Journal
CELLULAR SIGNALLING
Volume 19, Issue 11, Pages 2218-2226Publisher
ELSEVIER SCIENCE INC
DOI: 10.1016/j.cellsig.2007.06.006
Keywords
processive phosphorylation; serine/threonine kinase; tyrosine kinase; posttranslational modification; Cas; SR proteins
Categories
Funding
- NCI NIH HHS [R01 CA058530, R01 CA058530-13, CA58530] Funding Source: Medline
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Recent proteomic data indicate that a majority of the phosphorylated proteins in a eucaryotic cell contain multiple sites of phosphorylation. In many signaling events, a single kinase phosphorylates multiple sites on a target protein. Processive phosphorylation occurs when a protein kinase binds once to a substrate and phosphorylates all of the available sites before dissociating. In this review, we discuss examples of processive phosphorylation by serine/threonine kinases and tyrosine kinases. We describe current experimental approaches for distinguishing processive from non-processive phosphorylation. Finally, we contrast the biological situations that are suited to regulation by processive and non-processive phosphorylation. (C) 2007 Elsevier Inc. All rights reserved.
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