A yeast two-hybrid study of human p97/Gab2 interactions with its SH2 domain-containing binding partners (Q28186960)

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M Arnaud

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F Gesbert

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J Camonis

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J Bertoglio

Characterization of two SHP-2-associated binding proteins and potential substrates in hematopoietic cells.

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language of work or name

English

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publication date

27 April 2001

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published in

FEBS Letters

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volume

495

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page(s)

148-53

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issue

3

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cites work

1 reference

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A new tyrosine-phosphorylated 97-kDa adaptor protein mediates interleukin-2-induced association of SHP-2 with p85-phosphatidylinositol 3-kinase in human T lymphocytes

21 January 2018

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Cloning of p97/Gab2, the major SHP2-binding protein in hematopoietic cells, reveals a novel pathway for cytokine-induced gene activation

21 January 2018

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Gab2, a new pleckstrin homology domain-containing adapter protein, acts to uncouple signaling from ERK kinase to Elk-1

21 January 2018

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Interaction of SH2-containing protein tyrosine phosphatase 2 with the insulin receptor and the insulin-like growth factor-I receptor: studies of the domains involved using the yeast two-hybrid system

21 January 2018

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Determination of Gab1 (Grb2-associated binder-1) interaction with insulin receptor-signaling molecules

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Yeast two-hybrid in vivo association of the Src kinase Lyn with the proto-oncogene product Cbl but not with the p85 subunit of PI 3-kinase

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

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Cloning of human Stat5B. Reconstitution of interleukin-2-induced Stat5A and Stat5B DNA binding activity in COS-7 cells

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SH2 domains recognize specific phosphopeptide sequences

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Modular peptide recognition domains in eukaryotic signaling

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Recognition and specificity in protein tyrosine kinase-mediated signalling

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Shc proteins are phosphorylated and regulated by the v-Src and v-Fps protein-tyrosine kinases

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New role for Shc in activation of the phosphatidylinositol 3-kinase/Akt pathway

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

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Crystal structure of the tyrosine phosphatase SHP-2

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Recruitment of the protein-tyrosine phosphatase SHP-2 to the C-terminal tyrosine of the prolactin receptor and to the adaptor protein Gab2.

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CrkL mediates Ras-dependent activation of the Raf/ERK pathway through the guanine nucleotide exchange factor C3G in hematopoietic cells stimulated with erythropoietin or interleukin-3.

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Signaling of hepatocyte growth factor/scatter factor (HGF) to the small GTPase Rap1 via the large docking protein Gab1 and the adapter protein CRKL

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Interleukin-2 stimulation induces tyrosine phosphorylation of p120-Cbl and CrkL and formation of multimolecular signaling complexes in T lymphocytes and natural killer cells

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Characterization of a novel tyrosine phosphorylated 100-kDa protein that binds to SHP-2 and phosphatidylinositol 3'-kinase in myeloid cells

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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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A conditionally expressed third partner stabilizes or prevents the formation of a transcriptional activator in a three-hybrid system

7 January 2021

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Plant lipoxygenase 2 is a translation initiation factor-4E-binding protein

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Recent advances in the understanding of interleukin-2 signal transduction

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Cutting edge: gab2 mediates an inhibitory phosphatidylinositol 3'-kinase pathway in T cell antigen receptor signaling

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7 January 2021

Identifiers

DOI

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Consolidated OpenCitations Corpus – April 2017

5008347

5008347

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Consolidated OpenCitations Corpus – April 2017

Consolidated OpenCitations Corpus – April 2017

1 reference