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Front Genet. 2014 Aug 7;5:270. doi: 10.3389/fgene.2014.00270. eCollection 2014.

Physicochemical mechanisms of protein regulation by phosphorylation.

Author information

1
Graduate School of Medical Life Science, Yokohama City University Yokohama Japan.
2
National Center for Biotechnology Information, National Library of Medicine, National Institutes of Health Bethesda, MD USA.

Abstract

Phosphorylation offers a dynamic way to regulate protein activity and subcellular localization, which is achieved through its reversibility and fast kinetics. Adding or removing a dianionic phosphate group somewhere on a protein often changes the protein's structural properties, its stability and dynamics. Moreover, the majority of signaling pathways involve an extensive set of protein-protein interactions, and phosphorylation can be used to regulate and modulate protein-protein binding. Losses of phosphorylation sites, as a result of disease mutations, might disrupt protein binding and deregulate signal transduction. In this paper we focus on the effects of phosphorylation on protein stability, dynamics, and binding. We describe several physico-chemical mechanisms of protein regulation through phosphorylation and pay particular attention to phosphorylation in protein complexes and phosphorylation in the context of disorder-order and order-disorder transitions. Finally we assess the role of multiple phosphorylation sites in a protein molecule, their possible cooperativity and function.

KEYWORDS:

allosteric regulation; multisite phosphorylation; protein disorder; protein phosphorylation; protein–protein interactions

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