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The interaction between endogenous calcineurin and the plasma membrane calcium‐dependent ATPase is isoform specific in breast cancer cells
Author(s) -
Holton Marylouisa,
Yang Di,
Wang Weiguang,
Mohamed Tamer M.A.,
Neyses Ludwig,
Armesilla Angel L.
Publication year - 2007
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2007.07.054
Subject(s) - calcineurin , endogeny , gene isoform , calcium , atpase , plasma membrane ca2+ atpase , chemistry , membrane , breast cancer , cancer , biochemistry , microbiology and biotechnology , enzyme , biology , medicine , transplantation , organic chemistry , gene
Plasma membrane calcium/calmodulin‐dependent ATPases (PMCAs) are high affinity calcium pumps that extrude calcium from the cell. Emerging evidence suggests a novel role for PMCAs as regulators of calcium/calmodulin‐dependent signal transduction pathways via interaction with specific partner proteins. In this work, we demonstrate that endogenous human PMCA2 and ‐4 both interact with the signal transduction phosphatase, calcineurin, whereas, no interaction was detected with PMCA1. The strongest interaction was observed between PMCA2 and calcineurin. The domain of PMCA2 involved in the interaction is equivalent to that reported for PMCA4b. PMCA2–calcineurin interaction results in inhibition of the calcineurin/nuclear factor of activated T‐cells signalling pathway.