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Phosphorylation of the PDGF receptor beta subunit creates a tight binding site for phosphatidylinositol 3 kinase.

1990; Springer Nature; Volume: 9; Issue: 10 Linguagem: Inglês

10.1002/j.1460-2075.1990.tb07527.x

1460-2075

A. Kazlauskas, Jonathan A. Cooper,

Receptor Mechanisms and Signaling

Research Article1 October 1990free access Phosphorylation of the PDGF receptor beta subunit creates a tight binding site for phosphatidylinositol 3 kinase. A. Kazlauskas A. Kazlauskas Department of Cell Biology, Fred Hutchinson Cancer Research Center, Seattle, WA 98104. Search for more papers by this author J. A. Cooper J. A. Cooper Department of Cell Biology, Fred Hutchinson Cancer Research Center, Seattle, WA 98104. Search for more papers by this author A. Kazlauskas A. Kazlauskas Department of Cell Biology, Fred Hutchinson Cancer Research Center, Seattle, WA 98104. Search for more papers by this author J. A. Cooper J. A. Cooper Department of Cell Biology, Fred Hutchinson Cancer Research Center, Seattle, WA 98104. Search for more papers by this author Author Information A. Kazlauskas1 and J. A. Cooper1 1Department of Cell Biology, Fred Hutchinson Cancer Research Center, Seattle, WA 98104. The EMBO Journal (1990)9:3279-3286https://doi.org/10.1002/j.1460-2075.1990.tb07527.x PDFDownload PDF of article text and main figures. ToolsAdd to favoritesDownload CitationsTrack CitationsPermissions ShareFacebookTwitterLinked InMendeleyWechatReddit Figures & Info The beta subunit of the platelet derived growth factor receptor (PDGFR) coprecipitates with a phosphatidyl-inositol 3 kinase activity (PI3K) following stimulation of cells by PDGF. Mutagenesis of a tyrosine (Y) phosphorylation site, Y751, in the PDGFR, greatly reduces PI3K, consistent with the possibility that phosphorylation of Y751 signals association of PI3K. To test this we have reconstituted the binding of the PDGFR beta subunit and PI3K in vitro. Binding is rapid, saturable and requires phosphorylation of the PDGFR at Y751, but does not require PDGF-dependent phosphorylation of PI3K. To test which portions of the PDGFR are important for binding, we used an antibody to a small region of the receptor that includes Y751. This antibody blocked in vitro binding of PI3K to the receptor, while an antiserum to the C-terminus of the receptor had no effect on binding of PI3K. In addition, we found that PDGF stimulation of a cell results in the association of essentially all the PI3K activity with cellular PDGFRs. These data suggest that PI3K is a specific ligand for PDGF receptors that are phosphorylated at Y751. Previous ArticleNext Article Volume 9Issue 101 October 1990In this issue RelatedDetailsLoading ...