Characterization of PISP, a novel single-PDZ protein that binds to all plasma membrane Ca2+-ATPase b-splice variants

Geoffrey M. Goellner, Steven J. DeMarco, Emanuel E. Strehler

Research output: Contribution to journalArticle

50 Scopus citations

Abstract

Plasma membrane Ca2+ ATPases (PMCAs) maintain intracellular Ca2+ homeostasis and participate in the local regulation of Ca2+ signaling. Spatially separate demands for Ca2+ regulation require proper membrane targeting of PMCAs, but the mechanism of PMCA targeting is unknown. Using the PMCA2b carboxyl-terminal tail as yeast two-hybrid bait, we isolated a novel PDZ domain-containing protein from a human brain cDNA library. This protein, named PISP for PMCA-interacting single-PDZ protein, consists of 140 amino acids and contains little else besides a single PDZ domain. Pulldown experiments showed that PISP interacts with all PMCA b-splice forms. PISP was found to be ubiquitously expressed and, in MDCK cells, was present in a punctate pattern throughout the cytosol and at the basolateral membrane. When added to microsomal membranes expressing PMCA4b, PISP was unable to stimulate the PMCA-dependent ATPase activity. Our data suggest that PISP is a transiently interacting partner of the PMCA b-splice forms that may play a role in their sorting to or from the plasma membrane.

Original languageEnglish (US)
Pages (from-to)461-471
Number of pages11
JournalAnnals of the New York Academy of Sciences
Volume986
DOIs
StatePublished - Jan 1 2003

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Keywords

  • Calcium pump
  • PDZ domain
  • PMCA
  • Plasma membrane Ca-ATPase

ASJC Scopus subject areas

  • Neuroscience(all)
  • Biochemistry, Genetics and Molecular Biology(all)
  • History and Philosophy of Science

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