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Article

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

Molecular biology of the cell - 1 May 1997

Verderame M F

Abstract excerpt

Substrates critical for transformation by pp60v-src remain unknown, as does the precise role of the src homology 2 (SH2) domain in this process. To continue exploring the role of the SH2 domain in pp60v-src-mediated transformation, site-directed mutagenesis was used to create mutant v-src alleles...

Topics

Animals
Cell Line
Cell Transformation, Neoplastic
Chick Embryo
Gene Expression
Mutation
Oncogene Protein pp60(v-src)
Phosphopeptides
Protein Binding
Rats
Species Specificity
src Homology Domains

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Identifiers

PMID: 9168470
DOI: 10.1091/mbc.8.5.843
PMCID: PMC276133

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 30 Aug 2026. Prepared record publication-9168470-2026-08-30.1. Manifest publication-graph-cohort-2026-08-30.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 30 Aug 2026.

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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.PMID 9168470Read ↗

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 ↗

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 ↗

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

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

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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 ↗

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 ↗

Activation of the proto-oncogene p60c-src by point mutations in the SH2 domain.Semantic proximity Read ↗

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pp60c-src binding to polyomavirus middle T-antigen (MT) requires residues 185 to 210 of the MT sequence.Semantic proximity Read ↗

Aberrant protein phosphorylation at tyrosine is responsible for the growth-inhibitory action of pp60v-src expressed in the yeast Saccharomyces cerevisiae.Semantic proximity Read ↗

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