Erythropoietin activates Raf1 by an Shc-independent pathway in CTLL-EPO-R cells.

No abstract is available for this paper.

• Publication year

  1997

• Venue

  Blood

• Publication date

  Unknown publication date

• Fields of study

  Biology, Medicine

• Identifiers
  DOI 10.1182/BLOOD.V89.1.55.55_55_64PMID 8978277
• External record

  Open on Semantic Scholar

• Source metadata

  Semantic Scholar, PubMed

• No claims are published for this paper.

• No concepts are published for this paper.

• Evidence for a role for the phosphotyrosine-binding domain of Shc in interleukin 2 signaling.

  1996cited by this paper
• Tyrosine phosphorylation of Shc is not required for proliferation or viability signaling by granulocyte-macrophage colony-stimulating factor in hematopoietic cell lines.

  1996cited by this paper
• The 145-kDa protein induced to associate with Shc by multiple cytokines is an inositol tetraphosphate and phosphatidylinositol 3,4,5-triphosphate 5-phosphatase.

  1996cited by this paper
• Tyrosine 425 within the activated erythropoietin receptor binds Syp, reduces the erythropoietin required for Syp tyrosine phosphorylation, and promotes mitogenesis.

  1996cited by this paper
• Multiple forms of an inositol polyphosphate 5-phosphatase form signaling complexes with Shc and Grb2.

  1996cited by this paper
• Erythropoietin induces activation of Stat5 through association with specific tyrosines on the receptor that are not required for a mitogenic response

  1996cited by this paper
• p150Ship, a signal transduction molecule with inositol polyphosphate-5-phosphatase activity.

  1996cited by this paper
• Evidence for a Physical Association between the Shc-PTB Domain and the βc Chain of the Granulocyte-Macrophage Colony-stimulating Factor Receptor (*)

  1996cited by this paper
• Erythropoietin-induced recruitment of Shc via a receptor phosphotyrosine-independent, Jak2-associated pathway

  1995cited by this paper
• PTB domain binding to signaling proteins through a sequence motif containing phosphotyrosine.

  1995cited by this paper
• Analysis of Interleukin-2-dependent Signal Transduction through the Shc/Grb2 Adapter Pathway

  1995cited by this paper
• Specificity of the PTB Domain of Shc for β Turn-forming Pentapeptide Motifs Amino-terminal to Phosphotyrosine (*)

  1995cited by this paper
• Growth Hormone-promoted Tyrosyl Phosphorylation of SHC Proteins and SHC Association with Grb2 (*)

  1995cited by this paper
• The Phosphotyrosine Interaction Domain of SHC Recognizes Tyrosine-phosphorylated NPXY Motif (*)

  1995cited by this paper
• Protein modules and signalling networks

  1995cited by this paper
• Protein tyrosine kinase Syk is associated with and activated by the IL-2 receptor: possible link with the c-myc induction pathway.

  1995cited by this paper
• Interaction of Shc with Grb2 regulates association of Grb2 with mSOS

  1995cited by this paper
• Overexpression of Shc proteins potentiates the proliferative response to the granulocyte-macrophage colony-stimulating factor and recruitment of Grb2/SoS and Grb2/p140 complexes to the beta receptor subunit.

  1995cited by this paper
• Distinct regions of c-Mpl cytoplasmic domain are coupled to the JAK-STAT signal transduction pathway and Shc phosphorylation.

  1995cited by this paper
• Involvement of SH2-containing Phosphotyrosine Phosphatase Syp in Erythropoietin Receptor Signal Transduction Pathways (*)

  1995cited by this paper
• The c-Mpl Ligand (Thrombopoietin) Stimulates Tyrosine Phosphorylation of Jak2, Shc, and c-Mpl (*)

  1995cited by this paper
• The PTB domain: a new protein module implicated in signal transduction.

  1995cited by this paper
• Tyrosine phosphorylation of the erythropoietin receptor: role for differentiation and mitogenic signal transduction.

  1995cited by this paper
• Interleukin 2 and erythropoietin activate STAT5/MGF via distinct pathways.

  1995cited by this paper
• Trk receptors use redundant signal transduction pathways involving SHC and PLC-gamma 1 to mediate NGF responses.

  1994cited by this paper
• A region in Shc distinct from the SH2 domain can bind tyrosine-phosphorylated growth factor receptors.

  1994cited by this paper
• Trk receptors use redundant signal transduction pathways involving SHC and PLC-γ1 to mediate NGF responses

  1994cited by this paper
• Involvement of the Jak-3 Janus kinase in signalling by interleukins 2 and 4 in lymphoid and myeloid cells

  1994cited by this paper
• Protein-tyrosine-phosphatase SHPTP2 couples platelet-derived growth factor receptor beta to Ras.

  1994cited by this paper
• An alternative to SH2 domains for binding tyrosine-phosphorylated proteins.

  1994cited by this paper
• JAK2 associates with the beta c chain of the receptor for granulocyte-macrophage colony-stimulating factor, and its activation requires the membrane-proximal region

  1994cited by this paper
• Formation of Shc-Grb2 complexes is necessary to induce neoplastic transformation by overexpression of Shc proteins.

  1994cited by this paper
• Multiple hemopoietins, with the exception of interleukin-4, induce modification of Shc and mSos1, but not their translocation.

  1994cited by this paper
• A new function for a phosphotyrosine phosphatase: linking GRB2-Sos to a receptor tyrosine kinase

  1994cited by this paper
• Hierarchy of binding sites for Grb2 and Shc on the epidermal growth factor receptor

  1994cited by this paper
• The adapter protein Shc interacts with the interleukin-2 (IL-2) receptor upon IL-2 stimulation.

  1994cited by this paper
• Activation of the mitogen-activated protein kinase pathway by the erythropoietin receptor.

  1994cited by this paper
• Gene transfer of the interleukin (IL)‐2 receptor β chain into an IL‐7‐dependent pre‐B cell line permits IL‐2‐driven proliferation: Tyrosine phosphorylation of Shc is induced by IL‐2 but not IL‐7

  1994cited by this paper
• Tyrosine phosphorylation of Shc is induced by IL-3, IL-5 and GM-CSF.

  1994cited by this paper
• Erythropoietin and interleukin-2 activate distinct JAK kinase family members

  1994cited by this paper
• Interaction of the protein kinase Raf-1 with 14-3-3 proteins.

  1994cited by this paper
• Specific motifs recognized by the SH2 domains of Csk, 3BP2, fps/fes, GRB-2, HCP, SHC, Syk, and Vav

  1994cited by this paper
• Neuronal differentiation signals are controlled by nerve growth factor receptor/Trk binding sites for SHC and PLC gamma.

  1994cited by this paper
• Shc phosphorylation in myeloid cells is regulated by granulocyte macrophage colony-stimulating factor, interleukin-3, and steel factor and is constitutively increased by p210BCR/ABL.

  1994cited by this paper
• A dominant negative erythropoietin (EPO) receptor inhibits EPO-dependent growth and blocks F-gp55-dependent transformation

  1994cited by this paper
• Interleukin-2-induced tyrosine phosphorylation of Shc proteins correlates with factor-dependent T cell proliferation.

  1994cited by this paper
• Activation of mitogen-activated protein kinase cascade through erythropoietin receptor.

  1994cited by this paper
• Activated Ki-Ras complements erythropoietin signaling in CTLL-2 cells, inducing tyrosine phosphorylation of a 160-kDa protein.

  1994cited by this paper
• 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.

  1994cited by this paper
• The function of GRB2 in linking the insulin receptor to Ras signaling pathways.

  1993cited by this paper
• Guanine-nucleotide-releasing factor hSos1 binds to Grb2 and links receptor tyrosine kinases to Ras signalling

  1993cited by this paper
• The SH2 and SH3 domains of mammalian Grb2 couple the EGF receptor to the Ras activator mSos1

  1993cited by this paper
• The 64-kDa protein that associates with the platelet-derived growth factor receptor beta subunit via Tyr-1009 is the SH2-containing phosphotyrosine phosphatase Syp.

  1993cited by this paper
• Interleukin-2-induced tyrosine phosphorylation of p52shc in T lymphocytes.

  1993cited by this paper
• Inactivation of erythropoietin receptor function by point mutations in a region having homology with other cytokine receptors

  1993cited by this paper
• Activation of a phosphotyrosine phosphatase by tyrosine phosphorylation.

  1993cited by this paper
• JAK2 associates with the erythropoietin receptor and is tyrosine phosphorylated and activated following stimulation with erythropoietin.

  1993cited by this paper
• Epidermal growth factor regulates p21ras through the formation of a complex of receptor, Grb2 adapter protein, and Sos nucleotide exchange factor.

  1993cited by this paper
• Association of p56lck with IL‐2 receptor beta chain is critical for the IL‐2‐induced activation of p56lck.

  1993cited by this paper
• Binding of the Ras activator son of sevenless to insulin receptor substrate-1 signaling complexes.

  1993cited by this paper
• Grb2 mediates the EGF-dependent activation of guanine nucleotide exchange on Ras

  1993cited by this paper
• Multiple cytokines induce the tyrosine phosphorylation of Shc and its association with Grb2 in hemopoietic cells.

  1993cited by this paper
• Ligand-dependent activation of chimeric receptors with the cytoplasmic domain of the interleukin-3 receptor beta subunit (beta IL3).

  1993cited by this paper
• A widely expressed human protein-tyrosine phosphatase containing src homology 2 domains.

  1993cited by this paper
• Erythropoietin stimulates the tyrosine phosphorylation of Shc and its association with Grb2 and a 145-Kd tyrosine phosphorylated protein.

  1993cited by this paper
• Association of Sos Ras exchange protein with Grb2 is implicated in tyrosine kinase signal transduction and transformation

  1993cited by this paper
• Solubilization and purification of enzymatically active glutathione S-transferase (pGEX) fusion proteins.

  1993cited by this paper
• Signal transduction by the high‐affinity GM‐CSF receptor: two distinct cytoplasmic regions of the common beta subunit responsible for different signaling.

  1993cited by this paper
• Activation of the erythropoietin receptor by the Friend spleen focus-forming virus gp55 glycoprotein induces constitutive protein tyrosine phosphorylation.

  1992cited by this paper
• Molecular cloning of a novel protein‐tyrosine phosphatase SH‐PTP3 with sequence similarity to the src‐homology region 2

  1992cited by this paper
• The SH2 and SH3 domain-containing protein GRB2 links receptor tyrosine kinases to ras signaling.

  1992cited by this paper
• A novel transforming protein (SHC) with an SH2 domain is implicated in mitogenic signal transduction.

  1992cited by this paper
• Identification of a human src homology 2-containing protein-tyrosine-phosphatase: a putative homolog of Drosophila corkscrew.

  1992cited by this paper
• 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.

  1992cited by this paper
• Distinct downstream signaling mechanism between erythropoietin receptor and interleukin‐2 receptor.

  1992cited by this paper
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  1991cited by this paper
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  1991cited by this paper
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  1991cited by this paper
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  1991cited by this paper
• Induction of tyrosine phosphorylation by the erythropoietin receptor correlates with mitogenesis

  1991cited by this paper
• The cytoplasmic region of the erythropoietin receptor contains nonoverlapping positive and negative growth-regulatory domains

  1991cited by this paper
• Friend spleen focus-forming virus induces factor independence in an erythropoietin-dependent erythroleukemia cell line

  1990cited by this paper
• Expression cloning of the murine erythropoietin receptor.

  1989cited by this paper
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  1977cited by this paper

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  2003cites this paper
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  2003cites this paper
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  2003cites this paper
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