Association of coatomer proteins with the beta-receptor for platelet-derived growth factor
Författare
Summary, in English
The nonreceptor tyrosine kinase Src binds to and is activated by the beta-receptor for platelet-derived growth factor (PDGF). The interaction leads to Src phosphorylation of Tyr934 in the kinase domain of the receptor. In the course of the functional characterization of this phosphorylation, we noticed that components of 136 and 97 kDa bound to a peptide from this region of the receptor in a phosphorylation-independent manner. These components have now been purified and identified as alpha- and beta'-coatomer proteins (COPs), respectively. COPs are a family of proteins involved in the regulation of intracellular vesicle transport. In order to explore the functional significance of the interaction between alpha- and beta'-COP and the PDGF receptor, a receptor mutant was made in which the conserved histidine residue 928 was mutated to an alanine residue. The mutant receptor, which was unable to bind alpha- or beta'-COP, showed a normal ligand-induced autophosphorylation. The mutant receptor also behaved like the wildtype receptor with regard to biosynthesis and maturation, and mediated a mitogenic signal. The possible functional importance of the interaction between the PDGF beta-receptor and alpha- and beta'-COP, is discussed.
Publiceringsår
1997
Språk
Engelska
Sidor
455-460
Publikation/Tidskrift/Serie
Biochemical and Biophysical Research Communications
Volym
235
Issue
3
Dokumenttyp
Artikel i tidskrift
Förlag
Elsevier
Ämne
- Medicinal Chemistry
Nyckelord
- Platelet-Derived Growth Factor beta Receptors
- Platelet-Derived Growth Factor/chemistry/isolation & purification/*metabolism Recombinant Fusion Proteins/chemistry/isolation & purification/metabolism Transfection Tyrosine src Homology Domains
- Amino Acid Sequence Binding Sites Chromatography
- Site-Directed Oligopeptides/chemical synthesis/chemistry Peptide Fragments/chemistry Phosphorylation Point Mutation Receptor
- Affinity Coatomer Protein Conserved Sequence Hela Cells Histidine Humans Membrane Proteins/isolation & purification/*metabolism Microtubule-Associated Proteins/metabolism Molecular Sequence Data Molecular Weight Mutagenesis
Status
Published
ISBN/ISSN/Övrigt
- ISSN: 1090-2104