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Vol. 15, Issue 8, 3915-3925, August 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, Unité Mixte Recherche 5086 Centre National de la Recherche Scientifique, 69367 Lyon Cedex 07, France; and
Laboratoire de Biochimie et Biophysique des Systèmes Intégrés, Unité Mixte Recherche 5092, Centre National de la Recherche Scientifique, Commissariat à l'Energie Atomique (Saclay, France), Grenoble, France
Submitted December 19, 2003;
Revised May 14, 2004;
Accepted June 2, 2004
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 also is 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. Because 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.
Abbreviations used: FAK, focal adhesion kinase; PB, phosphate buffer; RBD, ras-binding domain; ROCK, rho-activated kinase.
These authors contributed equally to this work.
|| Corresponding author. E-mail address: pierre.cosson{at}medecine.unige.ch.
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