oru.sePublications
Change search
CiteExportLink to record
Permanent link

Direct link
Cite
Citation style
  • apa
  • ieee
  • modern-language-association-8th-edition
  • vancouver
  • Other style
More styles
Language
  • de-DE
  • en-GB
  • en-US
  • fi-FI
  • nn-NO
  • nn-NB
  • sv-SE
  • Other locale
More languages
Output format
  • html
  • text
  • asciidoc
  • rtf
Demonstration of functionally different interactions between phospholipase C-gamma and the two types of platelet-derived growth factor receptors
Ludwig Institute for Cancer Research, Uppsala, Sweden.
Department of Pathology, University Hospital, Uppsala, Sweden.ORCID iD: 0000-0001-8889-5803
Ludwig Institute for Cancer Research, Uppsala, Sweden.
Ludwig Institute for Cancer Research, Uppsala, Sweden.
Show others and affiliations
1995 (English)In: Journal of Biological Chemistry, ISSN 0021-9258, E-ISSN 1083-351X, Vol. 270, no 13, p. 7773-7781Article in journal (Refereed) Published
Abstract [en]

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.

Place, publisher, year, edition, pages
American Society for Biochemistry and Molecular Biology, 1995. Vol. 270, no 13, p. 7773-7781
National Category
Medical and Health Sciences Cell and Molecular Biology
Identifiers
URN: urn:nbn:se:oru:diva-79023DOI: 10.1074/jbc.270.13.7773ISI: A1995QQ43100107PubMedID: 7535778Scopus ID: 2-s2.0-0028951440OAI: oai:DiVA.org:oru-79023DiVA, id: diva2:1386795
Funder
Magnus Bergvall FoundationNIH (National Institute of Health), CA43720
Note

This work was supported by the Swedish Natural Science Research Council, Magn. Bergvall Fund, and by National Institutes of Health Grant CA43720. The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore by hereby marked “advertisement” in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

Available from: 2013-10-20 Created: 2020-01-20 Last updated: 2020-01-24Bibliographically approved

Open Access in DiVA

No full text in DiVA

Other links

Publisher's full textPubMedScopus

Authority records BETA

Nånberg, Eewa

Search in DiVA

By author/editor
Nånberg, Eewa
In the same journal
Journal of Biological Chemistry
Medical and Health SciencesCell and Molecular Biology

Search outside of DiVA

GoogleGoogle Scholar

doi
pubmed
urn-nbn

Altmetric score

doi
pubmed
urn-nbn
Total: 29 hits
CiteExportLink to record
Permanent link

Direct link
Cite
Citation style
  • apa
  • ieee
  • modern-language-association-8th-edition
  • vancouver
  • Other style
More styles
Language
  • de-DE
  • en-GB
  • en-US
  • fi-FI
  • nn-NO
  • nn-NB
  • sv-SE
  • Other locale
More languages
Output format
  • html
  • text
  • asciidoc
  • rtf