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Volume 270, Number 29, Issue of July 21, pp. 17221-17228, 1995
©1995 by The American Society for Biochemistry and Molecular Biology, Inc.

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A Small GTP-binding Protein, Rho, Associates with the Platelet-derived Growth Factor Type- Receptor upon Ligand Binding

(Received for publication, April 5, 1995)

From the  (1)Cancer Research Center, Boston University School of Medicine, Boston, Massachusetts 02118, (2)Consejo Superior de Investigaciones Cientficas, Instituto de Biomedicina y Parasitologia, Granada 18001, Spain, and the (3)Division of Immunology, Beth Israel Hospital, Harvard Medical School, Boston, Massachusetts 02115

Ligand binding to the platelet-derived growth factor (PDGF) receptor initiates a complex and diverging cascade of signaling pathways. GTP-binding proteins with intrinsic GTPase activity (G-proteins) frequently link cell surface receptors to intracellular signaling pathways, but no close associations of the PDGF receptor and any small G-proteins, nor any such associations activated by ligand binding to the receptor have been previously reported. We demonstrate that a small GTP-binding protein binds specifically to the murine and human PDGF type- receptor. In response to PDGF-BB stimulation, there is an increase in the amount of labeled small G-protein associated with the PDGF type- receptor. The GTP-binding protein did not undergo ligand-induced association with a mutant receptor protein that was unable to bind ATP. Proteolytic cleavage analysis, together with two-dimensional separation techniques, identified the small G-protein specifically associating with the PDGF type- receptor after ligand binding as a member of the Rho family. This was confirmed by demonstration that the small G-protein co-immunoprecipitated by the anti-PDGF receptor antibody was a substrate for the ADP-ribosyltransferase C3 exoenzyme. Thus, the PDGF type- receptor may form a complex with one or more small G-proteins upon binding PDGF-BB, and the Rho small G-protein is likely to be an important component of the proteins making up the multimeric signaling complex of the PDGF type- receptor.

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