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

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    Authors
    Holton, Marylouisa
    Yang, Di
    Wang, Weiguang
    Mohamed, Tamer M. A.
    Neyses, Ludwig
    Armesilla, Angel cc
    Issue Date
    2007
    
    Metadata
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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
    Publisher
    Elsevier
    Journal
    FEBS Letters
    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
    Type
    Journal article
    Language
    en
    ISSN
    0014-5793
    ae974a485f413a2113503eed53cd6c53
    10.1016/j.febslet.2007.07.054
    Scopus Count
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    Research Institute in Healthcare Science

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