{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,25]],"date-time":"2026-09-25T09:50:06Z","timestamp":1790329806655,"version":"4.1.0"},"reference-count":32,"publisher":"American Society for Cell Biology (ASCB)","issue":"11","content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["MBoC"],"published-print":{"date-parts":[[2005,11]]},"abstract":"<jats:p>Polycystin-1 (PC-1) is the product of the PKD1 gene, which is mutated in autosomal dominant polycystic kidney disease. We show that the Na,K-ATPase \u03b1-subunit interacts in vitro and in vivo with the final 200 amino acids of the polycystin-1 protein, which constitute its cytoplasmic C-terminal tail. Functional studies suggest that this association may play a role in the regulation of the Na,K-ATPase activity. Chinese hamster ovary cells stably expressing the entire PC-1 protein exhibit a dramatic increase in Na,K-ATPase activity, although the kinetic properties of the enzyme remain unchanged. These data indicate that polycystin-1 may contribute to the regulation of Na,K-ATPase activity in kidneys in situ, thus modulating renal tubular fluid and electrolyte transport.<\/jats:p>","DOI":"10.1091\/mbc.e05-03-0200","type":"journal-article","created":{"date-parts":[[2005,8,18]],"date-time":"2005-08-18T00:34:00Z","timestamp":1124325240000},"page":"5087-5093","source":"Crossref","is-referenced-by-count":29,"title":["The C-Terminal Tail of the Polycystin-1 Protein Interacts with the Na,K-ATPase \u03b1-Subunit"],"prefix":"10.1091","volume":"16","author":[{"given":"Alessandra","family":"Zatti","sequence":"first","affiliation":[{"name":"Department of Cellular and Molecular Physiology, Yale University School of Medicine, New Haven, CT 06510"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Veronique","family":"Chauvet","sequence":"additional","affiliation":[{"name":"Department of Cellular and Molecular Physiology, Yale University School of Medicine, New Haven, CT 06510"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Vanathy","family":"Rajendran","sequence":"additional","affiliation":[{"name":"Department of Cellular and Molecular Physiology, Yale University School of Medicine, New Haven, CT 06510"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Thoru","family":"Kimura","sequence":"additional","affiliation":[{"name":"Department of Cellular and Molecular Physiology, Yale University School of Medicine, New Haven, CT 06510"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Phillip","family":"Pagel","sequence":"additional","affiliation":[{"name":"Department of Cellular and Molecular Physiology, Yale University School of Medicine, New Haven, CT 06510"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Michael J.","family":"Caplan","sequence":"additional","affiliation":[{"name":"Department of Cellular and Molecular Physiology, Yale University School of Medicine, New Haven, CT 06510"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"1076","reference":[{"key":"REF1","doi-asserted-by":"crossref","unstructured":"Arnould, T., Kim, E., Tsiokas, L., Jochimsen, F., Gruning, W., Chang, J. D., and Walz, G. (1998). 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.J. Biol. Chem.273, 6013\u20136018.","DOI":"10.1074\/jbc.273.11.6013"},{"key":"REF2","doi-asserted-by":"crossref","unstructured":"Blostein, R., Dunbar, L., Mense, M., Scanzano, R., Wilczynska, A., and Caplan, M. J. (1999). Cation selectivity of gastric H,K-ATPase and Na,K-ATPase chimeras.J. Biol. Chem.275, 18374\u201318381.","DOI":"10.1074\/jbc.274.26.18374"},{"key":"REF3","doi-asserted-by":"crossref","unstructured":"Brill, S. R., Ross, K. E., Davidow, C. J., Ye, M., Grantham, J. J., and Caplan, M. J. (1996). Immunolocalization of ion transport proteins in human autosomal dominant polycystic kidney epithelial cells.Proc. Natl. Acad. Sci. USA93, 10206\u201310211.","DOI":"10.1073\/pnas.93.19.10206"},{"key":"REF4","doi-asserted-by":"crossref","unstructured":"Chauvet, V.et al. (2002). 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J., Ye, M., Gattone V. H., 2nd, and Sullivan, L. P. (1995). In vitro fluid secretion by epithelium from polycystic kidneys.J. Clin. Investig.95, 195\u2013202.","DOI":"10.1172\/JCI117638"},{"key":"REF12","doi-asserted-by":"crossref","unstructured":"Grimm, D. H., Cai, Y., Chauvet, V., Rajendran, V., Zeltner, R., Geng, L., Avner, E. D., Sweeney, W., Somlo, S., and Caplan, M. J. (2003). Polycystin-1 distribution is modulated by polycystin-2 expression in mammalian cells.J. Biol. Chem.278, 36786\u201336793.","DOI":"10.1074\/jbc.M306536200"},{"key":"REF13","doi-asserted-by":"crossref","unstructured":"Ibraghimov-Beskrovnaya, O.et al. (1997). Polycystin: in vitro synthesis, in vivo tissue expression, and subcellular localization identifies a large membrane-associated protein.Proc. Natl. Acad. Sci. 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A role for Na\/K adenosine triphosphatase in the pathogenesis of cyst formation in experimental polycystic kidney disease.J. Lab. Clin. Med.129, 517\u2013526.","DOI":"10.1016\/S0022-2143(97)90006-8"},{"key":"REF24","doi-asserted-by":"crossref","unstructured":"Thomson, R. B., Mentone, S., Kim, R., Earle, K., Delpire., E., Somlo, S., and Aronson, P. S. (2003) Histopathological analysis of renal cystic epithelia in the Pkd2WS25\/mouse model of ADPKD.Am. J. Physiol.285, F870\u2013F880.","DOI":"10.1152\/ajprenal.00153.2003"},{"key":"REF25","doi-asserted-by":"crossref","unstructured":"Toyoshima, C., Nakasako, M., Nomura, H., and Ogawa, H. (2000). Crystal structure of the calcium pump of sarcoplasmic reticulum at 2.6 A resolution.Nature405, 647\u2013655.","DOI":"10.1038\/35015017"},{"key":"REF26","doi-asserted-by":"crossref","unstructured":"Toyoshima, C., Nomura, H., and Tsuda, T. (2004). 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The isolated polycystin-1 cytoplasmic COOH terminus prolongs ATP-stimulated Cl\u2013conductance through increased Ca2+ entry.Am. J. Physiol.285, F1168\u2013F1178.","DOI":"10.1152\/ajprenal.00171.2003"},{"key":"REF30","doi-asserted-by":"crossref","unstructured":"Wilson, P. D. (2004a). Polycystic kidney disease: new understanding in the pathogenesis.Int J. Biochem. Cell Biol.36, 1868\u20131873.","DOI":"10.1016\/j.biocel.2004.03.012"},{"key":"REF31","doi-asserted-by":"crossref","unstructured":"Wilson, P. D. (2004b). Polycystic kidney disease.N. Engl. J. Med.350, 151\u2013164.","DOI":"10.1056\/NEJMra022161"},{"key":"REF32","doi-asserted-by":"crossref","unstructured":"Wilson, P. D., Devuyst, O., Li, X., Gatti, L., Falkenstein, D., Robinson, S., Fambrough, D., and Burrow, C. R. (2000). Apical plasma membrane mispolarization of NaK-ATPase in polycystic kidney disease epithelia is associated with aberrant expression of the beta2 isoform.Am. J. 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