Page Contents: Abstract | Summary Chart

---

Gebbie, L., Benghezal, M., Cornillon, S., Froquet, R., Cherix, N., Malbouyres, M., Lefkir, Y., Grangeasse, C., Fache, S., Dalous, J., Bruckert, F., Letourneur, F., Cosson, P., (2004) ' Phg2, a kinase involved in adhesion and focal site modeling in Dictyostelium. ' Mol Biol Cell 15 3915-25

 

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.
Status:	Published	Type:	Journal article	Source:	PUBMED	PubMed ID:	15194808

---

 

	Genes addressed in this paper
	myoI	phg1A	phg2	rapA	rasG	rasS	talA
Topics in this paper
Protein Physical Properties			X
Mitosis	X	X	X				X
Adhesion	X	X	X				X
Protein Functional Domain			X
Cytoskeleton	X	X	X				X
Strains/Constructs			X
Cellular Location			X
Synonym	X	X		X			X
Function/Process	X	X	X				X
Chemotaxis/Motility	X	X	X				X
Endocytosis	X	X	X				X
Protein-Protein Interactions			X	X	X	X
DNA/RNA Sequence Features			X
Mutants/Phenotypes	X	X	X				X