Phg2, a Kinase Involved in Adhesion and Focal Site Modeling inDictyostelium
Copyright policy )Phg2, a Kinase Involved in Adhesion and Focal Site Modeling inDictyostelium
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.
- University of Lyon System France
- French National Centre for Scientific Research France
- University of Queensland Australia
- University of Queensland Australia
- Institut de Biologie et de Chimie des Protéines France
Talin, actin cytoskeleton, Protozoan Proteins, membrane proteins, myosins, cell movement, Cell Movement, Dictyostelium, Membrane Proteins/genetics/physiology, Phagocytosis/genetics/physiology, Talin/genetics/physiology, protozoan proteins, myosin VII, Cell Movement/genetics/physiology, phagocytosis, phg2, Protein-Serine-Threonine Kinases/analysis/genetics/physiology, Protozoan Proteins/genetics/physiology, Cell Shape/genetics/physiology, animals, Actin Cytoskeleton, Myosins/genetics/physiology, Cell Adhesion/genetics/physiology, 571, Mutation/genetics, Molecular Sequence Data, cytokinesis, molecular sequence data, 612, Myosins, Protein Serine-Threonine Kinases, cell shape, Phagocytosis, [SDV.BBM] Life Sciences [q-bio]/Biochemistry, Molecular Biology, Cell Adhesion, Animals, dictyostelium, Amino Acid Sequence, protein structure, Cell Shape, Cytokinesis, Actin Cytoskeleton/ultrastructure, talin, Cytokinesis/genetics/physiology, Membrane Proteins, cell adhesion, protein-serine-threonine kinases, amino acid sequence, Protein Structure, Tertiary, tertiary, Dictyostelium/enzymology/physiology/ultrastructure, Mutation, mutation, Polymerization/depolymerization, ddc: ddc:612
Talin, actin cytoskeleton, Protozoan Proteins, membrane proteins, myosins, cell movement, Cell Movement, Dictyostelium, Membrane Proteins/genetics/physiology, Phagocytosis/genetics/physiology, Talin/genetics/physiology, protozoan proteins, myosin VII, Cell Movement/genetics/physiology, phagocytosis, phg2, Protein-Serine-Threonine Kinases/analysis/genetics/physiology, Protozoan Proteins/genetics/physiology, Cell Shape/genetics/physiology, animals, Actin Cytoskeleton, Myosins/genetics/physiology, Cell Adhesion/genetics/physiology, 571, Mutation/genetics, Molecular Sequence Data, cytokinesis, molecular sequence data, 612, Myosins, Protein Serine-Threonine Kinases, cell shape, Phagocytosis, [SDV.BBM] Life Sciences [q-bio]/Biochemistry, Molecular Biology, Cell Adhesion, Animals, dictyostelium, Amino Acid Sequence, protein structure, Cell Shape, Cytokinesis, Actin Cytoskeleton/ultrastructure, talin, Cytokinesis/genetics/physiology, Membrane Proteins, cell adhesion, protein-serine-threonine kinases, amino acid sequence, Protein Structure, Tertiary, tertiary, Dictyostelium/enzymology/physiology/ultrastructure, Mutation, mutation, Polymerization/depolymerization, ddc: ddc:612
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