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 Bin/amphiphysin/Rvs (BAR) domain protein endophilin B2 interacts with plectin and controls perinuclear cytoskeletal architecture.

The Journal of biological chemistry - 20 Sept 2013

Vannier Christian, Pesty Arlette, San-Roman Mabel Jouve, Schmidt Anne A

Abstract excerpt

Proteins of the Bin/amphiphysin/Rvs (BAR) domain superfamily are essential in controlling the shape and dynamics of intracellular membranes. Here, we present evidence for the unconventional function of a member of the endophilin family of BAR and Src homology 3 domain-containing proteins, namely endophilin B2, in the perinuclear organization of intermediate filaments. Using mass spectrometry analysis based on...

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 Carrier Proteins

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Cell Nucleus

Share to Cytoskeleton

Share to HeLa Cells

Share to Multiprotein Complexes

Share to Plectin

Share to Protein Structure, Tertiary

Source

Open in PubMed Open full text

Identifiers

PMID: 23921385
DOI: 10.1074/jbc.M113.485482
PMCID: PMC3779758

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

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

The Bin/amphiphysin/Rvs (BAR) domain protein endophilin B2 interacts with plectin and controls perinuclear cytoskeletal architecture.PMID 23921385Read ↗

EPH Receptor Tyrosine Kinases Regulate Epithelial Morphogenesis and Phosphorylate the PAR-3 Scaffold Protein to Modulate Downstream Signaling NetworksSemantic proximity Read ↗

Endophilin BAR domain drives membrane curvature by two newly identified structure-based mechanisms.Semantic proximity Read ↗

Drebrin forms a cortical hub that connects actin, microtubules, and clathrin for endocytic transport of β2 integrinSemantic proximity Read ↗

GAS7 coordinates the activity of RAC1 and CDC42 to enhance macropinocytic surveillance and suppress motility in macrophagesSemantic proximity Read ↗

BAR domains as sensors of membrane curvature: the amphiphysin BAR structure.Semantic proximity Read ↗

The membrane curvature inducing REEP1 proteins generate a novel ER-derived vesicular compartmentSemantic proximity Read ↗

Septin 9-containging filaments and Golgi assembly depend on two polybasic domainsSemantic proximity Read ↗

The tails of apical scaffolding proteins EBP50 and E3KARP regulate their localization and dynamics.Semantic proximity Read ↗

Microscopic clusters feature the composition of biochemical tetraspanin-assemblies and constitute building-blocks of tetraspanin enriched domainsSemantic proximity Read ↗

Tetraspanin Proteins Mediate Cellular Penetration, Invasion, and Fusion Events and Define a Novel Type of Membrane MicrodomainSemantic proximity Read ↗

Role of plectin in cytoskeleton organization and dynamicsSemantic proximity Read ↗

Dynamin-2 Phosphorylation as A Critical Regulatory Target of Bin1 and GSK3α for Endocytosis in MuscleSemantic proximity Read ↗

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