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Wolverhampton Intellectual Repository and E-Theses > Research Institutes > Research Institute in Healthcare Science > Molecular Pharmacology Research Group > The interaction between endogenous calcineurin and the plasma membrane calcium-dependent ATPase is isoform specific in breast cancer cells

Please use this identifier to cite or link to this item: http://hdl.handle.net/2436/33739
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Title: The interaction between endogenous calcineurin and the plasma membrane calcium-dependent ATPase is isoform specific in breast cancer cells
Authors: Holton, Marylouisa
Yang, Di
Wang, Weiguang
Mohamed, Tamer M. A.
Neyses, Ludwig
Armesilla, Angel Luis
Citation: FEBS Letters, 581(21): 4115-4119
Publisher: Elsevier
Journal: FEBS Letters
Issue Date: 2007
URI: http://hdl.handle.net/2436/33739
DOI: 10.1016/j.febslet.2007.07.054
PubMed ID: 17689535
Additional Links: http://www.febsletters.org/article/S0014-5793(07)00831-9/abstract
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.
Type: Article
Language: en
Keywords: PMCA
Calcineurin
Interaction
MCF-7
Signalling
NFAT
MeSH: Breast Neoplasms
Calcineurin
Calmodulin
Cell Line, Tumor
Cell Membrane
Humans
Isoenzymes
NFATC Transcription Factors
Neoplasm Proteins
Plasma Membrane Calcium-Transporting ATPases
Protein Binding
Protein Structure, Tertiary
Signal Transduction
ISSN: 0014-5793
Appears in Collections: Molecular Pharmacology Research Group

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