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.

doi:10.1091/mbc.6.8.953

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Article

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.

Molecular biology of the cell - 1 Aug 1995

Verderame M F, Guan J L, Woods Ignatoski K M

Abstract excerpt

The biochemical properties of several pp60v-src substrates believed to participate in src-mediated transformation were examined in cells expressing a kinase-active, transformation-defective v-src allele (v-src-F172 delta/Y416F) and its parental allele, v-src-F172 delta, a host-range--dependent allele that transforms chicken cells to a fusiform morphology, but does not transform rat cells. Because pp60v-src-F172...

Topics

Adaptor Proteins, Signal Transducing
Adaptor Proteins, Vesicular Transport
Alleles
Animals
Cell Adhesion Molecules
Cell Line, Transformed
Cell Transformation, Neoplastic
Chickens
Cortactin
Focal Adhesion Kinase 1

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Focal Adhesion Protein-Tyrosine Kinases

GRB2 Adaptor Protein

GTPase-Activating Proteins

Genes, src

Microfilament Proteins

Oncogene Protein pp60(v-src)

Phosphatidylinositol 3-Kinases

Phosphorylation

Source

Open in PubMed Open full text

Identifiers

PMID: 7579711
DOI: 10.1091/mbc.6.8.953
PMCID: PMC301255

Genes

GRB2

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 29 Aug 2026. Prepared record publication-7579711-2026-08-29.1. Manifest publication-graph-cohort-2026-08-29.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 29 Aug 2026.

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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.PMID 7579711Read ↗

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

Autophosphorylation is required for high kinase activity and efficient transformation ability of proteins encoded by host range 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 ↗

Mutations in the SH3 domain of the src oncogene which decrease association of phosphatidylinositol 3'-kinase activity with pp60v-src and alter cellular morphology.Semantic proximity Read ↗

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

Functional dissection of transformation by c‐Src and v‐SrcSemantic proximity Read ↗

Mutational activation of pp60(c-src) leads to a tumorigenic phenotype in a preneoplastic Syrian hamster embryo cell line.Semantic proximity Read ↗

A mutation in the catalytic domain of pp60v-src is responsible for the host- and temperature-dependent phenotype of the Rous sarcoma virus mutant tsLA33-1.Semantic proximity Read ↗

Binding in vitro of phosphotyrosine-containing proteins to pp60c-src SH2 domain does not correlate with CEF transformation.Semantic proximity Read ↗

Site-directed mutagenesis of the SH2- and SH3-coding domains of c-src produces varied phenotypes, including oncogenic activation of p60c-src.Semantic proximity Read ↗

Tyrosine phosphorylation of three cellular proteins correlates with transformation of rat 1 cells by pp60src.Semantic proximity Read ↗

Reactivation of host-dependent src kinase activity by co-expression with a heterologous tyrosine kinase.Semantic proximity Read ↗

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