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

Comments

At the time of publication, Paul Thompson was not yet affiliated with UMass Medical School.

Related Resources

Link to Article in PubMed

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