Structural basis of 14-3-3 protein functions

被引:244
作者
Obsil, Tomas [1 ,2 ]
Obsilova, Veronika [2 ]
机构
[1] Charles Univ Prague, Fac Sci, Dept Phys & Macromol Chem, Prague 12843, Czech Republic
[2] Acad Sci Czech Republ, Inst Physiol, CR-14220 Prague, Czech Republic
关键词
14-3-3; Structure; Protein-protein interactions; Phosphorylation; FORKHEAD TRANSCRIPTION FACTOR; MEMBRANE H+-ATPASE; ACTIVATES TRYPTOPHAN 5-MONOOXYGENASE; PHOSPHORYLATED NITRATE REDUCTASE; SEROTONIN N-ACETYLTRANSFERASE; TYROSINE-HYDROXYLASE; EXOENZYME-S; LIGAND-BINDING; DNA-BINDING; SUBCELLULAR-LOCALIZATION;
D O I
10.1016/j.semcdb.2011.09.001
中图分类号
Q2 [细胞生物学];
学科分类号
071009 ; 090102 ;
摘要
The 14-3-3 proteins, a family of conserved regulatory molecules, participate in a wide range of cellular processes through binding interactions with hundreds of structurally and functionally diverse proteins. Several distinct mechanisms of the 14-3-3 protein function were described, including conformational modulation of the bound protein, masking of its sequence-specific or structural features, and scaffolding that facilitates interaction between two simultaneously bound proteins. Details of these functional modes, especially from the structural point of view, still remain mostly elusive. This review gives an overview of the current knowledge concerning the structure of 14-3-3 proteins and their complexes as well as the insights it provides into the mechanisms of their functions. We discuss structural basis of target recognition by 14-3-3 proteins, common structural features of their complexes and known mechanisms of 14-3-3 protein-dependent regulations. (C) 2011 Elsevier Ltd. All rights reserved.
引用
收藏
页码:663 / 672
页数:10
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