Suppression of signalling through transcription factor NF-AT by interactions between calcineurin and Bcl-2 View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

1997-04

AUTHORS

F Shibasaki, E Kondo, T Akagi, F McKeon

ABSTRACT

It is not known how the protein Bcl-2 inhibits cell death induced by calcium signalling and growth-factor withdrawal. Here we report that Bcl-2 forms a tight complex with calcineurin, resulting in the targeting of calcineurin to Bcl-2 sites on cytoplasmic membranes, and show that this interaction is dependent on the BH4 domain of Bcl-2. Calcineurin bound to Bcl-2 is an active phosphatase but is unable to promote the nuclear translocation of NF-AT, a transcription-factor required for induction of interleukin-2 expression, suggesting a mechanism by which Bcl-2 suppresses NF-AT activity. We also show that Bax, a pro-apoptotic member of the Bcl-2 family, interferes with interactions between calcineurin and Bcl-2. We propose that the ability of Bcl-2 to block NF-AT signalling is due to the sequestering of active calcineurin to the same domain of Bcl-2 which associates with Rad-1 (ref. 5), and that calcineurin may act in Bcl-2-regulated functions. More... »

PAGES

728-731

Journal

TITLE

Nature

ISSUE

6626

VOLUME

386

Author Affiliations

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  • Identifiers

    URI

    http://scigraph.springernature.com/pub.10.1038/386728a0

    DOI

    http://dx.doi.org/10.1038/386728a0

    DIMENSIONS

    https://app.dimensions.ai/details/publication/pub.1048327456

    PUBMED

    https://www.ncbi.nlm.nih.gov/pubmed/9109491


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