Overview of Protein Phosphorylation

Bartholomew M. Sefton1

1 The Salk Institute, San Diego, California
Publication Name:  Current Protocols in Cell Biology
Unit Number:  Unit 14.1
DOI:  10.1002/0471143030.cb1401s00
Online Posting Date:  May, 2001
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Phosphorylation is the most common and important mechanism of acute and reversible regulation of protein function. Studies of mammalian cells metabolically labeled with [32P]orthophosphate suggest that as many as one‐third of all cellular proteins are covalently modified by protein phosphorylation. Protein phosphorylation has an important role in essentially all aspects of cell biology. Most polypeptide growth factors (platelet‐derived growth factor and epidermal growth factor are among the best studied) and cytokines (e.g., interleukin 2, colony stimulating factor 1, and γ‐interferon) stimulate phosphorylation upon binding to their receptors. Induced phosphorylation in turn activates cytoplasmic protein kinases, such as Raf, the activators of the mitogen‐activated protein (MAP) kinases SEK and MEK, the MAP kinases ERK, JNK, and p38, the Janus/JAK kinases, the p21 activated kinases (PAKs), and the phosphatidylinsoitil 3'‐kinase‐activated kinase, protein kinase B/Akt. Additionally, in all nucleated organisms, cell cycle progression is regulated at both the G1/S and the G2/M transitions by cyclin‐dependent protein kinases. These kinases regulate the G1/S transition by the phosphorylation of cell cycle regulators such as Rb protein and the G2/M transition through the phosphorylation of nuclear lamins and histones.

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Table of Contents

  • History
  • Labeling Studies
  • Sites of Phosphorylation
  • Detection of Unlabeled Phosphoamino Acids
  • Protein Kinases
  • Protein Phosphatases
  • Literature Cited
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Literature Cited

Literature Cited
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