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.

journal_name

FEBS Lett

journal_title

FEBS letters

authors

Sluchanko NN,Gusev NB

doi

10.1016/j.febslet.2012.10.048

subject

Has Abstract

pub_date

2012-12-14 00:00:00

pages

4249-56

issue

24

eissn

0014-5793

issn

1873-3468

pii

S0014-5793(12)00840-X

journal_volume

586

pub_type

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