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Social Bookmarking                   What's this?  Previous Article  |  Table of Contents  |  Next Article  Blood, Vol. 93 No. 6 (March 15), 1999: pp. 1809-1816 RAPID COMMUNICATION Gab-Family Adapter Proteins Act Downstream of Cytokine and Growth Factor Receptors and T- and B-Cell Antigen Receptors Keigo Nishida, Yuichi Yoshida, Motoyuki Itoh, Toshiyuki Fukada, Takuya Ohtani, Takahiro Shirogane, Toru Atsumi, Mariko Takahashi-Tezuka, Katsuhiko Ishihara, Masahiko Hibi, and Toshio Hirano From the Division of Molecular Oncology, Biomedical Research Center, Osaka University Medical School, Osaka, Japan. We previously found that the adapter protein Gab1 (110 kD) is tyrosine-phosphorylated and forms a complex with SHP-2 and PI-3 kinase upon stimulation through either the interleukin-3 receptor (IL-3R) or gp130, the common receptor subunit of IL-6-family cytokines. In this report, we identified another adapter molecule (100 kD) interacting with SHP-2 and PI-3 kinase in response to various stimuli. The molecule displays striking homology to Gab1 at the amino acid level; thus, we named it Gab2. It contains a PH domain, proline-rich sequences, and tyrosine residues that bind to SH2 domains when they are phosphorylated. Gab1 is phosphorylated on tyrosine upon stimulation through the thrombopoietin receptor (TPOR), stem cell factor receptor (SCFR), and T-cell and B-cell antigen receptors (TCR and BCR, respectively), in addition to IL-3R and gp130. Tyrosine phosphorylation of Gab2 was induced by stimulation through gp130, IL-2R, IL-3R, TPOR, SCFR, and TCR. Gab1 and Gab2 were shown to be substrates for SHP-2 in vitro. Overexpression of Gab2 enhanced the gp130 or Src-related kinases-mediated ERK2 activation as that of Gab1 did. These data indicate that Gab-family molecules act as adapters for transmitting various signals. 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Gold The Gab1 Docking Protein Links the B Cell Antigen Receptor to the Phosphatidylinositol 3-Kinase/Akt Signaling Pathway and to the SHP2 Tyrosine Phosphatase J. Biol. Chem., April 6, 2001; 276(15): 12257 - 12265. [Abstract] [Full Text] [PDF] S. Yamasaki, K. Nishida, M. Hibi, M. Sakuma, R. Shiina, A. Takeuchi, H. Ohnishi, T. Hirano, and T. Saito Docking Protein Gab2 Is Phosphorylated by ZAP-70 and Negatively Regulates T Cell Receptor Signaling by Recruitment of Inhibitory Molecules J. Biol. Chem., November 21, 2001; 276(48): 45175 - 45183. [Abstract] [Full Text] [PDF] F. Mazerolles, C. Barbat, M. Trucy, W. Kolanus, and A. Fischer Molecular Events Associated with CD4-mediated Down-regulation of LFA-1-dependent Adhesion J. Biol. Chem., January 4, 2002; 277(2): 1276 - 1283. [Abstract] [Full Text] [PDF]

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