The interaction between endogenous calcineurin and the plasma membrane calcium-dependent ATPase is isoform specific in breast cancer cells
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Abstract
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.Citation
FEBS Letters, 581(21): 4115-4119Publisher
ElsevierJournal
FEBS LettersPubMed ID
17689535Additional Links
http://www.febsletters.org/article/S0014-5793(07)00831-9/abstractType
Journal articleLanguage
enISSN
0014-5793ae974a485f413a2113503eed53cd6c53
10.1016/j.febslet.2007.07.054
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