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Kinase consensus sequences: a breeding ground for crosstalk

dc.contributor.authorRust, Heather L.
dc.contributor.authorThompson, Paul R
dc.date2022-08-11T08:11:00.000
dc.date.accessioned2022-08-23T17:28:14Z
dc.date.available2022-08-23T17:28:14Z
dc.date.issued2011-09-16
dc.date.submitted2015-05-22
dc.identifier.citationACS Chem Biol. 2011 Sep 16;6(9):881-92. doi: 10.1021/cb200171d. Epub 2011 Jul 15. <a href="http://dx.doi.org/10.1021/cb200171d">Link to article on publisher's site</a>
dc.identifier.issn1554-8929 (Linking)
dc.identifier.doi10.1021/cb200171d
dc.identifier.urihttp://hdl.handle.net/20.500.14038/50036
dc.description<p>At the time of publication, Paul Thompson was not yet affiliated with UMass Medical School.</p>
dc.description.abstractThe best characterized examples of crosstalk between two or more different post-translational modifications (PTMs) occur with respect to histones. These examples demonstrate the critical roles that crosstalk plays in regulating cell signaling pathways. Recently, however, non-histone crosstalk has been observed between serine/threonine phosphorylation and the modification of arginine and lysine residues within kinase consensus sequences. Interestingly, many kinase consensus sequences contain critical arginine/lysine residues surrounding the substrate serine/threonine residue. Therefore, we hypothesize that non-histone crosstalk between serine/threonine phosphorylation and arginine/lysine modifications is a global mechanism for the modulation of cellular signaling. In this review, we discuss several recent examples of non-histone kinase consensus sequence crosstalk, as well as provide the biophysical basis for these observations. In addition, we predict likely examples of crosstalk between protein arginine methyltransferase 1 (PRMT1) and Akt and discuss the future implications of these findings.
dc.language.isoen_US
dc.relation<a href="http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?db=pubmed&cmd=Retrieve&list_uids=21721511&dopt=Abstract">Link to Article in PubMed</a>
dc.relation.urlhttp://www.ncbi.nlm.nih.gov/pmc/articles/PMC3176959/
dc.subjectAmino Acids
dc.subjectConsensus Sequence
dc.subjectHumans
dc.subjectPhosphorylation
dc.subjectProtein Kinases
dc.subjectSignal Transduction
dc.subjectBiochemistry
dc.subjectEnzymes and Coenzymes
dc.subjectMedicinal-Pharmaceutical Chemistry
dc.subjectTherapeutics
dc.titleKinase consensus sequences: a breeding ground for crosstalk
dc.typeJournal Article
dc.source.journaltitleACS chemical biology
dc.source.volume6
dc.source.issue9
dc.identifier.legacycoverpagehttps://escholarship.umassmed.edu/thompson/45
dc.identifier.contextkey7135714
html.description.abstract<p>The best characterized examples of crosstalk between two or more different post-translational modifications (PTMs) occur with respect to histones. These examples demonstrate the critical roles that crosstalk plays in regulating cell signaling pathways. Recently, however, non-histone crosstalk has been observed between serine/threonine phosphorylation and the modification of arginine and lysine residues within kinase consensus sequences. Interestingly, many kinase consensus sequences contain critical arginine/lysine residues surrounding the substrate serine/threonine residue. Therefore, we hypothesize that non-histone crosstalk between serine/threonine phosphorylation and arginine/lysine modifications is a global mechanism for the modulation of cellular signaling. In this review, we discuss several recent examples of non-histone kinase consensus sequence crosstalk, as well as provide the biophysical basis for these observations. In addition, we predict likely examples of crosstalk between protein arginine methyltransferase 1 (PRMT1) and Akt and discuss the future implications of these findings.</p>
dc.identifier.submissionpaththompson/45
dc.contributor.departmentDepartment of Biochemistry and Molecular Pharmacology
dc.source.pages881-92


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