Bcr phosphorylated on tyrosine 177 binds Grb2

Oncogene
G MaR B Arlinghaus

Abstract

We and others have shown that the Bcr-Abl oncoprotein binds activators of the Ras pathway such as Grb2 and Shc. Grb2 binding is mediated through a phosphorylated tyrosine residue (Y177) located within a consensus Grb2 binding site encoded by the first exon of the BCR gene. Our results indicate that P160 BCR is tyrosine phosphorylated at the same site by Bcr-Abl in kinase assays (Puil et al., 1994). We performed experiments to determine whether Bcr, which was tyrosine phosphorylated within cells by activated c-Abl, could also bind Grb2, and whether phosphotyrosine 177 was the major binding site. Complexes between Bcr and Abl were detected in a hemopoietic cell line lacking Bcr-Abl and in COS1 cells coexpressing both Bcr and Abl proteins. P160 BCR was tyrosine phosphorylated in COS1 cells coexpressing Abl and Bcr proteins. Similarly, various deletion mutants of Bcr including BCRN553, BCRN413 and BCRN221 were tyrosine phosphorylated by activated c-Abl whereas BCRN159 was not. Wild-type Bcr and Bcr Y177F were examined under these conditions for their ability to co-precipitate with Grb2. The results showed that while wild-type tyrosine phosphorylated Bcr efficiently bound Grb2, tyrosine phosphorylated Bcr Y177F had greatly reduced G...Continue Reading

Citations

May 10, 2001·International Journal of Hematology·Y Maru
Jul 3, 2009·Blood·Margret S FernandesMartin Sattler
Jan 11, 2003·Proceedings of the National Academy of Sciences of the United States of America·Arthur R SalomonEric C Peters
Jul 5, 2005·Biochemical and Biophysical Research Communications·S FlamantA G Turhan
Oct 25, 2016·Future Medicinal Chemistry·Pedro Alves Bezerra MoraisHeberth de Paula
Aug 12, 1999·Oncogene·Y WuR B Arlinghaus
Dec 14, 2001·The Journal of Biological Chemistry·Zaruhi PoghosyanDylan R Edwards
Feb 10, 2021·Biology·Elena VueltaManuel Sánchez-Martín

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