Signal transduction in neutrophil chemotaxis

Biochemistry (Mosc). 2001 Apr;66(4):351-68. doi: 10.1023/a:1010293809553.

Abstract

This review discusses current knowledge on signal transduction pathways controlling chemotaxis of neutrophils and similar cells. Most neutrophil chemoattractants bind to seven-transmembrane-helix receptors. These receptors activate trimeric G proteins of the Gi class in neutrophils to initiate chemotaxis. Phospholipases Cbeta, phosphoinositide 3-kinase gamma, and PH domain-containing proteins play various roles in signaling further downstream. The actin cytoskeleton is crucial for cell motility, and is controlled by Rho family GTP-binding proteins. PIP 5-kinase, LIM kinase, myosin light chain kinase and phosphatase, or WASP-like proteins may be important links between Rho GTPases and actin during chemotaxis. Newly emerging ideas on the regulation of the "compass" of chemotaxing cells, which may involve Cdc42 and certain PH domain-containing proteins, are also presented.

Publication types

  • Review

MeSH terms

  • Animals
  • Cell Movement / physiology*
  • Chemotactic Factors / physiology
  • Chemotaxis, Leukocyte / physiology*
  • GTP-Binding Proteins / chemistry
  • GTP-Binding Proteins / metabolism
  • Humans
  • Neutrophils / cytology
  • Neutrophils / metabolism*
  • Phosphatidylinositol 3-Kinases / metabolism
  • Receptors, Formyl Peptide
  • Receptors, Immunologic / chemistry
  • Receptors, Immunologic / metabolism
  • Receptors, Peptide / chemistry
  • Receptors, Peptide / metabolism
  • Signal Transduction / physiology*
  • cdc42 GTP-Binding Protein / physiology*
  • rho GTP-Binding Proteins / physiology*

Substances

  • Chemotactic Factors
  • Receptors, Formyl Peptide
  • Receptors, Immunologic
  • Receptors, Peptide
  • Phosphatidylinositol 3-Kinases
  • GTP-Binding Proteins
  • cdc42 GTP-Binding Protein
  • rho GTP-Binding Proteins