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    The sarcolemmal calcium pump inhibits the calcineurin/nuclear factor of activated T-cell pathway via interaction with the calcineurin A catalytic subunit.

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    Authors
    Buch, Mamta H.
    Pickard, Adam
    Rodriguez, Antonio
    Gillies, Sheona
    Maass, Alexander H.
    Emerson, Michael
    Cartwright, Elizabeth J.
    Williams, Judith C.
    Oceandy, Delvac
    Redondo, Juan Miguel
    Neyses, Ludwig
    Armesilla, Angel Luis
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    Issue Date
    2005
    
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    Abstract
    The calcineurin/nuclear factor of activated T-cell (NFAT) pathway represents a crucial transducer of cellular function. There is increasing evidence placing the sarcolemmal calcium pump, or plasma membrane calcium/calmodulin ATPase pump (PMCA), as a potential modulator of signal transduction pathways. We demonstrate a novel interaction between PMCA and the calcium/calmodulin-dependent phosphatase, calcineurin, in mammalian cells. The interaction domains were located to the catalytic domain of PMCA4b and the catalytic domain of the calcineurin A subunit. Endogenous calcineurin activity, assessed by measuring the transcriptional activity of its best characterized substrate, NFAT, was significantly inhibited by 60% in the presence of ectopic PMCA4b. This inhibition was notably reversed by the co-expression of the PMCA4b interaction domain, demonstrating the functional significance of this interaction. PMCA4b was, however, unable to confer its inhibitory effect in the presence of a calcium/calmodulin-independent constitutively active mutant calcineurin A suggesting a calcium/calmodulin-dependent mechanism. The modulatory function of PMCA4b is further supported by the observation that endogenous calcineurin moves from the cytoplasm to the plasma membrane when PMCA4b is overexpressed. We suggest recruitment by PMCA4b of calcineurin to a low calcium environment as a possible explanation for these findings. In summary, our results offer strong evidence for a novel functional interaction between PMCA and calcineurin, suggesting a role for PMCA as a negative modulator of calcineurin-mediated signaling pathways in mammalian cells. This study reinforces the emerging role of PMCA as a molecular organizer and regulator of signaling transduction pathways.
    Citation
    The Journal of Biological Chemistry, 280(33): 29479-29487
    Publisher
    American Society for Biochemistry and Molecular Biology
    URI
    http://hdl.handle.net/2436/7700
    DOI
    10.1074/jbc.M501326200
    PubMed ID
    15955804
    Additional Links
    http://www.jbc.org/cgi/reprint/280/33/29479
    Type
    Journal article
    Language
    en
    ISSN
    0021-9258
    ae974a485f413a2113503eed53cd6c53
    10.1074/jbc.M501326200
    Scopus Count
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    Research Institute in Healthcare Science

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