University of Massachusetts Medical School Faculty Publications
Title
Multisite phosphorylation by MAPK
UMMS Affiliation
Program in Molecular Medicine; UMass Metabolic Network
Publication Date
2016-10-14
Document Type
Article
Disciplines
Cell Biology | Cellular and Molecular Physiology | Molecular Biology
Abstract
Summary: Reversible protein phosphorylation plays a fundamental role in signal transduction networks. Phosphorylation alters protein function by regulating enzymatic activity, stability, cellular localization, or binding partners. Over three-quarters of human proteins may be phosphorylated, with many targeted at multiple sites. Such multisite phosphorylation substantially increases the scope for modulating protein function—a protein with n phosphorylation sites has the potential to exist in 2n distinct phosphorylation states, each of which could, in theory, display modified functionality. Proteins can be substrates for several protein kinases, thereby integrating distinct signals to provide a coherent biological response. However, they can also be phosphorylated at multiple sites by a single protein kinase to promote a specific functional output that can be reversed by dephosphorylation by protein phosphatases. On page 233 of this issue, Mylona et al. (1) reveal an unexpected role for multisite phosphorylation, whereby a protein kinase progressively phosphorylates sites on a transcription factor to promote and then subsequently limit its activity independently of dephosphorylation.
DOI of Published Version
10.1126/science.aai9381
Source
Science. 2016 Oct 14;354(6309):179-180. Link to article on publisher's site
Related Resources
Journal/Book/Conference Title
Science (New York, N.Y.)
PubMed ID
27738159
Repository Citation
Whitmarsh, Alan J. and Davis, Roger J., "Multisite phosphorylation by MAPK" (2016). University of Massachusetts Medical School Faculty Publications. 1046.
https://escholarship.umassmed.edu/faculty_pubs/1046