期刊
FEBS LETTERS
卷 586, 期 24, 页码 4249-4256出版社
ELSEVIER SCIENCE BV
DOI: 10.1016/j.febslet.2012.10.048
关键词
14-3-3 Protein; Monomer; Chaperone-like activity; Phosphorylation; Phosphomimicking mutation; Stability
资金
- Russian Foundation for Basic Science [12-04-31259, 10-04-00026]
- FEBS Short-Term Fellowship
14-3-3s predominantly form homo-/heterodimers that are in equilibrium with corresponding monomers. Dimer/monomer equilibrium depends on the nature and phosphorylation of Ser58 of certain 14-3-3 isoforms. The structure and properties of 14-3-3 dimers are well characterized, whereas 14-3-3 monomers are less investigated. Therefore design and analysis of dimer-incapable mutants of 14-3-3 are important. Truncated or heavily mutated proteins are not ideal since their structure may be distorted. Phosphomimicking mutations, such as S58(D/E), induce incomplete dimer dissociation. A recently characterized monomeric 14-3-3 contains few mutations and retains the original secondary structure. Monomeric 14-3-3 interacts with phosphorylated target proteins and has higher chaperone-like activity than dimeric 14-3-3. Further investigation of the properties of monomeric 14-3-3 is important for understanding its yet poorly characterized role in different cellular processes. (C) 2012 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
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