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Originally published as MBC in Press, 10.1091/mbc.E05-03-0200 on August 17, 2005

Vol. 16, Issue 11, 5087-5093, November 2005

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The C-Terminal Tail of the Polycystin-1 Protein Interacts with the Na,K-ATPase {alpha}-Subunit

Alessandra Zatti, Veronique Chauvet, Vanathy Rajendran, Thoru Kimura, Phillip Pagel, and Michael J. Caplan

Department of Cellular and Molecular Physiology, Yale University School of Medicine, New Haven, CT 06510

Submitted March 10, 2005; Revised July 21, 2005; Accepted August 8, 2005
Monitoring Editor: Guido Guidotti

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 {alpha}-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.

This article was published online ahead of print in MBC in Press (http://www.molbiolcell.org/cgi/doi/10.1091/mbc.E05–03–0200) on August 17, 2005.

Abbreviations used: ADPKD, autosomal dominant polycystic kidney disease; CHO, Chinese hamster ovary; MDCK, Madin-Darby canine kidney; HA, hemagglutinin; PBS, phosphate-buffered saline; PC-1, polycystin-1.

Address correspondence to: Michael J. Caplan (michael.caplan{at}yale.edu).




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