期刊
FEBS LETTERS
卷 581, 期 21, 页码 4115-4119出版社
WILEY
DOI: 10.1016/j.febslet.2007.07.054
关键词
PMCA; calcineurin; interaction; MCF-7; signalling; NFAT
资金
- MRC [G0500025] Funding Source: UKRI
- Medical Research Council [G0500025] Funding Source: Medline
- Medical Research Council [G0500025] Funding Source: researchfish
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. (c) 2007 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
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