The Src homology 2 domain containing inositol 5-phosphatase SHIP2 is recruited to the epidermal growth factor (EGF) receptor and dephosphorylates phosphatidylinositol 3,4,5-trisphosphate in EGF-stimulated COS-7 cells

The Src homology 2 domain containing inositol 5-phosphatase SHIP2 is recruited to the epidermal growth factor (EGF) receptor and dephosphorylates phosphatidylinositol 3,4,5-trisphosphate in EGF-stimulated COS-7 cells

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http://www.wikidata.org/entity/Q28188461

Q28188461

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Evidence that the tandem-pleckstrin-homology-domain-containing protein TAPP1 interacts with Ptd(3,4)P2 and the multi-PDZ-domain-containing protein MUPP1 in vivo The SH2-containing inositol polyphosphate 5-phosphatase, SHIP-2, binds filamin and regulates submembraneous actin SHIP-2 inositol phosphatase is inducibly expressed in human monocytes and serves to regulate Fcgamma receptor-mediated signaling Angiotensin II down-regulates nephrin-Akt signaling and induces podocyte injury: roleof c-Abl.SHIP2 multiple functions: a balance between a negative control of PtdIns(3,4,5)P₃ level, a positive control of PtdIns(3,4)P₂ production, and intrinsic docking properties.Novel phosphotyrosine targets of FGFR2IIIb signaling.Signal propagation from membrane messengers to nuclear effectors revealed by reporters of phosphoinositide dynamics and Akt activity 5'-Inositol phosphatase SHIP2 recruits Mena to stabilize invadopodia for cancer cell invasion.In-depth qualitative and quantitative profiling of tyrosine phosphorylation using a combination of phosphopeptide immunoaffinity purification and stable isotope dimethyl labeling SHIP2, a factor associated with diet-induced obesity and insulin sensitivity, attenuates FGF signaling in vivo.The host phosphoinositide 5-phosphatase SHIP2 regulates dissemination of vaccinia virus PTP1B-dependent regulation of receptor tyrosine kinase signaling by the actin-binding protein Mena.SHIP2 regulates epithelial cell polarity through its lipid product, which binds to Dlg1, a pathway subverted by hepatitis C virus core protein SHIP2 (SH2 domain-containing inositol phosphatase 2) SH2 domain negatively controls SHIP2 monoubiquitination in response to epidermal growth factor.SHIP2 and its involvement in various diseases.Qualitatively different T cell phenotypic responses to IL-2 versus IL-15 are unified by identical dependences on receptor signal strength and duration.Coupling an EML4-ALK-centric interactome with RNA interference identifies sensitizers to ALK inhibitors.SHIP2: Structure, Function and Inhibition.PI3K/SHIP2/PTEN pathway in cell polarity and hepatitis C virus pathogenesis.How does SHIP1/2 balance PtdIns(3,4)P2 and does it signal independently of its phosphatase activity?Evidence of SHIP2 Ser132 phosphorylation, its nuclear localization and stability.Inositol phospholipids regulate the guanine-nucleotide-exchange factor Tiam1 by facilitating its binding to the plasma membrane and regulating GDP/GTP exchange on Rac1 SH2-containing inositol 5-phosphatases 1 and 2 in blood platelets: their interactions and roles in the control of phosphatidylinositol 3,4,5-trisphosphate levels.PtdIns5P activates the host cell PI3-kinase/Akt pathway during Shigella flexneri infection.PI(3;4;5)P3 is dephosphorylated to PI(3;4)P2 by INPP5[2] at the plasma membrane Specific Eph receptor-cytoplasmic effector signaling mediated by SAM-SAM domain interactions.

P2860

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P2860

The Src homology 2 domain containing inositol 5-phosphatase SHIP2 is recruited to the epidermal growth factor (EGF) receptor and dephosphorylates phosphatidylinositol 3,4,5-trisphosphate in EGF-stimulated COS-7 cells

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http://www.wikidata.org/entity/Q28188461

description

2001 թուականի Յուլիսին հրատարակուած գիտական յօդուած

@hyw

2001 թվականի հուլիսին հրատարակված գիտական հոդված

@hy

article publié dans la revue scientifique Journal of Biological Chemistry

@fr

artículu científicu espublizáu en 2001

@ast

im Mai 2001 veröffentlichter wissenschaftlicher Artikel

@de

scientific article (publication date: 27 July 2001)

@en

vedecký článok (publikovaný 2001/07/27)

@sk

vědecký článek publikovaný v roce 2001

@cs

wetenschappelijk artikel (gepubliceerd op 2001/07/27)

@nl

наукова стаття, опублікована в липні 2001

@uk