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GRB2  -  growth factor receptor-bound protein 2

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High impact information on GRB2

  • We now show that receptor-induced tyrosine phosphorylation of NTAL and concomitant Grb2 complex formation critically modulate the Ca(2+) response without affecting SLP-65 and PLC-gamma2 phosphorylation [1].
  • Grb2 and the non-T cell activation linker NTAL constitute a Ca(2+)-regulating signal circuit in B lymphocytes [1].
  • Here we show that the Src ThrEF1Trp SH2 domain mutant binds pYVNV phosphopeptides in a beta turn conformation, which, despite differing conformations of the interacting tryptophan, closely resembles the native Grb2/pYVNV cognate peptide binding mode [2].
  • Transformation and pp60v-src autophosphorylation correlate with SHC-GRB2 complex formation in rat and chicken cells expressing host-range and kinase-active, transformation-defective alleles of v-src [3].
  • We found that relative to the wild-type receptor, enhanced binding to Grb2 further increases the incorporation of bromodeoxyuridine and the expression of Twist, while decreasing that of p27(Kip1) and myogenin [4].
 

Biological context of GRB2

  • Furthermore, association of phosphorylated SHC with the adapter GRB2 correlated with increased anchorage-independent growth (and autophosphorylation) in both rat and chicken cells independent of the morphological phenotype induced [3].
 

Anatomical context of GRB2

  • Preferential binding of Grb2 or phosphatidylinositol 3-kinase to the met receptor has opposite effects on HGF-induced myoblast proliferation [4].
 

Associations of GRB2 with chemical compounds

  • Thus, elevation of Ca(2+) is regulated by at least two signaling modules, the B cell-specific Ca(2+) initiation complex comprising SLP-65, Btk, and PLC-gamma2 and the more ubiquitously expressed NTAL/Grb2 complex, which acts as an amplifier by switching off inhibitory elements [1].

References

  1. Grb2 and the non-T cell activation linker NTAL constitute a Ca(2+)-regulating signal circuit in B lymphocytes. Stork, B., Engelke, M., Frey, J., Horejsí, V., Hamm-Baarke, A., Schraven, B., Kurosaki, T., Wienands, J. Immunity (2004) [Pubmed]
  2. Structural basis for specificity switching of the Src SH2 domain. Kimber, M.S., Nachman, J., Cunningham, A.M., Gish, G.D., Pawson, T., Pai, E.F. Mol. Cell (2000) [Pubmed]
  3. Transformation and pp60v-src autophosphorylation correlate with SHC-GRB2 complex formation in rat and chicken cells expressing host-range and kinase-active, transformation-defective alleles of v-src. Verderame, M.F., Guan, J.L., Woods Ignatoski, K.M. Mol. Biol. Cell (1995) [Pubmed]
  4. Preferential binding of Grb2 or phosphatidylinositol 3-kinase to the met receptor has opposite effects on HGF-induced myoblast proliferation. Leshem, Y., Gitelman, I., Ponzetto, C., Halevy, O. Exp. Cell Res. (2002) [Pubmed]
 
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