The interaction between endogenous calcineurin and the plasma membrane calcium-dependent ATPase is isoform specific in breast cancer cells

被引：34

作者：

Holton, Marylouisa

Yang, Di

Wang, Weiguang

Mohamed, Tamer M. A.

Neyses, Ludwig

Armesilla, Angel L.

机构：

[1] Wolverhampton Univ, Sch Appl Sci, Res Inst Healthcare Sci, Mol Pharmacol Grp, Wolverhampton WV1 1SB, England

[2] Wolverhampton Univ, Sch Appl Sci, Res Inst Healthcare Sci, Oncol Grp, Wolverhampton WV1 1SB, England

[3] Univ Manchester, Div Cardiol, Manchester M13 9PT, Lancs, England

来源：

FEBS LETTERS | 2007年 / 581卷 / 21期

基金：

英国医学研究理事会;

关键词：

PMCA; calcineurin; interaction; MCF-7; signalling; NFAT;

D O I：

10.1016/j.febslet.2007.07.054

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 [生物化学与分子生物学]; 081704 [应用化学];

摘要：

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.

引用

页码：4115 / 4119

页数：5

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