The SH2 inositol 5-phosphatase Ship1 is recruited in an SH2-dependent manner to the erythropoietin receptor (Q28144156)

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Q Liu

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D J Dumont

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D L Barber

Journal of Biological Chemistry

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language of work or name

English

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publication date

11 February 2000

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published in

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volume

275

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issue

6

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page(s)

4398-406

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cites work

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Crystallographic evidence for preformed dimers of erythropoietin receptor before ligand activation

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Generation of committed erythroid BFU-E and CFU-E progenitors does not require erythropoietin or the erythropoietin receptor

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Differential effects of an erythropoietin receptor gene disruption on primitive and definitive erythropoiesis.

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Jak2 deficiency defines an essential developmental checkpoint in definitive hematopoiesis

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Jak2 is essential for signaling through a variety of cytokine receptors

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Multiple tyrosine residues in the cytosolic domain of the erythropoietin receptor promote activation of STAT5.

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Proteasomes regulate erythropoietin receptor and signal transducer and activator of transcription 5 (STAT5) activation. Possible involvement of the ubiquitinated Cis protein

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Specific recruitment of SH-PTP1 to the erythropoietin receptor causes inactivation of JAK2 and termination of proliferative signals

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Phosphorylation of tyrosine 503 in the erythropoietin receptor (EpR) is essential for binding the P85 subunit of phosphatidylinositol (PI) 3-kinase and for EpR-associated PI 3-kinase activity

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Identification of a second SH2-domain-containing protein closely related to the phosphatidylinositol polyphosphate 5-phosphatase SHIP

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Shc interaction with Src homology 2 domain containing inositol phosphatase (SHIP) in vivo requires the Shc-phosphotyrosine binding domain and two specific phosphotyrosines on SHIP

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

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A dominant negative erythropoietin (EPO) receptor inhibits EPO-dependent growth and blocks F-gp55-dependent transformation

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SHIP is a negative regulator of growth factor receptor-mediated PKB/Akt activation and myeloid cell survival

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p150Ship, a signal transduction molecule with inositol polyphosphate-5-phosphatase activity

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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

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The cytoplasmic region of the erythropoietin receptor contains nonoverlapping positive and negative growth-regulatory domains

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The inositol 5'-phosphatase SHIP binds to immunoreceptor signaling motifs and responds to high affinity IgE receptor aggregation

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The inositol phosphatase SHIP inhibits Akt/PKB activation in B cells

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Targeted disruption of SHIP leads to Steel factor-induced degranulation of mast cells.

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Multiple Cytokines Stimulate the Binding of a Common 145-Kilodalton Protein to Shc at the Grb2 Recognition Site of Shc

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A multifunctional docking site mediates signaling and transformation by the hepatocyte growth factor/scatter factor receptor family

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Tyrosine 1101 of Tie2 is the major site of association of p85 and is required for activation of phosphatidylinositol 3-kinase and Akt

21 January 2018

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Truncated erythropoietin receptor causes dominantly inherited benign human erythrocytosis

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Targeted disruption of SHIP leads to hemopoietic perturbations, lung pathology, and a shortened life span

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STAT5 activation correlates with erythropoietin receptor-mediated erythroid differentiation of an erythroleukemia cell line.

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The prolactin receptor and severely truncated erythropoietin receptors support differentiation of erythroid progenitors

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Erythropoietin induces activation of Stat5 through association with specific tyrosines on the receptor that are not required for a mitogenic response.

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Protein kinase B (c-Akt): a multifunctional mediator of phosphatidylinositol 3-kinase activation.

21 January 2018

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The proto-oncogene product c-Cbl becomes tyrosine phosphorylated by stimulation with GM-CSF or Epo and constitutively binds to the SH3 domain of Grb2/Ash in human hematopoietic cells

21 January 2018

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Ion channels in human erythroblasts. Modulation by erythropoietin

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Erythropoietin modulation of intracellular calcium: a role for tyrosine phosphorylation.

21 January 2018

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Multiple forms of an inositol polyphosphate 5-phosphatase form signaling complexes with Shc and Grb2

21 January 2018

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Molecular cloning and chromosomal localization in human and mouse of the SH2-containing inositol phosphatase, INPP5D (SHIP). Amgen EST Program

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Identification of the erythropoietin receptor domain required for calcium channel activation

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Tyrosine Residues within the Intracellular Domain of the Erythropoietin Receptor Mediate Activation of AP-1 Transcription Factors

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