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Science 10 May 1991:
Vol. 252. no. 5007, pp. 844 - 848
DOI: 10.1126/science.1851331
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Articles

Science, Vol 252, Issue 5007, 844-848
Copyright © 1991 by American Association for the Advancement of Science

articles

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

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

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

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.


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