Overview of Protein Phosphorylation

Bartholomew M. Sefton1, Shirish Shenolikar2

1 The Salk Institute, San Diego, California, 2 Duke University Medical Center, Durham, North Carolina
Publication Name:  Current Protocols in Molecular Biology
Unit Number:  Unit 18.1
DOI:  10.1002/0471142727.mb1801s33
Online Posting Date:  May, 2001
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This overview discusses the significance and roles of protein phosphorylation in regulation of protein function. Sites of phosphorylation are described as well as methods for detecting both radiolabeled and unlabeled phosphoamino acids. Importantly, protein kinases and phosphatases, the regulators of phosphorylation are discussed.

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Table of Contents

  • History
  • Labeling Studies
  • Sites of Phosphorylation
  • Detection of Unlabeled Phosphoamino Acids
  • Protein Kinases
  • Protein Phosphatases
  • Literature Cited
PDF or HTML at Wiley Online Library


PDF or HTML at Wiley Online Library



Literature Cited

Literature Cited
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   Crews, C.M. and Erickson, R.L. 1992. Purification of a murine protein‐tyrosine/threonine kinase that phosphorylates and activates the erk‐1 gene product: Relationship to the fission yeast byr1 gene product. Proc. Natl. Acad. Sci. U.S.A. 89:8205‐8209.
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   Kamps, M.P. 1991. Determination of phosphoamino acid composition by acid hydrolysis of protein blotted to Immobilon. Methods Enzymol. 201:21‐27.
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   Sun, H., Charles, C.H., Lau, L.F., and Tonks, N.K. 1993. MKP‐1 (3CH134), an immediate early gene product, is a dual‐specificity phosphatase that dephosphorylates MAP kinase in vivo. Cell 75:487‐493.
   Thorburn, J., McMahon, M. and Thorburn, A. 1994. Raf‐1 kinase activity is necessary and sufficient for gene expression changes but not sufficient for cellular morphology changes associated with cardiac myocyte hypertrophy. J. Biol. Chem. 269:30580‐30586.
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