Rust, Heather L.Thompson, Paul R2022-08-232022-08-232011-09-162015-05-22ACS 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>1554-8929 (Linking)10.1021/cb200171dhttps://hdl.handle.net/20.500.14038/50036<p>At the time of publication, Paul Thompson was not yet affiliated with UMass Medical School.</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.en-USAmino AcidsConsensus SequenceHumansPhosphorylationProtein KinasesSignal TransductionBiochemistryEnzymes and CoenzymesMedicinal-Pharmaceutical ChemistryTherapeuticsJournal Articlehttps://escholarship.umassmed.edu/thompson/457135714thompson/45