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 14-3-3 proteins; bringing new definitions to scaffolding Tzivion G; Shen YH; Zhu JOncogene  2001[Oct]; 20 (44): 6331-8The 14-3-3 proteins are a part of an emerging family of proteins and protein  domains that bind to serine/threonine-phosphorylated residues in a context  specific manner, analogous to the Src homology 2 (SH2) and phospho-tyrosine  binding (PTB) domains. 14-3-3 proteins bind and regulate key proteins involved in  various physiological processes such as intracellular signaling (e.g. Raf, MLK,  MEKK, PI-3 kinase, IRS-1), cell cycling (e.g. Cdc25, Wee1, CDK2, centrosome),  apoptosis (e.g. BAD, ASK-1) and transcription regulation (e.g. FKHRL1, DAF-16,  p53, TAZ, TLX-2, histone deacetylase). In contrast to SH2 and PTB domains, which  serve mainly to mediate protein-protein interactions, 14-3-3 proteins in many  cases alter the function of the target protein, thus allowing them to serve as  direct regulators of their targets. This review focuses on the various mechanisms  employed by the 14-3-3 proteins in the regulation of their diverse targets, the  structural basis for 14-3-3-target protein interaction with emphasis on the role  of 14-3-3 dimerization in target protein binding and regulation and provides an  insight on 14-3-3 regulation itself.|14-3-3 Proteins[MESH]|Animals[MESH]|Cell Cycle[MESH]|Humans[MESH]|Models, Biological[MESH]|Phosphorylation[MESH]|Protein Structure, Tertiary[MESH]|Signal Transduction[MESH]|Transcription, Genetic[MESH]|Tyrosine 3-Monooxygenase/*chemistry/*metabolism/*physiology[MESH]
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