Journal
MOLECULAR BIOLOGY OF THE CELL
Volume 16, Issue 11, Pages 5087-5093Publisher
AMER SOC CELL BIOLOGY
DOI: 10.1091/mbc.E05-03-0200
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Funding
- NIDDK NIH HHS [DK-57328, P50 DK057328] Funding Source: Medline
- NIGMS NIH HHS [R01 GM042136, GM-42136] Funding Source: Medline
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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.
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