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The interaction between endogenous calcineurin and the plasma membrane calcium-dependent ATPase is isoform specific in breast cancer cells
Holton, Marylouisa Yang, Di Wang, Weiguang Mohamed, Tamer M. A. Neyses, Ludwig
Holton, Marylouisa
Yang, Di
Wang, Weiguang
Mohamed, Tamer M. A.
Neyses, Ludwig
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Issue Date
2007
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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): 4115-4119
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Journal
Research Unit
PubMed ID
17689535
PubMed Central ID
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Journal article
Language
en
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ISSN
0014-5793