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Article

Host range mutants of v-src: alterations in kinase activity and substrate interactions.

Journal of virology - 1 Jul 1992

Liebl E C, England L J, DeClue J E, Martin G S

Abstract excerpt

Host range mutants of Schmidt-Ruppin v-src that transform chicken embryo fibroblasts (CEF) but not Rat-2 cells were generated previously by linker insertion-deletion mutagenesis (J. E. DeClue and G. S. Martin, J. Virol. 63:542-554, 1989). One of these mutants, SRX5, in which Tyr-416 is substituted by the sequence Ser Arg Asp, retained high levels of kinase activity in vitro and in vivo, both in CEF and in Rat-2...

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Identifiers

PMID: 1534851
DOI: 10.1128/JVI.66.7.4315-4324.1992
PMCID: PMC241237

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Host range mutants of v-src: alterations in kinase activity and substrate interactions.PMID 1534851Read ↗

Autophosphorylation is required for high kinase activity and efficient transformation ability of proteins encoded by host range alleles of v-src.Semantic proximity Read ↗

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pp60v-src transformation of rat cells but not chicken cells strongly correlates with low-affinity phosphopeptide binding by the SH2 domain.Semantic proximity Read ↗

Transformation and pp60v-src autophosphorylation correlate with SHC-GRB2 complex formation in rat and chicken cells expressing host-range and kinase-active, transformation-defective alleles of v-src.Semantic proximity Read ↗

Highly conserved amino acids in the SH2 and catalytic domains of v-src are altered in naturally occurring, transformation-defective alleles.Semantic proximity Read ↗

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Biological and biochemical activity of v-Crk chimeras containing the SH2/SH3 regions of phosphatidylinositol-specific phospholipase C-gamma and Src.Semantic proximity Read ↗

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