Issue 9, 2008
From the journal:

Molecular BioSystems

Linking the kinome and phosphorylome—a comprehensive review of approaches to find kinase targets

Richelle Sopkoa  and  Brenda J. Andrews*b  

* Corresponding authors

a Samuel Lunenfeld Research Institute, Mount Sinai Hospital, Toronto, Canada

b Department of Molecular Genetics, Terrence Donnelly Centre for Cellular and Biomolecular Research, Banting and Best Department of Medical Research, University of Toronto, Toronto, Ontario, Canada, Centre for Cellular and Biomolecular Research, 160 College Street, Toronto, Ontario, Canada
E-mail: brenda.andrews@utoronto.ca
Fax: +1 416-946-8253
Tel: +1 416-978-8562

Abstract

Protein phosphorylation is associated with most cell signaling and developmental processes in eukaryotes. Despite the vast extent of the phosphoproteome within the cell, connecting specific kinases with relevant targets remains a significant experimental frontier. The challenge of linking kinases and their substrates reflects the complexity of kinase function. For example, kinases tend to exert their biological effects through supernumerary, redundant phosphorylation, often on multiple protein complex components. Although these types of phosphorylation events are biologically significant, those kinases responsible are often difficult to identify. Recent methods for global analysis of proteinphosphorylation promise to substantially accelerate efforts to map the dynamic phosphorylome. Here, we review both conventional methods to identify kinase targets and more comprehensive genomic and proteomic approaches to connect the kinome and phosphorylome.

Graphical abstract: Linking the kinome and phosphorylome—a comprehensive review of approaches to find kinase targets

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Article information

DOI
https://doi.org/10.1039/B801724G
Article type
Review Article
Submitted
30 Jan 2008
Accepted
10 Jun 2008
First published
17 Jul 2008

Mol. BioSyst., 2008,4, 920-933

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Linking the kinome and phosphorylome—a comprehensive review of approaches to find kinase targets

R. Sopko and B. J. Andrews, Mol. BioSyst., 2008, 4, 920 DOI: 10.1039/B801724G

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