Evidence map›Paper›PMID 27343996›Full record

ReviewJournal of structural biology2016

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

Annika Hohendahl, Aurélien Roux, Valentina Galli

Open access · hybridAbstract readReview
In one paragraph

Review in Journal of structural biology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
1.7field-weighted citation impact, top 18% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

24 citing papers in PubMed, 39 citations in OpenAlex.

  1. Article
  2. Bend it like BIN1: how a membrane-curving adaptor protein shapes cardiac physiology.American journal of physiology. Heart and circulatory physiology · 2025
    Review
  3. BIN1 reduction amelioratesProceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  4. A novelFrontiers in genetics · 2025
    Article
  5. Review
  6. Dynamics of membrane tubulation coupled with fission by a two-component module.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  7. Article
  8. Molecular mechanisms of polarized transport to the apical plasma membrane.Frontiers in cell and developmental biology · 2024
    Review
  9. Article
  10. Review
  11. Article
  12. Article
  13. Genes · 2022
    Article
  14. Review
  15. Article
  16. Article
  17. Article
  18. Article
  19. Phosphatidylinositol Kinases and Phosphatases inFrontiers in cellular and infection microbiology · 2019
    Review
  20. Protein Amphipathic Helix Insertion: A Mechanism to Induce Membrane Fission.Frontiers in cell and developmental biology · 2019
    Review
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

3 authors at 1 institution in 1 country.

Annika HohendahlBiochemistry Department, University of Geneva, CH-1211 Geneva, Switzerland.
Aurélien RouxBiochemistry Department, University of Geneva, CH-1211 Geneva, Switzerland; Swiss National Centre for Competence in Research Programme Chemical Biology, CH-1211 Geneva, Switzerland. Electronic address: Aurelien.roux@unige.ch.
Valentina GalliBiochemistry Department, University of Geneva, CH-1211 Geneva, Switzerland.
University of Geneva · CH

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

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 functional data from the study of endocytosis mainly, we discuss how the CNM mutations could affect the structure and the function of these ubiquitous proteins and cause the muscle-specific phenotype. The literature shows that both proteins are involved in the plasma membrane tubulation required for T-tubule biogenesis. However, this system also requires the regulation of the dynamin-mediated membrane fission, and the formation of a stable protein-scaffold to maintain the T-tubule structure. We discuss how the specific functions, isoforms and partners (myotubularin in particular) of these two proteins can lead to the establishment of muscle-specific features.

Indexed as

MutationAdaptor Proteins, Signal TransducingDynamin IIEndocytosisMuscle, SkeletalMyopathies, Structural, CongenitalNuclear ProteinsTumor Suppressor ProteinsAdaptor Proteins, Signal TransducingBIN1 protein, humanDynamin IINuclear ProteinsTumor Suppressor ProteinsBAR domainBIN1Centranuclear myopathyClathrin-mediated endocytosisDynaminMembrane fissionMuscleMyotubularinStructureT-tubule

Identifiers

PMID27343996
PMCPMC5039012
OpenAlexW2460101436

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.