Linker insertion-deletion mutagenesis of the v-src gene: isolation of host- and temperature-dependent mutants
about
Multiple SH2-mediated interactions in v-src-transformed cells.The SH3 domain directs acto-myosin-dependent targeting of v-Src to focal adhesions via phosphatidylinositol 3-kinase.Distinctive regulation of v-Src-associated phosphatidylinositol 3-kinase during PC12 cell differentiation.The role of the Src homology domains in morphological transformation by v-srcDisease specificity of kinase domains: the src-encoded catalytic domain converts erbB into a sarcoma oncogenePhysical and functional interactions between SH2 and SH3 domains of the Src family protein tyrosine kinase p59fynMutations in v-Src SH3 and catalytic domains that jointly confer temperature-sensitive transformation with minimal temperature-dependent changes in cellular tyrosine phosphorylationAberrant protein phosphorylation at tyrosine is responsible for the growth-inhibitory action of pp60v-src expressed in the yeast Saccharomyces cerevisiae.Binding of the Src SH2 domain to phosphopeptides is determined by residues in both the SH2 domain and the phosphopeptides.The v-Src SH3 domain binds phosphatidylinositol 3'-kinase.En bloc substitution of the Src homology region 2 domain activates the transforming potential of the c-Abl protein tyrosine kinase.Host range mutants of v-src: alterations in kinase activity and substrate interactionsEffects of SH2 and SH3 deletions on the functional activities of wild-type and transforming variants of c-Src.Identification and characterization of a novel cytoskeleton-associated pp60src substrate.The SH2 and SH3 domains of pp60src direct stable association with tyrosine phosphorylated proteins p130 and p110.Identification of domains of the v-crk oncogene product sufficient for association with phosphotyrosine-containing proteins.Deletions in the SH2 domain of p60v-src prevent association with the detergent-insoluble cellular matrixMutations in src homology regions 2 and 3 of activated chicken c-src that result in preferential transformation of mouse or chicken cells.Site-directed mutagenesis of the SH2- and SH3-coding domains of c-src produces varied phenotypes, including oncogenic activation of p60c-src.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.Transformation by pp60src or stimulation of cells with epidermal growth factor induces the stable association of tyrosine-phosphorylated cellular proteins with GTPase-activating protein.Stable association of activated pp60src with two tyrosine-phosphorylated cellular proteinsSrc homology region 2 domains direct protein-protein interactions in signal transduction.Temperature-sensitive transformation by an Abelson virus mutant encoding an altered SH2 domain.Src SH2 arginine 175 is required for cell motility: specific focal adhesion kinase targeting and focal adhesion assembly functionRas-independent transformation by v-SrcEngineering unnatural nucleotide specificity for Rous sarcoma virus tyrosine kinase to uniquely label its direct substrates.Autophosphorylation is required for high kinase activity and efficient transformation ability of proteins encoded by host range alleles of v-src.Suppression of src transformation by overexpression of full-length GTPase-activating protein (GAP) or of the GAP C terminusVaccinia virus B1 kinase: phenotypic analysis of temperature-sensitive mutants and enzymatic characterization of recombinant proteins.Activation of the proto-oncogene p60c-src by point mutations in the SH2 domain.The common src homology region 2 domain of cytoplasmic signaling proteins is a positive effector of v-fps tyrosine kinase function.Deletions within the amino-terminal half of the c-src gene product that alter the functional activity of the protein.Transformation of chicken embryo fibroblasts by direct DNA transfection of single oncogenes: comparative analyses of src, erbB, myc, and ras.Delineation of functional determinants in the transforming protein of Fujinami sarcoma virus.Point mutations in the abl SH2 domain coordinately impair phosphotyrosine binding in vitro and transforming activity in vivo.Transformation by v-Src: Ras-MAPK and PI3K-mTOR mediate parallel pathways.Shc proteins are phosphorylated and regulated by the v-Src and v-Fps protein-tyrosine kinasesSecondary structure of Src homology 2 domain of c-Abl by heteronuclear NMR spectroscopy in solution.pp60v-src transformation of rat cells but not chicken cells strongly correlates with low-affinity phosphopeptide binding by the SH2 domain.
P2860
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P2860
Linker insertion-deletion mutagenesis of the v-src gene: isolation of host- and temperature-dependent mutants
description
1989 nî lūn-bûn
@nan
1989年の論文
@ja
1989年論文
@yue
1989年論文
@zh-hant
1989年論文
@zh-hk
1989年論文
@zh-mo
1989年論文
@zh-tw
1989年论文
@wuu
1989年论文
@zh
1989年论文
@zh-cn
name
Linker insertion-deletion muta ...... temperature-dependent mutants
@ast
Linker insertion-deletion muta ...... temperature-dependent mutants
@en
type
label
Linker insertion-deletion muta ...... temperature-dependent mutants
@ast
Linker insertion-deletion muta ...... temperature-dependent mutants
@en
prefLabel
Linker insertion-deletion muta ...... temperature-dependent mutants
@ast
Linker insertion-deletion muta ...... temperature-dependent mutants
@en
P2860
P1433
P1476
Linker insertion-deletion muta ...... temperature-dependent mutants
@en
P2093
G S Martin
J E DeClue
P2860
P304
P407
P577
1989-02-01T00:00:00Z