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Oligomeric structure of 14‐3‐3 protein: What do we know about monomers?
Author(s) -
Sluchanko Nikolai N.,
Gusev Nikolai B.
Publication year - 2012
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2012.10.048
Subject(s) - chemistry , monomer , biochemistry , organic chemistry , polymer
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.