Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Direct interaction of Cbl with pTyr 1045 of the EGF receptor (EGFR) is required to sort the EGFR to lysosomes for degradation.

Experimental cell research - 1 Nov 2004

Grøvdal Lene Melsaether, Stang Espen, Sorkin Alexander, Madshus Inger Helene

Abstract excerpt

Mutation of the binding site for Cbl (Tyr1045) in the EGF receptor (EGFR) results in impaired ubiquitination but does not affect EGFR internalization. However, the Y1045F mutation resulted in strongly decreased degradation of the EGFR, as well as efficient recycling of EGFR to the plasma membrane...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Epidermal Growth Factor
Share to ErbB Receptors
Share to HeLa Cells

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Lysosomes

Share to Proto-Oncogene Proteins

Share to Proto-Oncogene Proteins c-cbl

Share to Tyrosine

Share to Ubiquitin-Protein Ligases

Source

Identifiers

PMID: 15475003
DOI: 10.1016/j.yexcr.2004.07.003

Genes

EGFR
EGF

Variants

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 1 Sept 2026. Prepared record publication-15475003-2026-09-01.1. Manifest publication-graph-cohort-2026-09-01.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 1 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Direct interaction of Cbl with pTyr 1045 of the EGF receptor (EGFR) is required to sort the EGFR to lysosomes for degradation.PMID 15475003Read ↗

A tale of two Cbls: interplay of c-Cbl and Cbl-b in epidermal growth factor receptor downregulation.Semantic proximity Read ↗

Serine mutations that abrogate ligand-induced ubiquitination and internalization of the EGF receptor do not affect c-Cbl association with the receptor.Semantic proximity Read ↗

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

CIN85 phosphorylation is essential for EGFR ubiquitination and sorting into multivesicular bodies.Semantic proximity Read ↗

c-Cbl ubiquitinates the EGF receptor at the plasma membrane and remains receptor associated throughout the endocytic route.Semantic proximity Read ↗

A mutant EGF-receptor defective in ubiquitylation and endocytosis unveils a role for Grb2 in negative signaling.Semantic proximity Read ↗

c-Cbl-mediated ubiquitinylation is required for epidermal growth factor receptor exit from the early endosomes.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 ↗

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

EGF receptor ubiquitination is not necessary for its internalization.Semantic proximity Read ↗

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

[Ubiquitination-mediated degradation of epidermal growth factor receptor].Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.