| Literature DB >> 20638895 |
Tufan Gökirmak1, Anna-Lisa Paul, Robert J Ferl.
Abstract
Regulation of the activity, location, and interactions of proteins by phosphorylation is crucial for many cellular processes including regulation of signaling. Phosphorylation-dependent interactions between proteins are one outcome of phosphorylation that can contribute to that regulation. Several kinds of phosphopeptide-binding proteins have been characterized, but in plants only by the forkhead-associated (FHA) domain proteins and, predominantly, the 14-3-3 proteins exist. 14-3-3 proteins have been shown to interact with several different classes of phosphorylated target proteins throughout eukaryotes. Initially, plant 14-3-3s were thought to be primarily associated with metabolic enzyme regulation; however, recent years have seen an increasing number of reports describing roles of 14-3-3 proteins in signal transduction, with plant 14-3-3 proteins now shown to interact with key proteins in signaling pathways.Mesh:
Substances:
Year: 2010 PMID: 20638895 DOI: 10.1016/j.pbi.2010.06.001
Source DB: PubMed Journal: Curr Opin Plant Biol ISSN: 1369-5266 Impact factor: 7.834