Journal
CURRENT OPINION IN BIOTECHNOLOGY
Volume 40, Issue -, Pages 185-192Publisher
ELSEVIER SCI LTD
DOI: 10.1016/j.copbio.2016.06.005
Keywords
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Funding
- American Cancer Society [RSG-15-010-01-CDD]
- National Science Foundation [CBET-1450751, CBET-1264807, CBET-1511853]
- National Institutes of Health [R21-CA195158]
- Div Of Chem, Bioeng, Env, & Transp Sys
- Directorate For Engineering [1700687, 1264807] Funding Source: National Science Foundation
- Div Of Chem, Bioeng, Env, & Transp Sys
- Directorate For Engineering [1450751, 1511853] Funding Source: National Science Foundation
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Proper spatiotemporal regulation of protein phosphorylation in cells and tissues is required for normal development and homeostasis, but aberrant protein phosphorylation regulation leads to various diseases. The study of signaling regulation by protein phosphorylation is complicated in part by the sheer scope of the kinome and phosphoproteome, dependence of signaling protein functionality on cellular localization, and the complex multivariate relationships that exist between protein phosphorylation dynamics and the cellular phenotypes they control. Additional complexities arise from the ability of microenvironmental factors to influence phosphorylation-dependent signaling and from the tendency for some signaling processes to occur heterogeneously among cells. These considerations should be taken into account when measuring cell signaling regulation by protein phosphorylation.
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