Phosphotyrosine binding domain-dependent upregulation of the platelet-derived growth factor receptor alpha signaling cascade by transforming mutants of Cbl: implications for Cbl's function and oncogenicity.

doi:10.1128/MCB.17.8.4597

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Article

Phosphotyrosine binding domain-dependent upregulation of the platelet-derived growth factor receptor alpha signaling cascade by transforming mutants of Cbl: implications for Cbl's function and oncogenicity.

Molecular and cellular biology - 1 Aug 1997

Bonita D P, Miyake S, Lupher M L, Langdon W Y, Band H

Abstract excerpt

Recent studies have demonstrated that Cbl, the 120-kDa protein product of the c-cbl proto-oncogene, serves as a substrate of a number of receptor-coupled tyrosine kinases and forms complexes with SH3 and SH2 domain-containing proteins, pointing to its role in signal transduction. Based on genetic...

Topics

3T3 Cells
Animals
Cell Division
Cell Transformation, Neoplastic
Humans
Mice
Mutation
Phosphoproteins
Phosphorylation
Phosphotyrosine
Platelet-Derived Growth Factor
Protein-Tyrosine Kinases
Proto-Oncogene Mas
Proto-Oncogene Proteins

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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Proto-Oncogene Proteins c-cbl

Receptor, Platelet-Derived Growth Factor alpha

Receptors, Platelet-Derived Growth Factor

Signal Transduction

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Identifiers

PMID: 9234717
DOI: 10.1128/MCB.17.8.4597
PMCID: PMC232313

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 30 Aug 2026. Prepared record publication-9234717-2026-08-30.1. Manifest publication-graph-cohort-2026-08-30.1.

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