The Plexin-B1/Rac interaction inhibits PAK activation and enhances Sema4D ligand binding
Copyright policy )The Plexin-B1/Rac interaction inhibits PAK activation and enhances Sema4D ligand binding
The small GTPase Rac has been implicated in growth cone guidance mediated by semaphorins and their receptors. Here we demonstrate that plexin-B1, a receptor for Semaphorin4D (Sema4D), and p21-activated kinase (PAK) can compete for the interaction with active Rac and plexin-B1 can inhibit Rac-induced PAK activation. We have also demonstrated that expression of active Rac enhances the ability of plexin-B1 to interact with Sema4D. Active Rac stimulates the localization of plexin-B1 to the cell surface. The enhancement in Sema4D binding depends on the ability of Rac to bind plexin-B1. These observations support a model where signaling between Rac and plexin-B1 is bidirectional; Rac modulates plexin-B1 activity and plexin-B1 modulates Rac function.
- University of Michigan–Ann Arbor United States
- University of Michigan–Flint United States
Membrane Glycoproteins, Dose-Response Relationship, Drug, Cell Membrane, Nerve Tissue Proteins, Protein Serine-Threonine Kinases, Ligands, Models, Biological, Cell Line, Protein Structure, Tertiary, Enzyme Activation, Kinetics, Antigens, CD, COS Cells, Animals, Humans, Biotinylation, Endopeptidase K, Glycoproteins, Plasmids, Protein Binding
Membrane Glycoproteins, Dose-Response Relationship, Drug, Cell Membrane, Nerve Tissue Proteins, Protein Serine-Threonine Kinases, Ligands, Models, Biological, Cell Line, Protein Structure, Tertiary, Enzyme Activation, Kinetics, Antigens, CD, COS Cells, Animals, Humans, Biotinylation, Endopeptidase K, Glycoproteins, Plasmids, Protein Binding
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