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Article

The evolutionarily conserved N-terminal region of Cbl is sufficient to enhance down-regulation of the epidermal growth factor receptor.

The Journal of biological chemistry - 7 Jan 2000

Lill N L, Douillard P, Awwad R A, Ota S, Lupher M L, Miyake S, Meissner-Lula N, Hsu V W, Band H

Abstract excerpt

The mammalian proto-oncoprotein Cbl and its homologues in Caenorhabditis elegans and Drosophila are evolutionarily conserved negative regulators of the epidermal growth factor receptor (EGF-R). Overexpression of wild-type Cbl enhances down-regulation of activated EGF-R from the cell surface. We report that the Cbl tyrosine kinase-binding (TKB) domain is essential for this activity. Whereas wild-type Cbl enhanced...

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Source

Identifiers

PMID: 10617627
DOI: 10.1074/jbc.275.1.367

Genes

EGF

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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The evolutionarily conserved N-terminal region of Cbl is sufficient to enhance down-regulation of the epidermal growth factor receptor.PMID 10617627Read ↗

Cbl-mediated ubiquitinylation is required for lysosomal sorting of epidermal growth factor receptor but is dispensable for endocytosis.Semantic proximity Read ↗

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c-Cbl/Sli-1 regulates endocytic sorting and ubiquitination of the epidermal growth factor receptor.Semantic proximity Read ↗

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RING finger mutations that abolish c-Cbl-directed polyubiquitination and downregulation of the EGF receptor are insufficient for cell transformation.Semantic proximity Read ↗

Epidermal growth factor receptors with tyrosine kinase domain mutations exhibit reduced Cbl association, poor ubiquitylation, and down-regulation but are efficiently internalized.Semantic proximity Read ↗

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