The C-terminal tail of the polycystin-1 protein interacts with the Na,K-ATPase alpha-subunit |
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Authors: | Zatti Alessandra Chauvet Veronique Rajendran Vanathy Kimura Thoru Pagel Phillip Caplan Michael J |
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Institution: | Department of Cellular and Molecular Physiology, Yale University School of Medicine, New Haven, CT 06510, USA. |
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Abstract: | 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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