PMID: 8603102Mar 27, 1996Paper

Association of phosphatidylinositol 3-kinase, via the SH2 domains of p85, with focal adhesion kinase in polyoma middle t-transformed fibroblasts

Biochimica Et Biophysica Acta
C BachelotLewis C Cantley

Abstract

Focal adhesion kinase (FAK), a non-receptor protein tyrosine kinase, becomes activated and phosphorylated on tyrosine in cells transformed with v-src. By cytoimmunofluorescence a sub-fraction of the p85 subunit of phosphoinositide 3-kinase (PI 3-kinase) localized in focal adhesion plaques. We examined the possibility that FAK associates with PI 3-kinase. In fibroblasts transformed with polyoma middle t, PI 3-kinase activity co-immunoprecipitated with pp125FAK using two different antibodies against this protein. PP125FAK from middle t-transformed cells associated with a glutathione-S-transferase fusion protein containing the 85-kDa subunit of phosphatidylinositol 3-kinase. Both of the SH2 domains and the SH3 domain of p85 also formed complexes with pp125FAK in vitro. Phosphopeptides that bind to the SH2 domains completely blocked the binding of full-length p85 to pp125FAK, while a peptide that binds to the SH3 domain was ineffective, indicating that the association between p85 and pp125FAK is mediated by the SH2 domains of p85.

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Citations

Oct 16, 2008·The Journal of Biological Chemistry·Dominic P Del ReJoan Heller Brown
Dec 9, 2016·International Journal of Molecular Sciences·Daniela BianconiGerald W Prager
Jan 27, 1998·The Journal of Biological Chemistry·J A GreenwoodJ E Murphy-Ullrich
Feb 1, 1997·BioEssays : News and Reviews in Molecular, Cellular and Developmental Biology·S K Hanks, T R Polte
Mar 17, 2016·Oncotarget·Rajani KantetiRavi Salgia
Jul 15, 2020·Biophysics Reviews·Mihai Pruna, Elisabeth Ehler
Jul 19, 2020·Clinical Oral Investigations·Ibrahim O BelloPentti Nieminen
Nov 6, 2002·Biochimica Et Biophysica Acta·James W DennisMichael Demetriou

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