Role of the vav proto-oncogene product (Vav) in erythropoietin-mediated cell proliferation and phosphatidylinositol 3-kinase activity (Q28238969)

2

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T Otsuka

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Y Ohno

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F Arima

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Y Niho

Journal of Biological Chemistry

6

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language of work or name

English

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publication date

30 May 1997

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published in

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volume

272

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issue

22

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page(s)

14334-40

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cites work

Expression cloning of the murine erythropoietin receptor

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JAK2 associates with the erythropoietin receptor and is tyrosine phosphorylated and activated following stimulation with erythropoietin

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Induction of tyrosine phosphorylation by the erythropoietin receptor correlates with mitogenesis

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In vitro phosphorylation of the erythropoietin receptor and an associated protein, pp130

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Product of vav proto-oncogene defines a new class of tyrosine protein kinase substrates

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Tyrosine phosphorylation of vav proto-oncogene product containing SH2 domain and transcription factor motifs

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Tyrosine phosphorylation of the vav proto-oncogene product in activated B cells

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Interleukin-2 induces tyrosine phosphorylation of the vav proto-oncogene product in human T cells: lack of requirement for the tyrosine kinase lck

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

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Cytokine receptor signalling

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Binding of Vav to Grb2 through dimerization of Src homology 3 domains

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Vav is necessary for prolactin-stimulated proliferation and is translocated into the nucleus of a T-cell line

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Structural basis for the binding of proline-rich peptides to SH3 domains

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SH2 domains recognize specific phosphopeptide sequences

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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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Activation of Ras in vitro and in intact fibroblasts by the Vav guanine nucleotide exchange protein

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Dbl and Vav mediate transformation via mitogen-activated protein kinase pathways that are distinct from those activated by oncogenic Ras

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Structure, regulation and function of phosphoinositide 3-kinases

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cDNA cloning of a Novel 85 kd protein that has SH2 domains and regulates binding of PI3-kinase to the PDGF β-receptor

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Phosphatidylinositol 3-kinase: structure and expression of the 110 kd catalytic subunit

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Activation of Stat5 by interleukin 2 requires a carboxyl-terminal region of the interleukin 2 receptor beta chain but is not essential for the proliferative signal transmission

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Cloning of murine Stat6 and human Stat6, Stat proteins that are tyrosine phosphorylated in responses to IL-4 and IL-3 but are not required for mitogenesis

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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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