REVIEW: Signal Transduction in Neutrophil Chemotaxis

V. L. Katanaev

Institute of Biochemistry, University of Fribourg, Rue du Musee 5, CH-1700 Fribourg, Switzerland
Present address: Columbia University, College of Physicians and Surgeons, 701 West 168th Street, room 1120, New York, NY 10032, USA; fax: +1 212 305 3562; E-mail: vlk11@columbia.edu

Received August 11, 2000

---

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 G_i 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.

---

KEY WORDS: neutrophil chemotaxis, signal transduction, G protein-coupled receptors, PI3 kinases, Rho family proteins, actin polymerization

---