Review
Nature Reviews Molecular Cell Biology 8, 530-541 (July 2007) | doi:10.1038/nrm2203
There is an Erratum (1 August 2007) associated with this article.
Mechanisms of specificity in protein phosphorylation
Jeffrey A. Ubersax1 & James E. Ferrell Jr1 About the authors
Abstract
A typical protein kinase must recognize between one and a few hundred bona fide phosphorylation sites in a background of 
700,000 potentially phosphorylatable residues. Multiple mechanisms have evolved that contribute to this exquisite specificity, including the structure of the catalytic site, local and distal interactions between the kinase and substrate, the formation of complexes with scaffolding and adaptor proteins that spatially regulate the kinase, systems-level competition between substrates, and error-correction mechanisms. The responsibility for the recognition of substrates by protein kinases appears to be distributed among a large number of independent, imperfect specificity mechanisms.
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Author affiliations
- Department of Chemical and Systems Biology, Stanford University School of Medicine, Stanford, California 94305-5174, USA.
Correspondence to: Jeffrey A. Ubersax1 Email: jubersax@stanford.edu
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