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

The N terminus of Cbl-c regulates ubiquitin ligase activity by modulating affinity for the ubiquitin-conjugating enzyme.

The Journal of biological chemistry - 30 Jul 2010

Ryan Philip E, Sivadasan-Nair Nina, Nau Marion M, Nicholas Sarah, Lipkowitz Stanley

Abstract excerpt

Cbl proteins are ubiquitin ligases (E3s) that play a significant role in regulating tyrosine kinase signaling. There are three mammalian family members: Cbl, Cbl-b, and Cbl-c. All have a highly conserved N-terminal tyrosine kinase binding domain, a catalytic RING finger domain, and a C-terminal proline-rich domain that mediates interactions with Src homology 3 (SH3) containing proteins. Although both Cbl and...

Read the complete abstract on PubMed

Topics

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

Share to Glutathione Transferase
Share to Kinetics

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Mutagenesis, Site-Directed

Share to Proto-Oncogene Proteins c-cbl

Share to Recombinant Proteins

Share to src Homology Domains

Share to Ubiquitin

Share to Ubiquitin-Protein Ligases

Source

Open in PubMed Open full text

Identifiers

PMID: 20525694
DOI: 10.1074/jbc.M109.091157
PMCID: PMC2911298

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 5 Sept 2026. Manifest publication-graph-cohort-2026-09-05.1.

Source receipt: pubmed, retrieved 5 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

The N terminus of Cbl-c regulates ubiquitin ligase activity by modulating affinity for the ubiquitin-conjugating enzyme.PMID 20525694Read ↗

The Cbl RING finger C-terminal flank controls epidermal growth factor receptor fate downstream of receptor ubiquitination.Semantic proximity Read ↗

Regulation of ubiquitin protein ligase activity in c-Cbl by phosphorylation-induced conformational change and constitutive activation by tyrosine to glutamate point mutations.Semantic proximity Read ↗

The RING finger domain of Cbl is essential for negative regulation of the Syk tyrosine kinase.Semantic proximity Read ↗

Sprouty2 acts at the Cbl/CIN85 interface to inhibit epidermal growth factor receptor downregulation.Semantic proximity Read ↗

Structural flexibility regulates phosphopeptide-binding activity of the tyrosine kinase binding domain of Cbl-c.Semantic proximity Read ↗

The role of CBL family ubiquitin ligases in cancer progression and therapeutic strategiesSemantic proximity Read ↗

Modulation of Immune Cell Functions by the E3 Ligase Cbl-bSemantic proximity Read ↗

Mutant Cbl proteins as oncogenic drivers in myeloproliferative disordersSemantic proximity Read ↗

Mutations of c-Cbl in myeloid malignancies.Semantic proximity Read ↗

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

E3 ligase-inactivation rewires CBL interactome to elicit oncogenesis by hijacking RTK-CBL-CIN85 axis.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 ↗

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