Journal
SEMINARS IN CELL & DEVELOPMENTAL BIOLOGY
Volume 22, Issue 7, Pages 663-672Publisher
ACADEMIC PRESS LTD- ELSEVIER SCIENCE LTD
DOI: 10.1016/j.semcdb.2011.09.001
Keywords
14-3-3; Structure; Protein-protein interactions; Phosphorylation
Categories
Funding
- Grant Agency of the Academy of Sciences of the Czech Science Foundation [P305/11/0708, P207/11/0455]
- Czech Republic [IAA501110801]
- Grant Agency of the Charles University [28510]
- Ministry of Education, Youth, and Sports of the Czech Republic Research [MSM0021620857, LC554]
- Academy of Sciences of the Czech Republic [AV0Z50110509]
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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.
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