The browser you are using is not supported by this website. All versions of Internet Explorer are no longer supported, either by us or Microsoft (read more here: https://www.microsoft.com/en-us/microsoft-365/windows/end-of-ie-support).

Please use a modern browser to fully experience our website, such as the newest versions of Edge, Chrome, Firefox or Safari etc.

Functional co-operation between the subunits in heterodimeric platelet-derived growth factor receptor complexes

På svenska

Author

Summary, in English

To determine the importance of the phosphorylation capacity of receptor kinase as well as the ability to serve as docking sites for SH2-domain-containing signal transduction molecules, we established pig aortic endothelial cell lines stably expressing kinase-active platelet-derived growth factor (PDGF) alpha-receptors together with kinase-inactive beta-receptors, and vice versa. After stimulation with PDGF-AB, heterodimeric receptor complexes were formed in which the kinase-inactive receptor was phosphorylated by the kinase-active receptor, although less efficiently than in heterodimers of wild-type receptors. The kinase-active receptor was only minimally phosphorylated. Thus the phosphorylation within the receptor dimer occurred in trans between the components. Analyses of the abilities of heterodimeric receptor complexes of one kinase-active and one kinase-inactive receptor to mediate mitogenicity, chemotaxis and activation of mitogen-activated protein kinase revealed less efficient effects than those of heterodimers of wild-type receptors. Importantly, however, the fact that signalling capacities were retained illustrates a functional co-operation between the two receptor molecules in the dimer, where one receptor provides a functional kinase and the other acts as a substrate and provides docking sites for downstream signalling molecules.

Publishing year

1999

Language

English

Pages

523-528

Publication/Series

Biochemical Journal

Volume

341

Issue

3

Document type

Journal article

Publisher

Portland Press

Topic

  • Medicinal Chemistry

Keywords

  • Platelet-Derived Growth Factor/*metabolism*Signal TransductionSwineTyrosine/metabolism
  • AnimalsBase SequenceCalcium-Calmodulin-Dependent Protein Kinases/metabolismCell LineCell Movement/drug effectsDNA PrimersDimerizationEnzyme ActivationMitogens/pharmacologyPeptide MappingPhosphorylationPlatelet-Derived Growth Factor/pharmacologyReceptors

Status

Published

ISBN/ISSN/Other

  • ISSN: 0264-6021