期刊
MOLECULAR AND CELLULAR BIOLOGY
卷 23, 期 1, 页码 322-334出版社
AMER SOC MICROBIOLOGY
DOI: 10.1128/MCB.23.1.322-334.2003
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资金
- NCI NIH HHS [CA75556] Funding Source: Medline
- NHLBI NIH HHS [R01 HL062458, HL62458] Funding Source: Medline
- NATIONAL CANCER INSTITUTE [P01CA075556, Z01BC010544] Funding Source: NIH RePORTER
- NATIONAL HEART, LUNG, AND BLOOD INSTITUTE [R01HL062458] Funding Source: NIH RePORTER
More than 50% of human cancers contain p53 gene mutations and as a result accumulate altered forms of the full-length p53 protein. Although certain tumor types expressing mutant p53 protein have a poor prognostic process, the precise role of mutant p53 protein in highly malignant tumor cells is not well defined. Some p53 mutants, but not wild-type p53, are shown here to interact with Daxx, a Fas-binding protein that activates stress-inducible kinase pathways. Interaction of Daxx with p53 is highly dependent upon the specific mutation of p53. Tumorigenic mutants of p53 bind to Daxx and inhibit Daxx-dependent activation of the apoptosis signal-regulating kinase I stress-inducible kinases and Jun NH2-terminal kinase. Mutant p53 forms complexes with Daxx in cells, and consequently, mutant p53 is able to rescue cells from Daxx-dependent inhibition of proliferation. Thus, the accumulation of mutant p53 in tumor cells may contribute to tumorigenesis by inhibiting stress-inducible kinase pathways.
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