Shc associates with the IL-3 receptor β subunit, SHIP and Gab2 following IL-3 stimulation (Q28137857)

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scientific article (publication date: March 2000)

Shc associates with the IL-3 receptor beta subunit, SHIP and Gab2 following IL-3 stimulation. Contribution of Shc PTB and SH2 domains

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English	Shc associates with the IL-3 receptor β subunit, SHIP and Gab2 following IL-3 stimulation	scientific article (publication date: March 2000)	Shc associates with the IL-3 receptor beta subunit, SHIP and Gab2 following IL-3 stimulation. Contribution of Shc PTB and SH2 domains

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scholarly article

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Shc associates with the IL-3 receptor beta subunit, SHIP and Gab2 following IL-3 stimulation. Contribution of Shc PTB and SH2 domains (English)

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

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most precise value

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2

object named as

Melanie J. Welham

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Heather K. Bone

1

object named as

Heather Bone

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language of work or name

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publication date

March 2000

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number of pages

12

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Cellular Signalling

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12

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3

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183-194

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The panspecific hemopoietin of activated T lymphocytes (interleukin-3).

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Cytokines: coordinators of immune and inflammatory responses

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Cytokine receptors and signal transduction

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Expression cloning of the human IL-3 receptor cDNA reveals a shared beta subunit for the human IL-3 and GM-CSF receptors

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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

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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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Protein modules and signalling networks

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

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Evidence for a physical association between the Shc-PTB domain and the beta c chain of the granulocyte-macrophage colony-stimulating factor receptor

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

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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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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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Interleukin-3 Induces Association of the Protein-tyrosine Phosphatase SHP2 and Phosphatidylinositol 3-Kinase with a 100-kDa Tyrosine-phosphorylated Protein in Hemopoietic Cells

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Comparison of the specificity of bacterially expressed cytoplasmic protein-tyrosine phosphatases SHP and SH-PTP2 towards synthetic phosphopeptide substrates

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10.1016/S0898-6568(99)00088-1

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