The C-terminal tail of the polycystin-1 protein interacts with the Na,K-ATPase alpha-subunit

Mol Biol Cell. 2005 Nov;16(11):5087-93. doi: 10.1091/mbc.e05-03-0200. Epub 2005 Aug 17.

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.

Publication types

  • Research Support, N.I.H., Extramural

MeSH terms

  • Animals
  • CHO Cells / ultrastructure
  • Cell Line
  • Cricetinae
  • Cricetulus
  • Dogs
  • Enzyme Inhibitors
  • Escherichia
  • Mutation
  • Ouabain / pharmacology*
  • Polycystic Kidney Diseases
  • Proteins*
  • Recombinant Proteins
  • Sodium / pharmacology*
  • Sodium-Potassium-Exchanging ATPase / biosynthesis
  • Sodium-Potassium-Exchanging ATPase / drug effects
  • Sodium-Potassium-Exchanging ATPase / metabolism*
  • Sodium-Potassium-Exchanging ATPase / physiology*
  • TRPP Cation Channels
  • Transfection

Substances

  • Enzyme Inhibitors
  • Proteins
  • Recombinant Proteins
  • TRPP Cation Channels
  • polycystic kidney disease 1 protein
  • Ouabain
  • Sodium
  • Sodium-Potassium-Exchanging ATPase