Ontology highlight
ABSTRACT:
SUBMITTER: Messaritou G
PROVIDER: S-EPMC2804327 | biostudies-literature | 2010 Jan
REPOSITORIES: biostudies-literature
Messaritou Georgia G Grammenoudi Sofia S Skoulakis Efthimios M C EM
The Journal of biological chemistry 20091117 3
Members of the conserved 14-3-3 protein family spontaneously self-assemble as homo- and heterodimers via conserved sequences in the first four (alphaA-alphaD) of the nine helices that comprise them. Dimeric 14-3-3s bind conserved motifs in diverse protein targets involved in multiple essential cellular processes including signaling, intracellular trafficking, cell cycle regulation, and modulation of enzymatic activities. However, recent mostly in vitro evidence has emerged, suggesting functional ...[more]