Shc associates with the IL-3 receptor β subunit, SHIP and Gab2 following IL-3 stimulation

[1]  T. Hirano,et al.  Gab-family adapter proteins act downstream of cytokine and growth factor receptors and T- and B-cell antigen receptors. , 1999, Blood.

[2]  J. C. Pratt,et al.  Cloning of p97/Gab2, the major SHP2-binding protein in hematopoietic cells, reveals a novel pathway for cytokine-induced gene activation. , 1998, Molecular cell.

[3]  Keigo Nishida,et al.  Gab1 Acts as an Adapter Molecule Linking the Cytokine Receptor gp130 to ERK Mitogen-Activated Protein Kinase , 1998, Molecular and Cellular Biology.

[4]  M. Scheid,et al.  Dissociation of cytokine-induced phosphorylation of Bad and activation of PKB/akt: involvement of MEK upstream of Bad phosphorylation. , 1998, Proceedings of the National Academy of Sciences of the United States of America.

[5]  Y. Kido,et al.  Shc phosphotyrosine-binding domain dominantly interacts with epidermal growth factor receptors and mediates Ras activation in intact cells. , 1998, Molecular endocrinology.

[6]  J. Griffin,et al.  Signaling Functions of the Tyrosine Residues in the βc Chain of the Granulocyte-Macrophage Colony-Stimulating Factor Receptor , 1997 .

[7]  M. Welham,et al.  Interleukin-3 Induces Association of the Protein-tyrosine Phosphatase SHP2 and Phosphatidylinositol 3-Kinase with a 100-kDa Tyrosine-phosphorylated Protein in Hemopoietic Cells* , 1997, The Journal of Biological Chemistry.

[8]  B. Neel,et al.  Characterization of Two SHP-2-associated Binding Proteins and Potential Substrates in Hematopoietic Cells* , 1997, The Journal of Biological Chemistry.

[9]  L. Rohrschneider,et al.  Characterization of a Novel Tyrosine Phosphorylated 100-kDa Protein That Binds to SHP-2 and Phosphatidylinositol 3′-Kinase in Myeloid Cells* , 1997, The Journal of Biological Chemistry.

[10]  M. Welham,et al.  SHP1 and SHP2 protein-tyrosine phosphatases associate with betac after interleukin-3-induced receptor tyrosine phosphorylation. Identification of potential binding sites and substrates. , 1997, The Journal of biological chemistry.

[11]  P. Pelicci,et al.  Shc mediates IL-6 signaling by interacting with gp130 and Jak2 kinase. , 1997, Journal of immunology.

[12]  I. Babic,et al.  The Src Homology 2 (SH2) Domain of SH2-containing Inositol Phosphatase (SHIP) Is Essential for Tyrosine Phosphorylation of SHIP, Its Association with Shc, and Its Induction of Apoptosis* , 1997, The Journal of Biological Chemistry.

[13]  S. Fesik,et al.  Binding Affinities of Tyrosine-phosphorylated Peptides to the COOH-terminal SH2 and NH-terminal Phosphotyrosine Binding Domains of Shc (*) , 1996, The Journal of Biological Chemistry.

[14]  J. Griffin,et al.  Tyrosine phosphorylation of Shc is not required for proliferation or viability signaling by granulocyte-macrophage colony-stimulating factor in hematopoietic cell lines. , 1996, Journal of immunology.

[15]  J. C. Pratt,et al.  Evidence for a Physical Association between the Shc-PTB Domain and the βc Chain of the Granulocyte-Macrophage Colony-stimulating Factor Receptor (*) , 1996, The Journal of Biological Chemistry.

[16]  L. Rohrschneider,et al.  p150Ship, a signal transduction molecule with inositol polyphosphate-5-phosphatase activity. , 1996, Genes & development.

[17]  K. Arai,et al.  Granulocyte-macrophage Colony-stimulating Factor Provokes RAS Activation and Transcription of c-fos through Different Modes of Signaling (*) , 1996, The Journal of Biological Chemistry.

[18]  P. Majerus,et al.  The 145-kDa protein induced to associate with Shc by multiple cytokines is an inositol tetraphosphate and phosphatidylinositol 3,4,5-triphosphate 5-phosphatase. , 1996, Proceedings of the National Academy of Sciences of the United States of America.

[19]  G. Apell,et al.  Affinity, Specificity, and Kinetics of the Interaction of the SHC Phosphotyrosine Binding Domain with Asparagine-X-X-Phosphotyrosine Motifs of Growth Factor Receptors (*) , 1996, The Journal of Biological Chemistry.

[20]  A. Petros,et al.  Structure and ligand recognition of the phosphotyrosine binding domain of Shc , 1995, Nature.

[21]  J. Griffin,et al.  Identification of a viability domain in the granulocyte/macrophage colony-stimulating factor receptor beta-chain involving tyrosine-750. , 1995, Proceedings of the National Academy of Sciences of the United States of America.

[22]  S. Shoelson,et al.  Specificity of the PTB Domain of Shc for β Turn-forming Pentapeptide Motifs Amino-terminal to Phosphotyrosine (*) , 1995, The Journal of Biological Chemistry.

[23]  B. Margolis,et al.  The phosphotyrosine interaction domain of Shc binds an LXNPXY motif on the epidermal growth factor receptor , 1995, Molecular and cellular biology.

[24]  R. Aebersold,et al.  Comparison of the specificity of bacterially expressed cytoplasmic protein-tyrosine phosphatases SHP and SH-PTP2 towards synthetic phosphopeptide substrates. , 1995, European journal of biochemistry.

[25]  L. Cantley,et al.  The Phosphotyrosine Interaction Domain of SHC Recognizes Tyrosine-phosphorylated NPXY Motif (*) , 1995, The Journal of Biological Chemistry.

[26]  A. Ullrich,et al.  Shc Binding to Nerve Growth Factor Receptor Is Mediated by the Phosphotyrosine Interaction Domain (*) , 1995, The Journal of Biological Chemistry.

[27]  C. Turck,et al.  PTB domain binding to signaling proteins through a sequence motif containing phosphotyrosine. , 1995, Science.

[28]  M. Welham,et al.  Interleukin-13 Signal Transduction in Lymphohemopoietic Cells , 1995, The Journal of Biological Chemistry.

[29]  T. Pawson,et al.  A conserved amino-terminal Shc domain binds to phosphotyrosine motifs in activated receptors and phosphopeptides , 1995, Current Biology.

[30]  A. Miyajima,et al.  Interleukin‐3, granulocyte‐macrophage colony stimulating factor and interleukin‐5 transduce signals through two STAT5 homologs. , 1995, The EMBO journal.

[31]  Tony Pawson,et al.  Protein modules and signalling networks , 1995, Nature.

[32]  B. Margolis,et al.  A region in Shc distinct from the SH2 domain can bind tyrosine-phosphorylated growth factor receptors. , 1994, The Journal of biological chemistry.

[33]  G. Krystal,et al.  Multiple cytokines stimulate the binding of a common 145-kilodalton protein to Shc at the Grb2 recognition site of Shc , 1994, Molecular and cellular biology.

[34]  M. Welham,et al.  Interleukin (IL)-3 and granulocyte/macrophage colony-stimulating factor, but not IL-4, induce tyrosine phosphorylation, activation, and association of SHPTP2 with Grb2 and phosphatidylinositol 3'-kinase. , 1994, The Journal of biological chemistry.

[35]  D. Bowtell,et al.  Multiple hemopoietins, with the exception of interleukin-4, induce modification of Shc and mSos1, but not their translocation. , 1994, The Journal of biological chemistry.

[36]  T Pawson,et al.  Direct interaction between Shc and the platelet-derived growth factor beta-receptor. , 1994, The Journal of biological chemistry.

[37]  T Pawson,et al.  Specific motifs recognized by the SH2 domains of Csk, 3BP2, fps/fes, GRB-2, HCP, SHC, Syk, and Vav , 1994, Molecular and cellular biology.

[38]  R. Aebersold,et al.  Characterization and kinetic analysis of the intracellular domain of human protein tyrosine phosphatase beta (HPTP beta) using synthetic phosphopeptides. , 1994, The Biochemical journal.

[39]  F. Jirik,et al.  Characterization of protein tyrosine phosphatase SH-PTP2. Study of phosphopeptide substrates and possible regulatory role of SH2 domains. , 1994, The Journal of biological chemistry.

[40]  A. Miyajima,et al.  Receptors for granulocyte-macrophage colony-stimulating factor, interleukin-3, and interleukin-5 , 1993 .

[41]  J. Cleveland,et al.  Structure of the murine Jak2 protein-tyrosine kinase and its role in interleukin 3 signal transduction. , 1993, Proceedings of the National Academy of Sciences of the United States of America.

[42]  G. Zurawski,et al.  Receptors for interleukin‐13 and interleukin‐4 are complex and share a novel component that functions in signal transduction. , 1993, The EMBO journal.

[43]  T. Pawson,et al.  Epidermal growth factor stimulates the tyrosine phosphorylation of SHC in the mouse. , 1993, The Journal of biological chemistry.

[44]  A. Miyajima,et al.  Critical cytoplasmic domains of the common beta subunit of the human GM‐CSF, IL‐3 and IL‐5 receptors for growth signal transduction and tyrosine phosphorylation. , 1992, The EMBO journal.

[45]  V. Duronio,et al.  Multiple hemopoietic growth factors stimulate activation of mitogen-activated protein kinase family members. , 1992, Journal of immunology.

[46]  T. Pawson,et al.  A novel transforming protein (SHC) with an SH2 domain is implicated in mitogenic signal transduction , 1992, Cell.

[47]  V. Duronio,et al.  p21ras activation via hemopoietin receptors and c-kit requires tyrosine kinase activity but not tyrosine phosphorylation of p21ras GTPase-activating protein. , 1992, Proceedings of the National Academy of Sciences of the United States of America.

[48]  K. Arai,et al.  Expression cloning of the human IL-3 receptor cDNA reveals a shared β subunit for the human IL-3 and GM-CSF receptors , 1991, Cell.

[49]  J. Tavernier,et al.  A human high affinity interleukin-5 receptor (IL5R) is composed of an IL5-specific α chain and a β chain shared with the receptor for GM-CSF , 1991, Cell.

[50]  K. Miyazono,et al.  Establishment and characterization of a unique human cell line that proliferates dependently on GM‐CSF, IL‐3, or erythropoietin , 1989, Journal of cellular physiology.

[51]  M. Steinmetz,et al.  IL3-dependent mouse clones that express B-220 surface antigen, contain ig genes in germ-line configuration, and generate B lymphocytes in vivo , 1985, Cell.

[52]  U. K. Laemmli,et al.  Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4 , 1970, Nature.

[53]  J. Ihle,et al.  Interleukin-3 and hematopoiesis. , 1992, Chemical immunology.

[54]  T. Yokota,et al.  Cytokines: coordinators of immune and inflammatory responses. , 1990, Annual review of biochemistry.

[55]  J. Schrader The panspecific hemopoietin of activated T lymphocytes (interleukin-3). , 1986, Annual review of immunology.