Available online at www.sciencedirect.com ScienceDirect Cell signaling regulation by protein phosphorylation: a multivariate, heterogeneous, and context-dependent process 1,3 1,3 1,2 Evan K Day , Nisha G Sosale and Matthew J Lazzara Proper spatiotemporal regulation of protein phosphorylation in Many biomolecules participate in signaling, including cells and tissues is required for normal development and proteins, amino acids, lipids, and second messengers homeostasis, but aberrant protein phosphorylation regulation (e.g., cyclic AMP, inositol triphosphate). The focus here leads to various diseases. The study of signaling regulation by is signaling regulation by protein phosphorylation, which protein phosphorylation is complicated in part by the sheer plays several mechanistic roles. Phosphorylation general- scope of the kinome and phosphoproteome, dependence of ly receives greater attention than other post-translational signaling protein functionality on cellular localization, and the modiﬁcations, in part because kinases are often over- complex multivariate relationships that exist between protein expressed or mutated in disease, especially cancer. As a phosphorylation dynamics and the cellular phenotypes they result, many inhibitors and antibodies have been devel- control. Additional complexities arise from the ability of oped to antagonize the activity of kinases. microenvironmental factors to inﬂuence phosphorylation- dependent signaling and from the tendency for some signaling Protein phosphorylation
Current Opinion in Biotechnology – Elsevier
Published: Aug 1, 2016
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