Platelet-derived growth factor (PDGF)-dependent association of phospholipase C-gamma with the PDGF receptor signaling complex
about
Heart-specific activation of LTK results in cardiac hypertrophy, cardiomyocyte degeneration and gene reprogramming in transgenic miceGTPase-activating protein and phosphatidylinositol 3-kinase bind to distinct regions of the platelet-derived growth factor receptor beta subunitPhosphatidylinositol 3'-kinase is activated by association with IRS-1 during insulin stimulationTyrosine mutations within the alpha platelet-derived growth factor receptor kinase insert domain abrogate receptor-associated phosphatidylinositol-3 kinase activity without affecting mitogenic or chemotactic signal transductionFunctions of the major tyrosine phosphorylation site of the PDGF receptor beta subunitActivation of Src family kinases by colony stimulating factor-1, and their association with its receptorIdentification of two juxtamembrane autophosphorylation sites in the PDGF beta-receptor; involvement in the interaction with Src family tyrosine kinasesThe 64-kDa protein that associates with the platelet-derived growth factor receptor beta subunit via Tyr-1009 is the SH2-containing phosphotyrosine phosphatase SypA tyrosine-phosphorylated carboxy-terminal peptide of the fibroblast growth factor receptor (Flg) is a binding site for the SH2 domain of phospholipase C-gamma 1The tyrosine phosphorylated carboxyterminus of the EGF receptor is a binding site for GAP and PLC-gammaIn vivo binding properties of SH2 domains from GTPase-activating protein and phosphatidylinositol 3-kinaseA novel signaling molecule, p130, forms stable complexes in vivo with v-Crk and v-Src in a tyrosine phosphorylation-dependent mannerPhosphorylation sites in the PDGF receptor with different specificities for binding GAP and PI3 kinase in vivoOncogenic forms of the neu/HER2 tyrosine kinase are permanently coupled to phospholipase C gammaIdentification of Src, Fyn, and Lyn SH3-binding proteins: implications for a function of SH3 domainsAutophosphorylation of the focal adhesion kinase, pp125FAK, directs SH2-dependent binding of pp60srcAssociation of the tyrosine kinase LCK with phospholipase C-gamma 1 after stimulation of the T cell antigen receptorAdditive effects of PDGF receptor beta signaling pathways in vascular smooth muscle cell developmentPhosphoinositides: tiny lipids with giant impact on cell regulationSolution structure of tensin2 SH2 domain and its phosphotyrosine-independent interaction with DLC-1Direct binding of C-terminal region of p130Cas to SH2 and SH3 domains of Src kinaseThe 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 complexesPhosphorylation sites at the C-terminus of the platelet-derived growth factor receptor bind phospholipase C gamma 1Stoichiometry of interaction between interferon gamma and its receptorThe erbB-2 mitogenic signaling pathway: tyrosine phosphorylation of phospholipase C-gamma and GTPase-activating protein does not correlate with erbB-2 mitogenic potencyOncogenes, Protein Tyrosine Kinases, and Signal Transduction.Binding of the Src SH2 domain to phosphopeptides is determined by residues in both the SH2 domain and the phosphopeptides.Identification and characterization of a high-affinity interaction between v-Crk and tyrosine-phosphorylated paxillin in CT10-transformed fibroblastsThe SH2- and SH3-containing Nck protein transforms mammalian fibroblasts in the absence of elevated phosphotyrosine levels.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.The SH2 and SH3 domains of pp60src direct stable association with tyrosine phosphorylated proteins p130 and p110.Tyrosine phosphorylation of a 120-kilodalton pp60src substrate upon epidermal growth factor and platelet-derived growth factor receptor stimulation and in polyomavirus middle-T-antigen-transformed cells.Interleukin 2- and polyomavirus middle T antigen-induced modification of phosphatidylinositol 3-kinase activity in activated T lymphocytes.A point mutation at tyrosine-809 in the human colony-stimulating factor 1 receptor impairs mitogenesis without abrogating tyrosine kinase activity, association with phosphatidylinositol 3-kinase, or induction of c-fos and junB genes.Thrombin-stimulated immunoprecipitation of phosphatidylinositol 3-kinase from human platelets.Phosphorylation of the PDGF receptor beta subunit creates a tight binding site for phosphatidylinositol 3 kinasePlatelet-derived growth factor (PDGF) A-chain mRNA heterogeneity generated by the use of alternative promoters and alternative polyadenylation sites.A specific combination of substrates is involved in signal transduction by the kit-encoded receptor.Signal transduction by normal isoforms and W mutant variants of the Kit receptor tyrosine kinaseSelective upregulation of platelet-derived growth factor alpha receptors by transforming growth factor beta in scleroderma fibroblasts.
P2860
Q22003772-21C81599-8EDE-407E-90A2-A5AD688D2785Q24292767-34CFE9B7-5C71-4F69-9DCD-CDC630A8DA0AQ24293143-A3DFF6EB-195C-4080-BCFA-6E16AEF3B421Q24303984-3221679D-B149-47C8-9DEC-3EF60C532770Q24307555-688391A8-870C-4EF8-8074-043B16F14194Q24308705-8F9160D7-B39C-48A8-BDAA-612E6C27120FQ24309883-7A2987C5-E70E-46E1-ADB7-234F64048FD7Q24310396-4081FE30-E089-401D-88CD-FE41E4330EFAQ24310428-040EC89F-198C-47E7-94B6-F1F33014635BQ24314441-3C7D1C4E-C599-4865-ADF3-0CE15A3F3966Q24314627-0E75C89D-3DBE-4D9A-B4E4-FAACD7801D1BQ24318312-5EE1587C-0E7D-4584-87DC-0F98C9437326Q24336223-C7B697EE-8553-4628-B672-BCC94CABB070Q24561375-68BA4C4B-57AA-4420-969B-D91B7EB43C22Q24611670-24AE5389-8108-4F37-87D5-4B65C6A66355Q24614033-D02F039C-123F-4744-8423-DE1E0D9F6F38Q24675199-DC85E640-68B1-4BDE-A4DD-7A78DD3BCF41Q24806905-FC282125-3F1F-47EA-BDB7-875E5835CAC3Q27012953-AE68E67D-BF2D-4AF3-A97E-175078364D29Q27670849-47508DB6-5CFC-4D5E-B641-4FAEF8021ABDQ28277700-4CBF9CDE-C8CA-4210-9BE9-655F37495B36Q28367583-EAE1156F-6C13-4A0F-9547-7A50939ED56CQ28645716-0E3638A0-B969-43E5-8AAB-183D5E9169F1Q28646266-62670EF6-2FA5-4142-8446-FE85F0F9DFB2Q28678671-923C299D-FA5A-4F82-964D-898DDBDF8EC1Q30194476-9573ADDC-44EF-4926-A9F7-3C16EC46EB78Q30194700-1E7F2212-63BE-4A3C-8F34-9DF7469218D7Q30194902-9EC4965E-5E08-4354-B38E-5A1370832864Q30195199-AC0F99DD-4833-4192-8058-444EC217E2F9Q30195438-F8BE14A8-E90D-435C-93E3-3D7F98AA8297Q30195658-96547DBE-352A-4989-AF01-1855A5917064Q30441876-0049FD04-EB4A-4E6E-9470-ADC3B32AD7B8Q30450318-DFDE2AEC-3957-4080-8D9B-95E5E487B24EQ33769954-B9AA889E-3EFC-441E-8085-4137E804E6F8Q33918164-B66B9FEE-2CF7-4EBF-BFB8-619BBA2610CBQ33922224-17DD5B60-5C49-4645-ABD1-7262E36C08CCQ34245231-EB106E90-4A09-4656-AB84-188F21D9C25EQ35922486-81465607-6DC1-443B-9EE8-4C0C26E713FEQ35929162-740DDF6A-4518-4665-923E-4A5B7126EEB9Q36231258-2223AB6B-46EA-441B-B09E-05133CFB118F
P2860
Platelet-derived growth factor (PDGF)-dependent association of phospholipase C-gamma with the PDGF receptor signaling complex
description
1990 nî lūn-bûn
@nan
1990 թուականի Մայիսին հրատարակուած գիտական յօդուած
@hyw
1990 թվականի մայիսին հրատարակված գիտական հոդված
@hy
1990年の論文
@ja
1990年論文
@yue
1990年論文
@zh-hant
1990年論文
@zh-hk
1990年論文
@zh-mo
1990年論文
@zh-tw
1990年论文
@wuu
name
Platelet-derived growth factor ...... DGF receptor signaling complex
@ast
Platelet-derived growth factor ...... DGF receptor signaling complex
@en
type
label
Platelet-derived growth factor ...... DGF receptor signaling complex
@ast
Platelet-derived growth factor ...... DGF receptor signaling complex
@en
prefLabel
Platelet-derived growth factor ...... DGF receptor signaling complex
@ast
Platelet-derived growth factor ...... DGF receptor signaling complex
@en
P2093
P2860
P356
P1476
Platelet-derived growth factor ...... DGF receptor signaling complex
@en
P2093
D K Morrison
D R Kaplan
L T Williams
P2860
P304
P356
10.1128/MCB.10.5.2359
P407
P577
1990-05-01T00:00:00Z