Title
Kinase consensus sequences: a breeding ground for crosstalk
UMMS Affiliation
Department of Biochemistry and Molecular Pharmacology
Publication Date
2011-09-16
Document Type
Article
Subjects
Amino Acids; Consensus Sequence; Humans; Phosphorylation; Protein Kinases; Signal Transduction
Disciplines
Biochemistry | Enzymes and Coenzymes | Medicinal-Pharmaceutical Chemistry | Therapeutics
Abstract
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.
DOI of Published Version
10.1021/cb200171d
Source
ACS Chem Biol. 2011 Sep 16;6(9):881-92. doi: 10.1021/cb200171d. Epub 2011 Jul 15. Link to article on publisher's site
Journal/Book/Conference Title
ACS chemical biology
Related Resources
Repository Citation
Rust HL, Thompson PR. (2011). Kinase consensus sequences: a breeding ground for crosstalk. Thompson Lab Publications. https://doi.org/10.1021/cb200171d. Retrieved from https://escholarship.umassmed.edu/thompson/45
Comments
At the time of publication, Paul Thompson was not yet affiliated with UMass Medical School.