Discover Community Create You

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

Ligand binding induces Cbl-dependent EphB1 receptor degradation through the lysosomal pathway.

Traffic (Copenhagen, Denmark) - 1 Feb 2008

Fasen Katrin, Cerretti Douglas Pat, Huynh-Do Uyen

Abstract excerpt

Eph receptor tyrosine kinases play a critical role in embryonic patterning and angiogenesis. In the adult, they are involved in carcinogenesis and pathological neovascularization. However, the mechanisms underlying their role in tumor formation and metastasis remain to be defined. Here, we demons...

Read the complete abstract on PubMed

Topics

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

Share to Acetylcysteine
Share to Cell Communication
Share to Endocytosis

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Lysosomes

Share to Macrolides

Share to Proto-Oncogene Proteins c-cbl

Share to src-Family Kinases

Share to Ubiquitination

Source

Identifiers

PMID: 18034775
DOI: 10.1111/j.1600-0854.2007.00679.x

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 2 Sept 2026. Prepared record publication-18034775-2026-09-02.2. Manifest publication-graph-cohort-2026-09-02.2.

Source receipt: PubMed via Helena Literature Corpus, retrieved 2 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Ligand binding induces Cbl-dependent EphB1 receptor degradation through the lysosomal pathway.PMID 18034775Read ↗

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

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

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

A role of the protein Cbl in FGF-2-induced angiogenesis in murine brain endothelial cells.Semantic proximity Read ↗

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

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

Direct binding of Cbl to Tyr568 and Tyr936 of the stem cell factor receptor/c-Kit is required for ligand-induced ubiquitination, internalization and degradation.Semantic proximity Read ↗

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

C-Cbl binds the CSF-1 receptor at tyrosine 973, a novel phosphorylation site in the receptor's carboxy-terminus.Semantic proximity Read ↗

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

Ligand binding and calcium influx induce distinct ectodomain/gamma-secretase-processing pathways of EphB2 receptor.Semantic proximity Read ↗

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

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