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Related Experiment Videos

Bcr phosphorylated on tyrosine 177 binds Grb2

G Ma1, D Lu, Y Wu

  • 1Department of Molecular Pathology, The University of Texas, M.D. Anderson Cancer Centre, Houston 77030, USA.

Oncogene
|May 15, 1997
PubMed
Summary

The Bcr protein binds to Grb2 when phosphorylated at tyrosine 177. This interaction is crucial for Bcr

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Area of Science:

  • Molecular Biology
  • Oncology
  • Cell Signaling

Background:

  • The Bcr-Abl oncoprotein is known to interact with Ras pathway activators like Grb2 and Shc.
  • Grb2 binding to Bcr-Abl occurs at a specific phosphorylated tyrosine residue (Y177) within the BCR gene's first exon.

Purpose of the Study:

  • To investigate if Bcr, when tyrosine phosphorylated by c-Abl within cells, can bind Grb2.
  • To determine if phosphotyrosine 177 is the primary binding site for Grb2 interaction with Bcr.

Main Methods:

  • Co-expression of Bcr and Abl proteins in COS1 cells and a hemopoietic cell line.
  • Tyrosine phosphorylation analysis of Bcr and its deletion mutants using activated c-Abl.
  • Co-precipitation assays with Grb2 and studies using GST-SH2 (Grb2) to assess binding affinity.

Main Results:

  • Bcr and Abl protein complexes were detected in cellular models.
  • Tyrosine phosphorylation of Bcr at Y177 by activated c-Abl was confirmed.
  • Wild-type Bcr showed efficient Grb2 binding, while the Y177F mutant exhibited significantly reduced Grb2 binding.

Conclusions:

  • Phosphorylation of Bcr at tyrosine 177 is essential for its binding to Grb2.
  • This interaction suggests Bcr's role as a potential activator of the Ras pathway.

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