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A more recent version of this article appeared on August 1, 2004
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Submitted on December 19, 2003
Revised on May 14, 2004
Accepted on June 2, 2004
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*Université de Genève, Centre Médical Universitaire, Département de Morphologie, CH-1211 Genève 4, Switzerland;
Institut de Biologie et de Chimie des Protéines, UMR 5086 CNRS, Lyon Cedex 07, France;
Laboratoire de Biochimie et Biophysique des Systèmes Intégrés, UMR5092, CNRS, CEA, Grenoble, France
Monitoring Editor: Paul Matsudaira
The amoeba Dictyostelium is a simple genetic system for analyzing substrate adhesion, motility and phagocytosis. A new adhesion-defective mutant named phg2 was isolated in this system, and PHG2 encodes a novel serine/threonine kinase with a ras-binding domain. We compared the phenotype of phg2 null cells to other previously isolated adhesion mutants to evaluate the specific role of each gene product. Phg1, Phg2, myosin VII and talin all play similar roles in cellular adhesion. Like myosin VII and talin, Phg2 is also involved in the organization of the actin cytoskeleton. In addition phg2 mutant cells have defects in the organization of the actin cytoskeleton at the cell-substrate interface, and in cell motility. Since these last two defects are not seen in phg1, myoVII or talin mutants, this suggests a specific role for Phg2 in the control of local actin polymerization/depolymerization. This study establishes a functional hierarchy in the roles of Phg1, Phg2, myosinVII and talin in cellular adhesion, actin cytoskeleton organization and motility.
Corresponding author. E-mail: Pierre.Cosson{at}medecine.unige.ch