Phg2, a kinase involved in adhesion and focal site modeling in Dictyostelium

Leigh Gebbie, Mohammed Benghezal, Sophie Cornillon, Romain Froquet, Nathalie Cherix, Marilyne Malbouyres, Yaya Lefkir, Christophe Grangeasse, Sébastien Fache, Jérémie Dalous, Franz Brückert, François Letourneur, Pierre Cosson*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

49 Citations (Scopus)

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.

Original languageEnglish
Pages (from-to)3915-3925
Number of pages11
JournalMolecular Biology of the Cell
Volume15
Issue number8
DOIs
Publication statusPublished - Aug 2004
Externally publishedYes

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