Evidence for a requirement for both phospholipid and phosphotyrosine binding via the Shc phosphotyrosine-binding domain in vivo - Wikidata - wikimedia - TriplyDB

Evidence for a requirement for both phospholipid and phosphotyrosine binding via the Shc phosphotyrosine-binding domain in vivo

Evidence for a requirement for both phospholipid and phosphotyrosine binding via the Shc phosphotyrosine-binding domain in vivo

http://www.wikidata.org/entity/Q30452658

about

Disabled-2 exhibits the properties of a cargo-selective endocytic clathrin adaptor Structural basis of SNT PTB domain interactions with distinct neurotrophic receptors Crystal structures of the Dab homology domains of mouse disabled 1 and 2 Integrin 3 Phosphorylation Dictates Its Complex with the Shc Phosphotyrosine-binding (PTB) Domain Non-redundant signal transduction of interleukin-6-type cytokines. The adapter protein Shc is specifically recruited to rhe oncostatin M receptor Regulation of Cbl molecular interactions by the co-receptor molecule CD43 in human T cells Plasma membrane phospholipid scramblase 1 promotes EGF-dependent activation of c-Src through the epidermal growth factor receptor Signaling via Shc family adapter proteins Interaction domains: from simple binding events to complex cellular behavior Roles of Lck, Syk and ZAP-70 tyrosine kinases in TCR-mediated phosphorylation of the adapter protein Shc The ShcA phosphotyrosine docking protein sensitizes cardiovascular signaling in the mouse embryo PDZ domain proteins: plug and play!Identification and characterization of a dimerization domain in CED-6, an adapter protein involved in engulfment of apoptotic cells.Design 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.Sck is expressed in endothelial cells and participates in vascular endothelial growth factor-induced signaling.Interaction with Shc prevents aberrant Erk activation in the absence of extracellular stimuli.Characterization of four mammalian numb protein isoforms. Identification of cytoplasmic and membrane-associated variants of the phosphotyrosine binding domain.Phosphatidylinositol 4,5-bisphosphate activates Slo3 currents and its hydrolysis underlies the epidermal growth factor-induced current inhibition The disabled 1 phosphotyrosine-binding domain binds to the internalization signals of transmembrane glycoproteins and to phospholipids The pleckstrin homology (PH) domain-interacting protein couples the insulin receptor substrate 1 PH domain to insulin signaling pathways leading to mitogenesis and GLUT4 translocation PTB or not PTB -- that is the question.SH2 and PTB domains in tyrosine kinase signaling.Redirecting tyrosine kinase signaling to an apoptotic caspase pathway through chimeric adaptor proteins.Genome-wide functional annotation of dual-specificity protein- and lipid-binding modules that regulate protein interactions.Phospholipid binding to the FAK catalytic domain impacts function.The Rab GTPase-activating protein TBC1D4/AS160 contains an atypical phosphotyrosine-binding domain that interacts with plasma membrane phospholipids to facilitate GLUT4 trafficking in adipocytes.NUMB inhibition of NOTCH signalling as a therapeutic target in prostate cancer.Positive and negative regulation of antigen receptor signaling by the Shc family of protein adapters.Teaching an old dogma new tricks: twenty years of Shc adaptor signalling.Phosphotyrosine protein of molecular mass 30 kDa binds specifically to the positively charged region of the pleckstrin N-terminal pleckstrin homology domain.Phospho-Tyrosine(s) vs. Phosphatidylinositol Binding in Shc Mediated Integrin Signaling.A novel PTB-PDZ domain interaction mediates isoform-specific ubiquitylation of mammalian Numb.Pleckstrin homology and phosphotyrosine-binding domain-dependent membrane association and tyrosine phosphorylation of Dok-4, an inhibitory adapter molecule expressed in epithelial cells.NOS1AP Functionally Associates with YAP To Regulate Hippo Signaling.PTB domain of insulin receptor substrate-1 binds inositol compounds.Insulin receptor substrate-1 pleckstrin homology and phosphotyrosine-binding domains are both involved in plasma membrane targeting.The ShcD phosphotyrosine adaptor subverts canonical EGF receptor trafficking.A phosphoinositide-binding sequence is shared by PH domain target molecules--a model for the binding of PH domains to proteins.Phosphatidylinositol 3-kinase is required for insulin-stimulated tyrosine phosphorylation of Shc in 3T3-L1 adipocytes.

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P2860

Evidence for a requirement for both phospholipid and phosphotyrosine binding via the Shc phosphotyrosine-binding domain in vivo

http://www.wikidata.org/entity/Q30452658

description

1997 nî lūn-bûn

@nan

1997 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած

@hyw

1997 թվականի սեպտեմբերին հրատարակված գիտական հոդված

@hy

1997年の論文

@ja

1997年論文

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1997年論文

@zh-hant

1997年論文

@zh-hk

1997年論文

@zh-mo

1997年論文

@zh-tw

1997年论文

@wuu

name

Evidence for a requirement for ...... yrosine-binding domain in vivo

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Evidence for a requirement for ...... yrosine-binding domain in vivo

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type

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Evidence for a requirement for ...... yrosine-binding domain in vivo

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Evidence for a requirement for ...... yrosine-binding domain in vivo

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prefLabel

Evidence for a requirement for ...... yrosine-binding domain in vivo

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Evidence for a requirement for ...... yrosine-binding domain in vivo

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P1433

Molecular and Cellular Biology

P1476

Evidence for a requirement for ...... yrosine-binding domain in vivo

@en

P2093

J C Pratt

http://www.w3.org/2001/XMLSchema#string

J E Harlan

http://www.w3.org/2001/XMLSchema#string

K S Ravichandran

http://www.w3.org/2001/XMLSchema#string

M M Zhou

http://www.w3.org/2001/XMLSchema#string

S F Walk

http://www.w3.org/2001/XMLSchema#string

S J Burakoff

http://www.w3.org/2001/XMLSchema#string

S W Fesik

http://www.w3.org/2001/XMLSchema#string

P2860

The phosphotyrosine interaction domain of Shc binds an LXNPXY motif on the epidermal growth factor receptor

The Shc adaptor protein is highly phosphorylated at conserved, twin tyrosine residues (Y239/240) that mediate protein-protein interactions

The SH2/SH3 domain-containing protein GRB2 interacts with tyrosine-phosphorylated IRS1 and Shc: implications for insulin control of ras signalling

A novel transforming protein (SHC) with an SH2 domain is implicated in mitogenic signal transduction

Requirement of phospholipase C gamma, the tyrosine phosphatase Syp and the adaptor proteins Shc and Nck for PDGF-induced DNA synthesis: evidence for the existence of Ras-dependent and Ras-independent pathways

Signal transduction by the high-affinity GM-CSF receptor: two distinct cytoplasmic regions of the common beta subunit responsible for different signaling

The 145-kDa protein induced to associate with Shc by multiple cytokines is an inositol tetraphosphate and phosphatidylinositol 3,4,5-triphosphate 5-phosphatase

Different interleukin 2 receptor beta-chain tyrosines couple to at least two signaling pathways and synergistically mediate interleukin 2-induced proliferation

Tyrosine phosphorylation sites at amino acids 239 and 240 of Shc are involved in epidermal growth factor-induced mitogenic signaling that is distinct from Ras/mitogen-activated protein kinase activation

Solution structure of the Shc SH2 domain complexed with a tyrosine-phosphorylated peptide from the T-cell receptor

P304

5540-5549

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scholarly article

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10.1128/MCB.17.9.5540

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9

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17

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1997-09-01T00:00:00Z

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13949809

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P698

9271429

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P932

232402

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