006","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1016\/j.bbadis.2010.11.006_bb0195","doi-asserted-by":"crossref","first-page":"2328","DOI":"10.1093\/hmg\/ddp165","article-title":"Systems biology of autosomal dominant polycystic kidney disease (ADPKD): computational identification of gene expression pathways and integrated regulatory networks","volume":"18","author":"Song","year":"2009","journal-title":"Hum. Mol. Genet."},{"key":"10.1016\/j.bbadis.2010.11.006_bb0200","doi-asserted-by":"crossref","first-page":"1573","DOI":"10.1046\/j.1523-1755.2003.00256.x","article-title":"EGF receptor tyrosine kinase inhibition attenuates the development of PKD in Han:SPRD rats","volume":"64","author":"Torres","year":"2003","journal-title":"Kidney Int."},{"key":"10.1016\/j.bbadis.2010.11.006_bb0205","doi-asserted-by":"crossref","first-page":"637","DOI":"10.1681\/ASN.2005050534","article-title":"Polycystin-1 induces resistance to apoptosis through the phosphatidylinositol 3-kinase\/Akt signaling pathway","volume":"17","author":"Boca","year":"2006","journal-title":"J. Am. Soc. Nephrol."},{"key":"10.1016\/j.bbadis.2010.11.006_bb0210","doi-asserted-by":"crossref","first-page":"55455","DOI":"10.1074\/jbc.M402905200","article-title":"Polycystin-1 activates the calcineurin\/NFAT (nuclear factor of activated T-cells) signaling pathway","volume":"279","author":"Puri","year":"2004","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bbadis.2010.11.006_bb0215","doi-asserted-by":"crossref","first-page":"5466","DOI":"10.1073\/pnas.0509694103","article-title":"The mTOR pathway is regulated by polycystin-1, and its inhibition reverses renal cystogenesis in polycystic kidney disease","volume":"103","author":"Shillingford","year":"2006","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.bbadis.2010.11.006_bb0220","doi-asserted-by":"crossref","first-page":"27472","DOI":"10.1074\/jbc.M312183200","article-title":"Aberrant polycystin-1 expression results in modification of activator protein-1 activity, whereas Wnt signaling remains unaffected","volume":"279","author":"Le","year":"2004","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bbadis.2010.11.006_bb0225","doi-asserted-by":"crossref","first-page":"46","DOI":"10.1681\/ASN.2004080660","article-title":"Rapamycin markedly slows disease progression in a rat model of polycystic kidney disease","volume":"16","author":"Tao","year":"2005","journal-title":"J. Am. Soc. Nephrol."},{"key":"10.1016\/j.bbadis.2010.11.006_bb0230","doi-asserted-by":"crossref","first-page":"598","DOI":"10.1093\/ndt\/gfi181","article-title":"Inhibition of mTOR with sirolimus slows disease progression in Han:SPRD rats with autosomal dominant polycystic kidney disease (ADPKD)","volume":"21","author":"Wahl","year":"2006","journal-title":"Nephrol. Dial. Transplant."},{"key":"10.1016\/j.bbadis.2010.11.006_bb0235","doi-asserted-by":"crossref","first-page":"19987","DOI":"10.1074\/jbc.M312031200","article-title":"Calcium dependence of polycystin-2 channel activity is modulated by phosphorylation at Ser812","volume":"279","author":"Cai","year":"2004","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bbadis.2010.11.006_bb0240","doi-asserted-by":"crossref","first-page":"1342","DOI":"10.1681\/ASN.2007070730","article-title":"The subcellular localization of TRPP2 modulates its function","volume":"19","author":"Fu","year":"2008","journal-title":"J. Am. Soc. Nephrol."},{"key":"10.1016\/j.bbadis.2010.11.006_bb0245","doi-asserted-by":"crossref","first-page":"11520","DOI":"10.1074\/jbc.M211061200","article-title":"Regulation of a transient receptor potential (TRP) channel by tyrosine phosphorylation. SRC family kinase-dependent tyrosine phosphorylation of TRPV4 on TYR-253 mediates its response to hypotonic stress","volume":"278","author":"Xu","year":"2003","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bbadis.2010.11.006_bb0250","doi-asserted-by":"crossref","first-page":"861","DOI":"10.1016\/j.bbrc.2007.10.103","article-title":"Kidney injury molecule 1 (Kim1) is a novel ciliary molecule and interactor of polycystin 2","volume":"364","author":"Kuehn","year":"2007","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"10.1016\/j.bbadis.2010.11.006_bb0255","doi-asserted-by":"crossref","first-page":"21","DOI":"10.1038\/ng1701","article-title":"Defective planar cell polarity in polycystic kidney disease","volume":"38","author":"Fischer","year":"2006","journal-title":"Nat. Genet."},{"key":"10.1016\/j.bbadis.2010.11.006_bb0260","doi-asserted-by":"crossref","first-page":"321","DOI":"10.1146\/annurev.med.60.101707.125712","article-title":"Polycystic kidney disease","volume":"60","author":"Harris","year":"2009","journal-title":"Annu. Rev. Med."},{"key":"10.1016\/j.bbadis.2010.11.006_bb0265","doi-asserted-by":"crossref","first-page":"107","DOI":"10.1111\/j.1399-0004.2008.01148.x","article-title":"Cystic kidney diseases and planar cell polarity signaling","volume":"75","author":"Bacallao","year":"2009","journal-title":"Clin. Genet."},{"key":"10.1016\/j.bbadis.2010.11.006_bb0270","doi-asserted-by":"crossref","first-page":"699","DOI":"10.1016\/j.cell.2004.05.018","article-title":"Protein tyrosine phosphatases in the human genome","volume":"117","author":"Alonso","year":"2004","journal-title":"Cell"},{"key":"10.1016\/j.bbadis.2010.11.006_bb0275","doi-asserted-by":"crossref","first-page":"664","DOI":"10.1139\/o04-120","article-title":"Functional significance of the LAR receptor protein tyrosine phosphatase family in development and diseases","volume":"82","author":"Chagnon","year":"2004","journal-title":"Biochem. Cell Biol."},{"key":"10.1016\/j.bbadis.2010.11.006_bb0280","doi-asserted-by":"crossref","first-page":"3917","DOI":"10.1128\/MCB.26.10.3917-3934.2006","article-title":"Furin-, ADAM 10-, and gamma-secretase-mediated cleavage of a receptor tyrosine phosphatase and regulation of beta-catenin's transcriptional activity","volume":"26","author":"Anders","year":"2006","journal-title":"Mol. Cell. Biol."},{"key":"10.1016\/j.bbadis.2010.11.006_bb0285","doi-asserted-by":"crossref","first-page":"11686","DOI":"10.1073\/pnas.92.25.11686","article-title":"The LAR\/PTP delta\/PTP sigma subfamily of transmembrane protein-tyrosine-phosphatases: multiple human LAR, PTP delta, and PTP sigma isoforms are expressed in a tissue-specific manner and associate with the LAR-interacting protein LIP.1","volume":"92","author":"Pulido","year":"1995","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.bbadis.2010.11.006_bb0290","doi-asserted-by":"crossref","first-page":"47263","DOI":"10.1074\/jbc.M205810200","article-title":"Intra- and intermolecular interactions between intracellular domains of receptor protein-tyrosine phosphatases","volume":"277","author":"Blanchetot","year":"2002","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bbadis.2010.11.006_bb0295","doi-asserted-by":"crossref","first-page":"1519","DOI":"10.1083\/jcb.134.6.1519","article-title":"Association between a transmembrane protein tyrosine phosphatase and the cadherin-catenin complex","volume":"134","author":"Kypta","year":"1996","journal-title":"J. Cell Biol."},{"key":"10.1016\/j.bbadis.2010.11.006_bb0300","doi-asserted-by":"crossref","first-page":"1680","DOI":"10.1073\/pnas.94.5.1680","article-title":"Development of \u201csubstrate-trapping\u201d mutants to identify physiological substrates of protein tyrosine phosphatases","volume":"94","author":"Flint","year":"1997","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.bbadis.2010.11.006_bb0305","doi-asserted-by":"crossref","first-page":"208","DOI":"10.1128\/MCB.00707-06","article-title":"N-cadherin is an in vivo substrate for protein tyrosine phosphatase sigma (PTPsigma) and participates in PTPsigma-mediated inhibition of axon growth","volume":"27","author":"Siu","year":"2007","journal-title":"Mol. Cell. Biol."},{"key":"10.1016\/j.bbadis.2010.11.006_bb0310","doi-asserted-by":"crossref","first-page":"19","DOI":"10.1677\/joe.1.06069","article-title":"Protein tyrosine phosphatases and signalling","volume":"185","author":"Stoker","year":"2005","journal-title":"J. Endocrinol."},{"key":"10.1016\/j.bbadis.2010.11.006_bb0315","doi-asserted-by":"crossref","first-page":"681","DOI":"10.1016\/S1044-7431(03)00120-9","article-title":"Receptor protein tyrosine phosphatase sigma inhibits axonal regeneration and the rate of axon extension","volume":"23","author":"Thompson","year":"2003","journal-title":"Mol. Cell. Neurosci."},{"key":"10.1016\/j.bbadis.2010.11.006_bb0320","doi-asserted-by":"crossref","first-page":"814","DOI":"10.1681\/ASN.V115814","article-title":"Cellular and subcellular distribution of polycystin-2, the protein product of the PKD2 gene","volume":"11","author":"Foggensteiner","year":"2000","journal-title":"J. Am. Soc. Nephrol."},{"key":"10.1016\/j.bbadis.2010.11.006_bb0325","doi-asserted-by":"crossref","first-page":"1524","DOI":"10.1073\/pnas.93.4.1524","article-title":"Polycystin, the polycystic kidney disease 1 protein, is expressed by epithelial cells in fetal, adult, and polycystic kidney","volume":"93","author":"Ward","year":"1996","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.bbadis.2010.11.006_bb0330","doi-asserted-by":"crossref","first-page":"2353","DOI":"10.1242\/jcs.107.9.2353","article-title":"The role of the cytoplasmic domain in regulating CD44 function","volume":"107","author":"Isacke","year":"1994","journal-title":"J. Cell Sci."},{"key":"10.1016\/j.bbadis.2010.11.006_bb0335","doi-asserted-by":"crossref","first-page":"F397","DOI":"10.1152\/ajprenal.00310.2002","article-title":"Immortalized epithelial cells from human autosomal dominant polycystic kidney cysts","volume":"285","author":"Loghman-Adham","year":"2003","journal-title":"Am. J. Physiol. Ren. Physiol."},{"key":"10.1016\/j.bbadis.2010.11.006_bb0340","doi-asserted-by":"crossref","first-page":"1015","DOI":"10.1681\/ASN.2005080830","article-title":"Loss of polycystin-1 in human cyst-lining epithelia leads to ciliary dysfunction","volume":"17","author":"Nauli","year":"2006","journal-title":"J. Am. Soc. Nephrol."},{"key":"10.1016\/j.bbadis.2010.11.006_bb0345","doi-asserted-by":"crossref","first-page":"111","DOI":"10.1083\/jcb.149.1.111","article-title":"Compromised cytoarchitecture and polarized trafficking in autosomal dominant polycystic kidney disease cells","volume":"149","author":"Charron","year":"2000","journal-title":"J. Cell Biol."},{"key":"10.1016\/j.bbadis.2010.11.006_bb0350","doi-asserted-by":"crossref","first-page":"C213","DOI":"10.1152\/ajpcell.2002.282.1.C213","article-title":"Voxx: a PC-based, near real-time volume rendering system for biological microscopy","volume":"282","author":"Clendenon","year":"2002","journal-title":"Am. J. Physiol. Cell Physiol."},{"key":"10.1016\/j.bbadis.2010.11.006_bb0355","doi-asserted-by":"crossref","first-page":"9792","DOI":"10.1074\/jbc.275.13.9792","article-title":"Identification of tyrosine phosphatases that dephosphorylate the insulin receptor. A brute force approach based on \u201csubstrate-trapping\u201d mutants","volume":"275","author":"Walchli","year":"2000","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bbadis.2010.11.006_bb0360","doi-asserted-by":"crossref","first-page":"16","DOI":"10.1016\/j.ydbio.2005.06.034","article-title":"Disruption of polycystin-1 function interferes with branching morphogenesis of the ureteric bud in developing mouse kidneys","volume":"286","author":"Polgar","year":"2005","journal-title":"Dev. Biol."},{"key":"10.1016\/j.bbadis.2010.11.006_bb0365","doi-asserted-by":"crossref","first-page":"2608","DOI":"10.1128\/MCB.18.5.2608","article-title":"The second catalytic domain of protein tyrosine phosphatase delta (PTP delta) binds to and inhibits the first catalytic domain of PTP sigma","volume":"18","author":"Wallace","year":"1998","journal-title":"Mol. Cell. Biol."},{"key":"10.1016\/j.bbadis.2010.11.006_bb0370","first-page":"F602","article-title":"Polycystin expression is temporally and spatially regulated during renal development","volume":"272","author":"Van Adelsberg","year":"1997","journal-title":"Am. J. Physiol."},{"key":"10.1016\/j.bbadis.2010.11.006_bb0375","doi-asserted-by":"crossref","first-page":"347","DOI":"10.1038\/sj.ejhg.5201162","article-title":"Autosomal dominant polycystic kidney disease (ADPKD, MIM 173900, PKD1 and PKD2 genes, protein products known as polycystin-1 and polycystin-2)","volume":"12","author":"Boucher","year":"2004","journal-title":"Eur. J. Hum. Genet."},{"key":"10.1016\/j.bbadis.2010.11.006_bb0380","doi-asserted-by":"crossref","first-page":"513","DOI":"10.1042\/bj20020381","article-title":"Expression of the leucocyte common antigen-related (LAR) tyrosine phosphatase is regulated by cell density through functional E-cadherin complexes","volume":"365","author":"Symons","year":"2002","journal-title":"Biochem. J."},{"key":"10.1016\/j.bbadis.2010.11.006_bb0385","doi-asserted-by":"crossref","first-page":"4069","DOI":"10.1038\/sj.onc.1202794","article-title":"The transmembrane protein tyrosine phosphatase RPTPsigma modulates signaling of the epidermal growth factor receptor in A431 cells","volume":"18","author":"Suarez Pestana","year":"1999","journal-title":"Oncogene"},{"key":"10.1016\/j.bbadis.2010.11.006_bb0390","doi-asserted-by":"crossref","first-page":"21729","DOI":"10.1074\/jbc.M703218200","article-title":"Characterization of cis-autoproteolysis of polycystin-1, the product of human polycystic kidney disease 1 gene","volume":"282","author":"Wei","year":"2007","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bbadis.2010.11.006_bb0395","doi-asserted-by":"crossref","first-page":"8698","DOI":"10.1073\/pnas.86.22.8698","article-title":"A family of receptor-linked protein tyrosine phosphatases in humans and Drosophila","volume":"86","author":"Streuli","year":"1989","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.bbadis.2010.11.006_bb0400","doi-asserted-by":"crossref","first-page":"650","DOI":"10.1016\/0955-0674(95)80106-5","article-title":"Protein tyrosine phosphatases as adhesion receptors","volume":"7","author":"Brady-Kalnay","year":"1995","journal-title":"Curr. Opin. Cell Biol."},{"key":"10.1016\/j.bbadis.2010.11.006_bb0405","doi-asserted-by":"crossref","first-page":"611","DOI":"10.1016\/S0092-8674(00)81036-3","article-title":"The transmembrane tyrosine phosphatase DLAR controls motor axon guidance in Drosophila","volume":"84","author":"Krueger","year":"1996","journal-title":"Cell"},{"key":"10.1016\/j.bbadis.2010.11.006_bb0410","doi-asserted-by":"crossref","first-page":"193","DOI":"10.1016\/S0955-0674(97)80063-4","article-title":"Protein tyrosine phosphatases in signal transduction","volume":"9","author":"Neel","year":"1997","journal-title":"Curr. Opin. Cell Biol."},{"key":"10.1016\/j.bbadis.2010.11.006_bb0415","doi-asserted-by":"crossref","first-page":"437","DOI":"10.1038\/74805","article-title":"A sodium channel signaling complex: modulation by associated receptor protein tyrosine phosphatase beta","volume":"3","author":"Ratcliffe","year":"2000","journal-title":"Nat. Neurosci."},{"key":"10.1016\/j.bbadis.2010.11.006_bb0420","doi-asserted-by":"crossref","first-page":"143","DOI":"10.1083\/jcb.200211061","article-title":"RPTP-alpha acts as a transducer of mechanical force on alphav\/beta3-integrin-cytoskeleton linkages","volume":"161","author":"Von Wichert","year":"2003","journal-title":"J. Cell Biol."},{"key":"10.1016\/j.bbadis.2010.11.006_bb0425","doi-asserted-by":"crossref","first-page":"5106","DOI":"10.1128\/MCB.00101-06","article-title":"Receptor protein tyrosine phosphatase gamma is a marker for pyramidal cells and sensory neurons in the nervous system and is not necessary for normal development","volume":"26","author":"Lamprianou","year":"2006","journal-title":"Mol. Cell. Biol."},{"key":"10.1016\/j.bbadis.2010.11.006_bb0430","doi-asserted-by":"crossref","first-page":"2443","DOI":"10.1073\/pnas.0911235107","article-title":"The protein tyrosine phosphatases PTPRZ and PTPRG bind to distinct members of the contactin family of neural recognition molecules","volume":"107","author":"Bouyain","year":"2010","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.bbadis.2010.11.006_bb0435","doi-asserted-by":"crossref","first-page":"5872","DOI":"10.1523\/JNEUROSCI.0386-06.2006","article-title":"Mammalian motoneuron axon targeting requires receptor protein tyrosine phosphatases sigma and delta","volume":"26","author":"Uetani","year":"2006","journal-title":"J. Neurosci."},{"key":"10.1016\/j.bbadis.2010.11.006_bb0440","doi-asserted-by":"crossref","first-page":"905","DOI":"10.1681\/ASN.2004121083","article-title":"Kinesin family member 12 is a candidate polycystic kidney disease modifier in the cpk mouse","volume":"16","author":"Mrug","year":"2005","journal-title":"J. Am. Soc. Nephrol."},{"key":"10.1016\/j.bbadis.2010.11.006_bb0445","doi-asserted-by":"crossref","first-page":"681","DOI":"10.1083\/jcb.138.3.681","article-title":"Cellular redistribution of protein tyrosine phosphatases LAR and PTPsigma by inducible proteolytic processing","volume":"138","author":"Aicher","year":"1997","journal-title":"J. Cell Biol."},{"key":"10.1016\/j.bbadis.2010.11.006_bb0450","doi-asserted-by":"crossref","first-page":"F1034","DOI":"10.1152\/ajprenal.00195.2003","article-title":"Murine models of polycystic kidney disease: molecular and therapeutic insights","volume":"285","author":"Guay-Woodford","year":"2003","journal-title":"Am. J. Physiol. Ren. Physiol."},{"key":"10.1016\/j.bbadis.2010.11.006_bb0455","doi-asserted-by":"crossref","first-page":"693","DOI":"10.1016\/j.cell.2004.05.019","article-title":"Cilia and flagella revealed: from flagellar assembly in Chlamydomonas to human obesity disorders","volume":"117","author":"Snell","year":"2004","journal-title":"Cell"},{"key":"10.1016\/j.bbadis.2010.11.006_bb0460","doi-asserted-by":"crossref","first-page":"1881","DOI":"10.1128\/MCB.22.6.1881-1892.2002","article-title":"Heparan sulfate proteoglycans are ligands for receptor protein tyrosine phosphatase sigma","volume":"22","author":"Aricescu","year":"2002","journal-title":"Mol. Cell. Biol."},{"key":"10.1016\/j.bbadis.2010.11.006_bb0465","doi-asserted-by":"crossref","first-page":"e6","DOI":"10.1126\/scisignal.3110pe6","article-title":"A new role for RPTPsigma in spinal cord injury: signaling chondroitin sulfate proteoglycan inhibition","volume":"3","author":"Duan","year":"2010","journal-title":"Sci. Signal."},{"key":"10.1016\/j.bbadis.2010.11.006_bb0470","doi-asserted-by":"crossref","first-page":"1299","DOI":"10.1074\/mcp.M700054-MCP200","article-title":"The proteome of the mouse photoreceptor sensory cilium complex","volume":"6","author":"Liu","year":"2007","journal-title":"Mol. Cell. Proteomics"},{"key":"10.1016\/j.bbadis.2010.11.006_bb0475","doi-asserted-by":"crossref","first-page":"11543","DOI":"10.1523\/JNEUROSCI.1743-07.2007","article-title":"Sites and molecular mechanisms of modulation of Na(v)1.2 channels by Fyn tyrosine kinase","volume":"27","author":"Beacham","year":"2007","journal-title":"J. Neurosci."},{"key":"10.1016\/j.bbadis.2010.11.006_bb0480","doi-asserted-by":"crossref","first-page":"539","DOI":"10.1006\/bbrc.1999.0810","article-title":"Identification of the major site of in vitro PKA phosphorylation in the polycystin-1C-terminal cytosolic domain","volume":"259","author":"Parnell","year":"1999","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"10.1016\/j.bbadis.2010.11.006_bb0485","doi-asserted-by":"crossref","first-page":"625","DOI":"10.1006\/bbrc.1998.9514","article-title":"The polycystic kidney disease-1 protein, polycystin-1, binds and activates heterotrimeric G-proteins in vitro","volume":"251","author":"Parnell","year":"1998","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"10.1016\/j.bbadis.2010.11.006_bb0490","doi-asserted-by":"crossref","first-page":"6013","DOI":"10.1074\/jbc.273.11.6013","article-title":"The polycystic kidney disease 1 gene product mediates protein kinase C alpha-dependent and c-Jun N-terminal kinase-dependent activation of the transcription factor AP-1","volume":"273","author":"Arnould","year":"1998","journal-title":"J. Biol. Chem."}],"container-title":["Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0925443910002619?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0925443910002619?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2025,10,14]],"date-time":"2025-10-14T04:38:24Z","timestamp":1760416704000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0925443910002619"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2011,10]]},"references-count":98,"journal-issue":{"issue":"10","published-print":{"date-parts":[[2011,10]]}},"alternative-id":["S0925443910002619"],"URL":"https:\/\/doi.org\/10.1016\/j.bbadis.2010.11.006","relation":{},"ISSN":["0925-4439"],"issn-type":[{"value":"0925-4439","type":"print"}],"subject":[],"published":{"date-parts":[[2011,10]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Receptor protein tyrosine phosphatases are novel components of a polycystin complex","name":"articletitle","label":"Article Title"},{"value":"Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.bbadis.2010.11.006","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"Copyright \u00a9 2010 Elsevier B.V. All rights reserved.","name":"copyright","label":"Copyright"}]}}