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Article

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

Journal of virology - 1 Nov 1994

Woods K M, Verderame M F

Abstract excerpt

pp60v-src is a nonreceptor protein tyrosine kinase that can transform both chicken and rodent fibroblasts. The src homology 2 (SH2) domain of this protein serves a critical role in the regulation of protein tyrosine kinase activity. The host range proteins pp60v-src-L, which contains a deletion of a highly conserved residue (Phe-172) in the SH2 domain, and pp60v-src-PPP, which contains a change from a Leu to a...

Topics

Alleles
Amino Acid Sequence
Animals
Base Sequence
Cell Transformation, Neoplastic
Cells, Cultured
Chick Embryo
Genes, src
Molecular Sequence Data
Oncogene Protein pp60(v-src)
Phosphorylation

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Protein-Tyrosine Kinases

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Identifiers

PMID: 7933110
DOI: 10.1128/JVI.68.11.7267-7274.1994
PMCID: PMC237167

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 29 Aug 2026. Prepared record publication-7933110-2026-08-29.1. Manifest publication-graph-cohort-2026-08-29.1.

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

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Autophosphorylation is required for high kinase activity and efficient transformation ability of proteins encoded by host range alleles of v-src.PMID 7933110Read ↗

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 ↗

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

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

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

Regulation of the oncogenic activity of the cellular src protein requires the correct spacing between the kinase domain and the C-terminal phosphorylated tyrosine (Tyr-527).Semantic proximity Read ↗

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

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