title: Oligomeric structure of 14-3-3 protein: what do we know about monomers?
abstract: 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.
authors.affiliation: A.N. Bach Institute of Biochemistry, Russian Academy of Sciences, Leninsky prospect 33, Moscow 119071, Russian Federation. nikolai.sluchanko@mail.ru
authors.forename: Nikolai N
authors.initials: NN
authors.lastname: Sluchanko
authors.forename: Nikolai B
authors.initials: NB
authors.lastname: Gusev
mesh_terms: D048948:14-3-3 Proteins / Q000737:chemistry* / Q000235:genetics; D006801:Humans; D018832:Molecular Chaperones / Q000737:chemistry; D009154:Mutation; D010766:Phosphorylation; D011485:Protein Binding; D055503:Protein Multimerization; D017433:Protein Structure, Secondary; D012694:Serine / Q000737:chemistry / Q000378:metabolism
chemical_list: D048948:14-3-3 Proteins; D018832:Molecular Chaperones; D012694:Serine