The C-terminal SH2 domain of p85 accounts for the high affinity and specificity of the binding of phosphatidylinositol 3-kinase to phosphorylated platelet-derived growth factor beta receptor.
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Fyn associates with Cbl and phosphorylates tyrosine 731 in Cbl, a binding site for phosphatidylinositol 3-kinaseA phosphatidylinositol 3-kinase/Akt pathway, activated by tumor necrosis factor or interleukin-1, inhibits apoptosis but does not activate NFkappaB in human endothelial cellsPhosphatidylinositol 3'-kinase is activated by association with IRS-1 during insulin stimulationThe SH3 domain of p56lck is involved in binding to phosphatidylinositol 3'-kinase from T lymphocytesThe 64-kDa protein that associates with the platelet-derived growth factor receptor beta subunit via Tyr-1009 is the SH2-containing phosphotyrosine phosphatase SypAlpha 2-chimerin, an SH2-containing GTPase-activating protein for the ras-related protein p21rac derived by alternate splicing of the human n-chimerin gene, is selectively expressed in brain regions and testesIn vivo binding properties of SH2 domains from GTPase-activating protein and phosphatidylinositol 3-kinaseStructure of a specific peptide complex of the carboxy-terminal SH2 domain from the p85 alpha subunit of phosphatidylinositol 3-kinaseSH2 domains exhibit high-affinity binding to tyrosine-phosphorylated peptides yet also exhibit rapid dissociation and exchangeThe SH2/SH3 domain-containing protein Nck is recognized by certain anti-phospholipase C-gamma 1 monoclonal antibodies, and its phosphorylation on tyrosine is stimulated by platelet-derived growth factor and epidermal growth factor treatmentAssociation of hematopoietic cell phosphatase with c-Kit after stimulation with c-Kit ligandDirect association of p110 beta phosphatidylinositol 3-kinase with p85 is mediated by an N-terminal fragment of p110 betaCloning of a novel, ubiquitously expressed human phosphatidylinositol 3-kinase and identification of its binding site on p85Binding of NCK to SOS and activation of ras-dependent gene expressionThe catalytic subunit of phosphatidylinositol 3-kinase is a substrate for the activated platelet-derived growth factor receptor, but not for middle-T antigen-pp60c-src complexesp150TSP, a conserved nuclear phosphoprotein that contains multiple tetratricopeptide repeats and binds specifically to SH2 domainsInteraction of p72syk with the gamma and beta subunits of the high-affinity receptor for immunoglobulin E, Fc epsilon RIIdentification and sequence analysis of cDNAs encoding a 110-kilodalton actin filament-associated pp60src substrate.Binding of the Src SH2 domain to phosphopeptides is determined by residues in both the SH2 domain and the phosphopeptides.Phosphatidylinositol 3-kinase activity is important for progesterone-induced Xenopus oocyte maturation.A region of the 85-kilodalton (kDa) subunit of phosphatidylinositol 3-kinase binds the 110-kDa catalytic subunit in vivo.The v-Src SH3 domain binds phosphatidylinositol 3'-kinase.Structure of 85 kDa subunit of human phosphatidylinositol 3-kinase analyzed by using monoclonal antibodies.The SH2- and SH3-containing Nck protein transforms mammalian fibroblasts in the absence of elevated phosphotyrosine levels.Activation of c-Src in cells bearing v-Crk and its suppression by CskSH3--an abundant protein domain in search of a function.Using a phage display library to identify basic residues in A-Raf required to mediate binding to the Src homology 2 domains of the p85 subunit of phosphatidylinositol 3'-kinase.Five isoforms of the phosphatidylinositol 3-kinase regulatory subunit exhibit different associations with receptor tyrosine kinases and their tyrosine phosphorylations.Phospholipase C-gamma 1 can induce DNA synthesis by a mechanism independent of its lipase activity.The phosphatidylinositol 3-kinase alpha is required for DNA synthesis induced by some, but not all, growth factors.Fc receptor stimulation of phosphatidylinositol 3-kinase in natural killer cells is associated with protein kinase C-independent granule release and cell-mediated cytotoxicity.Role of the PI3K regulatory subunit in the control of actin organization and cell migration.Tyrosines 1021 and 1009 are phosphorylation sites in the carboxy terminus of the platelet-derived growth factor receptor beta subunit and are required for binding of phospholipase C gamma and a 64-kilodalton protein, respectivelyMicroinjection of the SH2 domain of the 85-kilodalton subunit of phosphatidylinositol 3-kinase inhibits insulin-induced DNA synthesis and c-fos expressionInteractions between SH2 domains and tyrosine-phosphorylated platelet-derived growth factor beta-receptor sequences: analysis of kinetic parameters by a novel biosensor-based approachThe interaction of small domains between the subunits of phosphatidylinositol 3-kinase determines enzyme activity.Cpk is a novel class of Drosophila PtdIns 3-kinase containing a C2 domain.Modification of the 85-kilodalton subunit of phosphatidylinositol-3 kinase in platelet-derived growth factor-stimulated cellsSignal transduction at point-blank range: analysis of a spatial coupling mechanism for pathway crosstalkShc proteins are phosphorylated and regulated by the v-Src and v-Fps protein-tyrosine kinases
P2860
Q22008672-5330723A-3DC6-400D-9DD7-C59530EB3C17Q22253428-35166738-207E-4FAA-B00C-6EE58F47C126Q24293143-5E9E2B2A-FCBB-4F56-9BB3-9722B2E77792Q24304668-5C7A27B8-3F40-49B4-82B5-1F6B6E55BB92Q24310396-42F0DE71-4E0D-41D2-9F4C-3413DDCD972CQ24310421-FDF6867B-FD1C-4941-8755-4CC8D58B44E9Q24314627-1682FD21-25D4-46D9-B3F1-127A5DA5E802Q24324349-8AD3796F-F803-47E0-A379-F915E96CF2C4Q24337707-D0026898-D332-47B9-9077-061A1947C0F4Q24600605-891CC259-6856-489A-A52A-7FCACB155851Q24604791-C70C8257-7ED1-41A6-85D5-7B88BB10D095Q24613360-3F76FA6F-CC3A-4B44-8672-A656DD7BA545Q24629213-2672F7F0-E00B-47FC-9CE2-58AA937B027FQ24652890-41FC66C0-F929-4323-8911-9D20FA2AD5EDQ28367583-64FC752D-2DF8-41D2-B9CA-3F559A727E15Q28504919-9087D52B-29AB-42A5-87ED-292F42AFFE91Q28611006-B7C9BF28-A6E8-4115-A68D-80FD3B295CB7Q30194681-F39ED80D-9A88-491F-899D-FDE31163499CQ30194700-4146FC3C-0336-4965-9BEB-C11E99DB598DQ30194718-9CDC76F4-6191-477C-8BFD-E4A95E7F8202Q30194817-C29EEEA3-D926-4C56-A876-188174DD7D65Q30194840-20835F7D-E01F-42F2-8D04-68273926273AQ30195126-A567FD66-2517-401D-841B-305A804AF226Q30195199-CEF1690F-D6AF-4DBF-BBEF-D0F5877D1DC9Q30195267-21630A79-702A-48C7-B43C-43786464E8D9Q30195311-1AF06DD7-BD64-4514-B832-15087F2FEEF5Q30914495-51E0A7A0-6F26-46E0-B1D1-6FCA01D6E243Q31924344-ACE00EDC-5553-4076-A0C2-59E5113EEFBDQ35582318-BE2A0D92-E1C1-49AF-A5F2-4E9DA2C3DB9DQ35769059-BEAD879F-2F04-4C9F-99DE-30A21F588274Q36363884-0DDFEA98-546F-4BC1-980B-6D1D19D0E1B2Q36366957-FE65AA01-F710-4EE1-AC45-B391332EC3E6Q36658598-D689460D-6F08-4BE7-894C-0E0067C0D89DQ36669823-9F61FF8D-71DD-4032-9A9D-8058EA2BAFE7Q36686508-5B18761E-1C8D-4F1D-ABE3-5C787E47627DQ36745695-B766D87A-BC83-4D85-AEAB-FAA7FA020B71Q36802890-499B860F-072A-416E-8810-0DECC7889D02Q36821017-12C87276-6379-43FA-A8D1-55CF2A0578D7Q36838819-33CE79ED-94D9-42B6-8487-D8A85BAEBA3EQ37212669-AF901994-DA1C-466E-A0CC-0F95FABF16E4
P2860
The C-terminal SH2 domain of p85 accounts for the high affinity and specificity of the binding of phosphatidylinositol 3-kinase to phosphorylated platelet-derived growth factor beta receptor.
description
1992 nî lūn-bûn
@nan
1992 թուականի Ապրիլին հրատարակուած գիտական յօդուած
@hyw
1992 թվականի ապրիլին հրատարակված գիտական հոդված
@hy
1992年の論文
@ja
1992年論文
@yue
1992年論文
@zh-hant
1992年論文
@zh-hk
1992年論文
@zh-mo
1992年論文
@zh-tw
1992年论文
@wuu
name
The C-terminal SH2 domain of p ...... d growth factor beta receptor.
@ast
The C-terminal SH2 domain of p ...... d growth factor beta receptor.
@en
type
label
The C-terminal SH2 domain of p ...... d growth factor beta receptor.
@ast
The C-terminal SH2 domain of p ...... d growth factor beta receptor.
@en
prefLabel
The C-terminal SH2 domain of p ...... d growth factor beta receptor.
@ast
The C-terminal SH2 domain of p ...... d growth factor beta receptor.
@en
P2093
P2860
P356
P1476
The C-terminal SH2 domain of p ...... d growth factor beta receptor.
@en
P2093
Escobedo JA
Williams LT
P2860
P304
P356
10.1128/MCB.12.4.1451
P407
P577
1992-04-01T00:00:00Z