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NF-AT activation requires suppression of Crm1-dependent export by calcineurin

Author

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  • Jiangyu Zhu

    (Harvard Medical School)

  • Frank McKeon

    (Harvard Medical School)

Abstract

Nuclear import of the NF-AT transcription factors during T-cell activation requires the calcium-activated phosphatase calcineurin, which unmasks nuclear-location signals on NF-AT (1–5). We show here that the nuclear import of NF-ATs is not sufficient to activate NF-AT target genes, as NF-ATs are subject to a futile cycling across the nuclear envelope owing to engagement with the exportin protein Crm1 (6–8). Calcineurin suppresses this futile cycling by a non-catalytic mechanism involving the masking of nuclear export signals on NF-AT targeted by Crm1. This clustering of binding sites for calcineurin and Crm1 on NF-AT establishes an inherent competition between these molecules that imparts exquisite calcium sensitivity to the shuttling dynamics of the NF-AT transcription factors. Such a balance between nuclear import and export may regulate the action of other transcription factors.

Suggested Citation

  • Jiangyu Zhu & Frank McKeon, 1999. "NF-AT activation requires suppression of Crm1-dependent export by calcineurin," Nature, Nature, vol. 398(6724), pages 256-260, March.
    • Handle: RePEc:nat:nature:v:398:y:1999:i:6724:d:10.1038_18473
    DOI: 10.1038/18473
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