Phg2, a Kinase Involved in Adhesion and Focal Site Modeling in Dictyostelium

Overview

Journal Mol Biol Cell

Specialties Cell Biology
Molecular Biology

Date 2004 Jun 15

PMID 15194808

Citations 34

Authors

Leigh Gebbie

Mohammed Benghezal

Sophie Cornillon

Romain Froquet

Nathalie Cherix

Marilyne Malbouyres

Yaya Lefkir

Christophe Grangeasse

Sebastien Fache

Jeremie Dalous

Franz Bruckert

Francois Letourneur

Pierre Cosson

Affiliations

Soon will be listed here.

Abstract

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.

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