Show simple item record

dc.contributor.authorWhitmarsh, Alan J.
dc.contributor.authorDavis, Roger J.
dc.date2022-08-11T08:08:19.000
dc.date.accessioned2022-08-23T15:51:04Z
dc.date.available2022-08-23T15:51:04Z
dc.date.issued2016-10-14
dc.date.submitted2016-12-06
dc.identifier.citationScience. 2016 Oct 14;354(6309):179-180. <a href="http://dx.doi.org/10.1126/science.aai9381">Link to article on publisher's site</a>
dc.identifier.issn0036-8075 (Linking)
dc.identifier.doi10.1126/science.aai9381
dc.identifier.pmid27738159
dc.identifier.urihttp://hdl.handle.net/20.500.14038/28807
dc.description.abstractSummary: 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.
dc.language.isoen_US
dc.relation<a href="http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?db=pubmed&cmd=Retrieve&list_uids=27738159&dopt=Abstract">Link to Article in PubMed</a>
dc.relation.urlhttp://dx.doi.org/10.1126/science.aai9381
dc.subjectCell Biology
dc.subjectCellular and Molecular Physiology
dc.subjectMolecular Biology
dc.titleMultisite phosphorylation by MAPK
dc.typeJournal Article
dc.source.journaltitleScience (New York, N.Y.)
dc.source.volume354
dc.source.issue6309
dc.identifier.legacycoverpagehttps://escholarship.umassmed.edu/faculty_pubs/1046
dc.identifier.contextkey9445258
html.description.abstract<p>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 <em>n</em> phosphorylation sites has the potential to exist in 2<em>n</em> 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 <em>et al.</em> (<em>1</em>) 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.</p>
dc.identifier.submissionpathfaculty_pubs/1046
dc.contributor.departmentUMass Metabolic Network
dc.contributor.departmentProgram in Molecular Medicine
dc.source.pages179-180


This item appears in the following Collection(s)

Show simple item record