Inhibition of PDGF β Receptor Signal Transduction by Coexpression of a Truncated Receptor
- 10 May 1991
- journal article
- Published by American Association for the Advancement of Science (AAAS) in Science
- Vol. 252 (5007) , 844-848
- https://doi.org/10.1126/science.1851331
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.Keywords
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