期刊
MOLECULAR AND CELLULAR BIOLOGY
卷 20, 期 2, 页码 702-712出版社
AMER SOC MICROBIOLOGY
DOI: 10.1128/MCB.20.2.702-712.2000
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资金
- NCI NIH HHS [R01 CA065861, CA65861, CA72009, P01 CA072009] Funding Source: Medline
- NATIONAL CANCER INSTITUTE [P01CA072009, R01CA065861] Funding Source: NIH RePORTER
Calcium-stimulated nuclear factor of activated T cells (NFAT) transcription activity at the interleukin-2 promoter is negatively regulated by cyclic AMP (cAMP), This effect of cAMP is mediated, in part, by protein kinase A phosphorylation of NFAT. The mechanism of regulation involves the creation of a phosphorylation-dependent binding site for 14-3-3. Decreased NFAT phosphorylation caused by the calcium-stimulated phosphatase calcineurin, or mutation of the PKA phosphorylation sites, disrupted 14-3-3 binding and increased NFAT transcription activity, In contrast, NFAT phosphorylation caused by cAMP increased 14-3-3 binding and reduced NFAT transcription activity. The regulated interaction between NFAT and 14-3-3 provides a mechanism for the integration of calcium and cAMP signaling pathways.
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