Association of coatomer proteins with the beta-receptor for platelet-derived growth factor
Hansen, Klaus ; Rönnstrand, Lars LU
; Rorsman, Charlotte
; Hellman, Ulf
and Heldin, Carl-Henrik
(1997)
In Biochemical and Biophysical Research Communications
235(3).
p.455-460
- Abstract
- 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... (More)
- 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. (Less)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/1783934
- author
- Hansen, Klaus
; Rönnstrand, Lars
LU
; Rorsman, Charlotte
; Hellman, Ulf
and Heldin, Carl-Henrik
- publishing date
- 1997
- type
- Contribution to journal
- publication status
- published
- subject
- keywords
- 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
- in
- Biochemical and Biophysical Research Communications
- volume
- 235
- issue
- 3
- pages
- 455 - 460
- publisher
- Elsevier
- external identifiers
-
- scopus:0031587963
- ISSN
- 1090-2104
- DOI
- 10.1006/bbrc.1997.6821
- language
- English
- LU publication?
- no
- additional info
- The information about affiliations in this record was updated in December 2015. The record was previously connected to the following departments: Experimental Clinical Chemistry (013016010)
- id
- 289ef61e-5297-4608-a1b3-dee50f682fb9 (old id 1783934)
- date added to LUP
- 2016-04-04 09:05:59
- date last changed
- 2022-01-29 08:17:23
@article{289ef61e-5297-4608-a1b3-dee50f682fb9,
abstract = {{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.}},
author = {{Hansen, Klaus and Rönnstrand, Lars and Rorsman, Charlotte and Hellman, Ulf and Heldin, Carl-Henrik}},
issn = {{1090-2104}},
keywords = {{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}},
language = {{eng}},
number = {{3}},
pages = {{455--460}},
publisher = {{Elsevier}},
series = {{Biochemical and Biophysical Research Communications}},
title = {{Association of coatomer proteins with the beta-receptor for platelet-derived growth factor}},
url = {{http://dx.doi.org/10.1006/bbrc.1997.6821}},
doi = {{10.1006/bbrc.1997.6821}},
volume = {{235}},
year = {{1997}},
}