Reference : The interaction between endogenous calcineurin and the plasma membrane calcium-depend...
Scientific journals : Article
Human health sciences : Oncology
http://hdl.handle.net/10993/18308
The interaction between endogenous calcineurin and the plasma membrane calcium-dependent ATPase is isoform specific in breast cancer cells.
English
Holton, Marylouisa [> >]
Yang, Di [> >]
Wang, Weiguang [> >]
Mohamed, Tamer M. A. [> >]
Neyses, Ludwig mailto [University of Luxembourg > Research Office]
Armesilla, Angel L. [> >]
2007
FEBS letters
581
21
4115-9
Yes (verified by ORBilu)
International
0014-5793
Netherlands
[en] Breast Neoplasms/enzymology ; Calcineurin/metabolism ; Calmodulin/metabolism ; Cell Line, Tumor ; Cell Membrane/enzymology ; Humans ; Isoenzymes/metabolism ; NFATC Transcription Factors/metabolism ; Neoplasm Proteins/metabolism ; Plasma Membrane Calcium-Transporting ATPases/metabolism ; Protein Binding ; Protein Structure, Tertiary ; Signal Transduction
[en] 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.
http://hdl.handle.net/10993/18308
10.1016/j.febslet.2007.07.054
http://www.sciencedirect.com/science/article/pii/S0014579307008319

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