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

Structural insights into the centronuclear myopathy-associated functions of BIN1 and dynamin 2.

Journal of structural biology - 1 Oct 2016

Hohendahl Annika, Roux Aurélien, Galli Valentina

Abstract excerpt

Centronuclear myopathies (CNMs) are genetic diseases whose symptoms are muscle weakness and atrophy (wasting) and centralised nuclei. Recent human genetic studies have isolated several groups of mutations. Among them, many are found in two interacting proteins essential to clathrin-mediated endocytosis, dynamin and the BIN-Amphiphysin-Rvs (BAR) protein BIN1/amphiphysin 2. In this review, by using structural and...

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 Dynamin II
Share to Endocytosis

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Muscle, Skeletal

Share to Mutation

Share to Myopathies, Structural, Congenital

Share to Nuclear Proteins

Share to Tumor Suppressor Proteins

Source

Open in PubMed Open full text

Identifiers

PMID: 27343996
DOI: 10.1016/j.jsb.2016.06.015
PMCID: PMC5039012

Genes

BIN1

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

Structural insights into the centronuclear myopathy-associated functions of BIN1 and dynamin 2.PMID 27343996Read ↗

Centronuclear Myopathy Caused by Defective Membrane Remodelling of Dynamin 2 and BIN1 Variants.Semantic proximity Read ↗

Dynamin-2 mutations associated with centronuclear myopathy are hypermorphic and lead to T-tubule fragmentation.Semantic proximity Read ↗

MTM1 overexpression prevents and reverts BIN1-related centronuclear myopathy.Semantic proximity Read ↗

Defective membrane remodeling in neuromuscular diseases: insights from animal models.Semantic proximity Read ↗

Mice with muscle-specific deletion of Bin1 recapitulate centronuclear myopathy and acute downregulation of dynamin 2 improves their phenotypes.Semantic proximity Read ↗

Defects in amphiphysin 2 (BIN1) and triads in several forms of centronuclear myopathies.Semantic proximity Read ↗

Adult-onset autosomal dominant centronuclear myopathy due to BIN1 mutations.Semantic proximity Read ↗

Mutations in amphiphysin 2 (BIN1) disrupt interaction with dynamin 2 and cause autosomal recessive centronuclear myopathy.Semantic proximity Read ↗

A centronuclear myopathy-dynamin 2 mutation impairs skeletal muscle structure and function in mice.Semantic proximity Read ↗

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

A novel mutation in the DNM2 gene impairs dynamin 2 localization in skeletal muscle of a patient with late onset centronuclear myopathy.Semantic proximity Read ↗

Uncovering the BIN1-SH3 interactome underpinning centronuclear myopathy.Semantic proximity Read ↗

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