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
about
Epidermal growth factor receptor and the adaptor protein p52Shc are specific substrates of T-cell protein tyrosine phosphatase.Protein kinase C-delta is a negative regulator of antigen-induced mast cell degranulationInactivating mutations in an SH2 domain-encoding gene in X-linked lymphoproliferative syndromep135 src homology 2 domain-containing inositol 5'-phosphatase (SHIPbeta ) isoform can substitute for p145 SHIP in fcgamma RIIB1-mediated inhibitory signaling in B cellsThe SH2 inositol 5-phosphatase Ship1 is recruited in an SH2-dependent manner to the erythropoietin receptorSignaling via Shc family adapter proteinsA spectrum of mutations in SH2D1A that causes X-linked lymphoproliferative disease and other Epstein-Barr virus-associated illnessesTyrosine phosphorylation and relocation of SHIP are integrin-mediated in thrombin-stimulated human blood plateletsPTP-PEST, a scaffold protein tyrosine phosphatase, negatively regulates lymphocyte activation by targeting a unique set of substratesAbsence of the lipid phosphatase SHIP2 confers resistance to dietary obesitySHIP1, an SH2 domain containing polyinositol-5-phosphatase, regulates migration through two critical tyrosine residues and forms a novel signaling complex with DOK1 and CRKLThe src homology domain 2-containing inositol phosphatase SHIP forms a ternary complex with Shc and Grb2 in antigen receptor-stimulated B lymphocytesIdentification and characterization of a dimerization domain in CED-6, an adapter protein involved in engulfment of apoptotic cells.Essential role for the C-terminal noncatalytic region of SHIP in FcgammaRIIB1-mediated inhibitory signalingDesign and use of an inducibly activated human immunodeficiency virus type 1 Nef to study immune modulation.Role of Shc in T-cell development and function.A key role for the phosphorylation of Ser440 by the cyclic AMP-dependent protein kinase in regulating the activity of the Src homology 2 domain-containing Inositol 5'-phosphatase (SHIP1).Regulation of the Src homology 2 domain-containing inositol 5'-phosphatase (SHIP1) by the cyclic AMP-dependent protein kinaseEvidence for a requirement for both phospholipid and phosphotyrosine binding via the Shc phosphotyrosine-binding domain in vivoPhosphoinositide lipid phosphatase SHIP1 and PTEN coordinate to regulate cell migration and adhesion.Cooperation and selectivity of the two Grb2 binding sites of p52Shc in T-cell antigen receptor signaling to Ras family GTPases and Myc-dependent survival.Negative signaling in health and disease.Early events in M-CSF receptor signaling.ERK phosphorylates p66shcA on Ser36 and subsequently regulates p27kip1 expression via the Akt-FOXO3a pathway: implication of p27kip1 in cell response to oxidative stress.IL-4 signaling is regulated through the recruitment of phosphatases, kinases, and SOCS proteins to the receptor complex.Inositol phospholipid signaling and the biology of natural killer cells.The inositol 5-phosphatase SHIP-1 and adaptors Dok-1 and 2 play central roles in CD4-mediated inhibitory signaling.DSHP: a "power bar" for sustained immune responses?A regulatory role for Src homology 2 domain-containing inositol 5'-phosphatase (SHIP) in phagocytosis mediated by Fc gamma receptors and complement receptor 3 (alpha(M)beta(2); CD11b/CD18)Recruitment and phosphorylation of SH2-containing inositol phosphatase and Shc to the B-cell Fc gamma immunoreceptor tyrosine-based inhibition motif peptide motif.A role for SHIP in stem cell biology and transplantation.Inhibitor and activator: dual functions for SHIP in immunity and cancer.Molecular control of PtdIns(3,4,5)P3 signaling in neutrophils.SHIP-mediated inhibition of K562 erythroid differentiation requires an intact catalytic domain and Shc binding site.FcγRIIB-Independent Mechanisms Controlling Membrane Localization of the Inhibitory Phosphatase SHIP in Human B Cells.Regulation of immune cell signaling by SHIP1: A phosphatase, scaffold protein, and potential therapeutic target.An SH2 domain-containing 5' inositolphosphatase inhibits insulin-induced GLUT4 translocation and growth factor-induced actin filament rearrangement.Gab adapter proteins as therapeutic targets for hematologic disease.Regulation of the Src homology 2-containing inositol 5-phosphatase SHIP1 in HIP1/PDGFbeta R-transformed cells.Positive regulation of interleukin-4-mediated proliferation by the SH2-containing inositol-5'-phosphatase.
P2860
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P2860
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
description
1997 թուականի Ապրիլին հրատարակուած գիտական յօդուած
@hyw
1997 թվականի ապրիլին հրատարակված գիտական հոդված
@hy
article publié dans la revue scientifique Journal of Biological Chemistry
@fr
artículu científicu espublizáu en 1997
@ast
im April 1997 veröffentlichter wissenschaftlicher Artikel
@de
scientific journal article
@en
vedecký článok (publikovaný 1997/04/18)
@sk
vědecký článek publikovaný v roce 1997
@cs
wetenschappelijk artikel (gepubliceerd op 1997/04/18)
@nl
наукова стаття, опублікована у квітні 1997
@uk
name
Shc interaction with Src homol ...... cific phosphotyrosines on SHIP
@ast
Shc interaction with Src homol ...... cific phosphotyrosines on SHIP
@en
Shc interaction with Src homol ...... cific phosphotyrosines on SHIP
@nl
type
label
Shc interaction with Src homol ...... cific phosphotyrosines on SHIP
@ast
Shc interaction with Src homol ...... cific phosphotyrosines on SHIP
@en
Shc interaction with Src homol ...... cific phosphotyrosines on SHIP
@nl
prefLabel
Shc interaction with Src homol ...... cific phosphotyrosines on SHIP
@ast
Shc interaction with Src homol ...... cific phosphotyrosines on SHIP
@en
Shc interaction with Src homol ...... cific phosphotyrosines on SHIP
@nl
P2093
P2860
P356
P1476
Shc interaction with Src homol ...... cific phosphotyrosines on SHIP
@en
P2093
G. Krystal
J. E. Damen
K. S. Ravichandran
S. F. Walk
T. D. Lamkin
P2860
P304
10396–10401
P356
10.1074/JBC.272.16.10396
P407
P577
1997-04-18T00:00:00Z