Monomeric 14-3-3ζ has a chaperone-like activity and is stabilized by phosphorylated HspB6.

ABSTRACT: Members of the 14-3-3 eukaryotic protein family predominantly function as dimers. The dimeric form can be converted into monomers upon phosphorylation of Ser(58) located at the subunit interface. Monomers are less stable than dimers and have been considered to be either less active or even inactive during binding and regulation of phosphorylated client proteins. However, like dimers, monomers contain the phosphoserine-binding site and therefore can retain some functions of the dimeric 14-3-3. Furthermore, 14-3-3 monomers may possess additional functional roles owing to their exposed intersubunit surfaces. Previously we have found that the monomeric mutant of 14-3-3ζ (14-3-3ζ(m)), like the wild type protein, is able to bind phosphorylated small heat shock protein HspB6 (pHspB6), which is in

SUBMITTER: Sluchanko NN 

PROVIDER: S-EPMC3413243 | biostudies-literature | 2012 Aug

REPOSITORIES: biostudies-literature