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

Multiple domains of Ruk/CIN85/SETA/CD2BP3 are involved in interaction with p85alpha regulatory subunit of PI 3-kinase.

Journal of molecular biology - 29 Oct 2004

Borthwick Emma B, Korobko Igor V, Luke Courtney, Drel Victor R, Fedyshyn Yaroslav Ya, Ninkina Natalia, Drobot Ludmila B, Buchman Vladimir L

Abstract excerpt

Ruk/CIN85/SETA/CD2BP3 and CD2AP/CMS/METS-1 comprise a new family of proteins involved in such fundamental processes as clustering of receptors and rearrangement of the cytoskeleton in regions of specialised cell-cell contacts, ligand-activated internalisation and targeting to lysosome degradation pathway of receptor tyrosine kinases, and apoptotic cell death. As typical adapter proteins they execute these...

Read the complete abstract on PubMed

Topics

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

Share to Adaptor Proteins, Signal Transducing
Share to Amino Acid Sequence

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Molecular Sequence Data

Share to Mutation

Share to Phosphatidylinositol 3-Kinases

Share to Protein Isoforms

Share to Protein Structure, Tertiary

Share to Two-Hybrid System Techniques

Source

Identifiers

PMID: 15476827
DOI: 10.1016/j.jmb.2004.08.075

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.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Multiple domains of Ruk/CIN85/SETA/CD2BP3 are involved in interaction with p85alpha regulatory subunit of PI 3-kinase.PMID 15476827Read ↗

Emerging Roles of Ruk/CIN85 in Vesicle-Mediated Transport, Adhesion, Migration and MalignancySemantic proximity Read ↗

CrkIII: a novel and biologically distinct member of the Crk family of adaptor proteinsSemantic proximity Read ↗

CIN85/RukL Is a Novel Binding Partner of Nephrin and Podocin and Mediates Slit Diaphragm Turnover in PodocytesSemantic proximity Read ↗

The Major CD9 and CD81 Molecular PartnerSemantic proximity Read ↗

Molecular and immunohistochemical analysis of signaling adaptor protein Crk in human cancersSemantic proximity Read ↗

Models of Crk Adaptor Proteins in CancerSemantic proximity Read ↗

Increased levels of the HER1 adaptor protein Ruk l /CIN85 contribute to breast cancer malignancySemantic proximity Read ↗

Functional specificity in 14-3-3 isoform interactions through dimer formation and phosphorylation. Chromosome location of mammalian isoforms and variants.Semantic proximity Read ↗

Nephrin binds to the COOH terminus of a large-conductance Ca<sup>2+</sup>-activated K<sup>+</sup> channel isoform and regulates its expression on the cell surfaceSemantic proximity Read ↗

The adapter protein Nck: Role of individual SH3 and SH2 binding modules for protein interactions in T lymphocytesSemantic proximity Read ↗

SETA/CIN85/Ruk and its binding partner AIP1 associate with diverse cytoskeletal elements, including FAKs, and modulate cell adhesion.Semantic proximity Read ↗

Distinct ubiquitin binding modes exhibited by SH3 domains: molecular determinants and functional implications.Semantic proximity Read ↗

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