Science. 1991 May 10;252(5007):844-8.

Inhibition of PDGF beta receptor signal transduction by coexpression of a truncated receptor.

Ueno H, Colbert H, Escobedo JA, Williams LT.

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Department of Medicine, University of California, San Francisco 94143.

Abstract

A mutated form of the platelet-derived growth factor (PDGF) beta receptor lacking most of its cytoplasmic domain was tested for its ability to block wild-type PDGF receptor function. PDGF induced the formation of complexes consisting of wild-type and truncated receptors. Such complexes were defective in autophosphorylation. When truncated receptors were expressed in excess compared to wild-type receptors, stimulation by PDGF of receptor autophosphorylation, association of phosphatidylinositol-3 kinase with the receptor, and calcium mobilization were blocked. Thus, a truncated receptor can inactivate wild-type receptor function by forming ligand-dependent receptor complexes (probably heterodimers) that are incapable of mediating the early steps of signal transduction.

PMID:: 1851331; [PubMed - indexed for MEDLINE]

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