Overview of protein phosphorylation

Curr Protoc Cell Biol. 2001 May:Chapter 14:Unit 14.1. doi: 10.1002/0471143030.cb1401s00.

Abstract

Phosphorylation is the most common and important mechanism of acute and reversible regulation of protein function. Studies of mammalian cells metabolically labeled with [(32)P]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 gamma-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.

Publication types

  • Review

MeSH terms

  • Animals
  • Humans
  • Phosphoprotein Phosphatases / metabolism
  • Phosphorylation*
  • Protein Kinases / metabolism
  • Proteins / chemistry
  • Proteins / metabolism*
  • Signal Transduction / physiology*

Substances

  • Proteins
  • Protein Kinases
  • Phosphoprotein Phosphatases