Search: WFRF:(Engström Henrik)
> (1980-1999) >
Demonstration of fu...
Demonstration of functionally different interactions between phospholipase C-gamma and the two types of platelet-derived growth factor receptors
-
- Eriksson, Anders (author)
- Ludwig Institute for Cancer Research, Uppsala, Sweden
-
- Nånberg, Eewa, 1957- (author)
- Department of Pathology, University Hospital, Uppsala, Sweden,Uppsala universitet, Medicinska vetenskapsområdet, Medicinska fakulteten, Institutionen för genetik och patologi
-
- Rönnstrand, Lars (author)
- Ludwig Institute for Cancer Research, Uppsala, Sweden
-
show more...
-
- Engström, Ulla (author)
- Ludwig Institute for Cancer Research, Uppsala, Sweden
-
- Hellman, Ulf (author)
- Ludwig Institute for Cancer Research, Uppsala, Sweden
-
- Rupp, Eva (author)
- Ludwig Institute for Cancer Research, Uppsala, Sweden
-
- Carpenter, Graham (author)
- Department of Biochemistry, School of Medicine, Vanderbilt University, Nashville, Tennessee
-
- Heldin, Carl-Henrik (author)
- Ludwig Institute for Cancer Research, Uppsala, Sweden
-
- Claesson-Welsh, Lena (author)
- Ludwig Institute for Cancer Research, Uppsala, Sweden
-
show less...
-
(creator_code:org_t)
- American Society for Biochemistry and Molecular Biology, 1995
- 1995
- English.
-
In: Journal of Biological Chemistry. - : American Society for Biochemistry and Molecular Biology. - 0021-9258 .- 1083-351X. ; 270:13, s. 7773-7781
- Related links:
-
https://doi.org/10.1...
-
show more...
-
http://www.jbc.org/a...
-
https://urn.kb.se/re...
-
https://doi.org/10.1...
-
https://urn.kb.se/re...
-
show less...
Abstract
Subject headings
Close
- Phosphorylated tyrosine residues in receptor tyrosine kinases serve as binding sites for signal transduction molecules. We have identified two autophosphorylation sites, Tyr-988 and Tyr-1018, in the platelet-derived growth factor (PDGF) alpha-receptor carboxyl-terminal tail, which are involved in binding of phospholipase C-gamma (PLC-gamma). The capacities of the Y988F and Y1018F mutant PDGF alpha-receptors, expressed in porcine aortic endothelial cells, to bind PLC-gamma are 60 and 5% of that of the wild-type receptor, respectively. Phosphorylated but not unphosphorylated peptides containing Tyr-1018 are able to compete with the intact receptor for binding to immobilized PLC-gamma SH2 domains; a phosphorylated Tyr-988 peptide competes 10 times less efficiently. The complex between PLC-gamma and the PDGF alpha-receptor is more stable than that of PLC-gamma and the PDGF beta-receptor. However, PDGF stimulation results in a smaller fraction of tyrosine-phosphorylated PLC-gamma and a smaller accumulation of inositol trisphosphate in cells expressing the alpha-receptor as compared with cells expressing the beta-receptor. We conclude that phosphorylated Tyr-988 and Tyr-1018 in the PDGF alpha-receptor carboxyl-terminal tail bind PLC-gamma, but this association leads to only a relatively low level of tyrosine phosphorylation and activation of PLC-gamma.
Subject headings
- MEDICIN OCH HÄLSOVETENSKAP -- Medicinska och farmaceutiska grundvetenskaper -- Cell- och molekylärbiologi (hsv//swe)
- MEDICAL AND HEALTH SCIENCES -- Basic Medicine -- Cell and Molecular Biology (hsv//eng)
Publication and Content Type
- ref (subject category)
- art (subject category)
Find in a library
To the university's database
- By the author/editor
-
Eriksson, Anders
-
Nånberg, Eewa, 1 ...
-
Rönnstrand, Lars
-
Engström, Ulla
-
Hellman, Ulf
-
Rupp, Eva
-
show more...
-
Carpenter, Graha ...
-
Heldin, Carl-Hen ...
-
Claesson-Welsh, ...
-
show less...
- About the subject
-
- MEDICAL AND HEALTH SCIENCES
-
MEDICAL AND HEAL ...
-
and Basic Medicine
-
and Cell and Molecul ...
- Articles in the publication
-
Journal of Biolo ...
- By the university
-
Örebro University
-
Karlstad University