14-3-3 proteins in apoptosis

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14-3-3 proteins in apoptosis.

The once obscure members of the 14-3-3 protein family play significant roles in the determination of cell fate. By inhibiting the pro-apoptotic BAD (Bcl-2-antagonist of cell death) and the transcription factor FKHRL-1, 14-3-3 displays important anti-apoptotic characteristics. To date, five points of interaction of 14-3-3 with the apoptotic machinery have been identified. How these interactions ...

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The 14-3-3 proteins

So what’s so interesting about them? In 1996 14-3-3 was found to bind to a variety of oncoproteins including Raf-1, polyoma middle T, and Bcr-Abl. Since then the 14-3-3 proteins have been shown to bind to a wide variety of proteins involved in signal transduction, cell cycle and apoptosis. These proteins include Cdc25, NFAT, Bad, Cbl, A20, PI 3-kinase, IRS-1, MEKK, p130Cas, glucocorticoid recep...

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14-3-3 proteins as signaling integration points for cell cycle control and apoptosis.

14-3-3 proteins play critical roles in the regulation of cell fate through phospho-dependent binding to a large number of intracellular proteins that are targeted by various classes of protein kinases. 14-3-3 proteins play particularly important roles in coordinating progression of cells through the cell cycle, regulating their response to DNA damage, and influencing life-death decisions follow...

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14-3-3 proteins block apoptosis and differentially regulate MAPK cascades.

14-3-3 family members are dimeric phosphoserine-binding proteins that participate in signal transduction and checkpoint control pathways. In this work, dominant-negative mutant forms of 14-3-3 were used to disrupt 14-3-3 function in cultured cells and in transgenic animals. Transfection of cultured fibroblasts with the R56A and R60A double mutant form of 14-3-3zeta (DN-14-3-3zeta) inhibited ser...

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Suppression of apoptosis signal-regulating kinase 1-induced cell death by 14-3-3 proteins.

Apoptosis signal-regulating kinase 1 (ASK1) is a pivotal component of a signaling pathway induced by many death stimuli, including tumor necrosis factor alpha, Fas, and the anticancer drugs cisplatin and paclitaxel. Here we report that ASK1 proapoptotic activity is antagonized by association with 14-3-3 proteins. We found that ASK1 specifically bound 14-3-3 proteins via a site involving Ser-967...

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ژورنال

عنوان ژورنال: Brazilian Journal of Medical and Biological Research

سال: 2003

ISSN: 0100-879X

DOI: 10.1590/s0100-879x2003000400001