Functional co-operation between the subunits in heterodimeric platelet-derived growth factor receptor complexes
Emaduddin, Muhammad ; Ekman, Simon ; Rönnstrand, Lars LU
and Heldin, Carl-Henrik
(1999)
In Biochemical Journal
341(3).
p.523-528
- Abstract
- 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... (More)
- 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. (Less)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/1782696
- author
- Emaduddin, Muhammad
; Ekman, Simon
; Rönnstrand, Lars
LU
and Heldin, Carl-Henrik
- publishing date
- 1999
- type
- Contribution to journal
- publication status
- published
- subject
- 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
- in
- Biochemical Journal
- volume
- 341
- issue
- 3
- pages
- 523 - 528
- publisher
- Portland Press
- external identifiers
-
- scopus:0033179048
- ISSN
- 0264-6021
- 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
- 7227e1c8-1d33-4f6c-9966-e0b7a36dcce8 (old id 1782696)
- alternative location
- http://www.ncbi.nlm.nih.gov/pmc/articles/PMC1220387/
- date added to LUP
- 2016-04-04 09:09:27
- date last changed
- 2022-03-23 04:16:19
@article{7227e1c8-1d33-4f6c-9966-e0b7a36dcce8,
abstract = {{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.}},
author = {{Emaduddin, Muhammad and Ekman, Simon and Rönnstrand, Lars and Heldin, Carl-Henrik}},
issn = {{0264-6021}},
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}},
language = {{eng}},
number = {{3}},
pages = {{523--528}},
publisher = {{Portland Press}},
series = {{Biochemical Journal}},
title = {{Functional co-operation between the subunits in heterodimeric platelet-derived growth factor receptor complexes}},
url = {{http://www.ncbi.nlm.nih.gov/pmc/articles/PMC1220387/}},
volume = {{341}},
year = {{1999}},
}