Evidence map›Paper›PMID 42349418›Full record

ArticleDevelopmental cell2026

The ALS- and FTD-associated proteins annexin A11 and CHMP2B act sequentially in plasma membrane repair.

Catherine M Heffner, Georgina P Starling, Lorian C Straker, Philippa C Hawes, Adrian M Isaacs, Jeremy G Carlton

Abstract read
In one paragraph

Article in Developmental cell, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
–field-weighted citation impact
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

4 citing papers in PubMed.

  1. Sorcin couples Annexin A11 recruitment to ESCRT-III assembly for plasma membrane repair.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  2. Review
  3. Article
  4. 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

6 authors.

Catherine M HeffnerOrganelle Dynamics Laboratory, The Francis Crick Institute, 1 Midland Road, London NW1 1AT, UK; UK Dementia Research Institute at UCL, London WC1E 6BT, UK; Department of Neurodegenerative Disease, UCL Queen Square Institute of Neurology, London WC1N 3BG, UK.
Georgina P StarlingOrganelle Dynamics Laboratory, The Francis Crick Institute, 1 Midland Road, London NW1 1AT, UK; School of Cancer & Pharmaceutical Sciences, King's College London, London SE1 1UL, UK; UK Dementia Research Institute at UCL, London WC1E 6BT, UK; Department of Neurodegenerative Disease, UCL Queen Square Institute of Neurology, London WC1N 3BG, UK.
Lorian C StrakerElectron Microscopy Science Technology Platform, The Francis Crick Institute, 1 Midland Road, London NW1 1AT, UK.
Philippa C HawesElectron Microscopy Science Technology Platform, The Francis Crick Institute, 1 Midland Road, London NW1 1AT, UK.
Adrian M IsaacsUK Dementia Research Institute at UCL, London WC1E 6BT, UK; Department of Neurodegenerative Disease, UCL Queen Square Institute of Neurology, London WC1N 3BG, UK. Electronic address: a.isaacs@ucl.ac.uk.
Jeremy G CarltonOrganelle Dynamics Laboratory, The Francis Crick Institute, 1 Midland Road, London NW1 1AT, UK; School of Cancer & Pharmaceutical Sciences, King's College London, London SE1 1UL, UK. Electronic address: jeremy.carlton@kcl.ac.uk.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Maintenance of plasma membrane integrity is essential for compartmentalization of the cytosol and for cellular viability. Upon membrane damage, several factors including endosomal sorting complex required for transport-III (ESCRT-III) proteins, annexins, stress granules, lipids, and membrane fusion proteins are mobilized to orchestrate membrane repair. However, whether these factors operate independently or act together is unclear. Here, using human cell lines, we expose temporal differences and interdependencies in the recruitment of ESCRT-III and annexin proteins to sites of plasma membrane damage. We show that annexin proteins are recruited immediately and form a plug at the damage site, restricting membrane permeability. We find that ESCRT-III assembles later and acts to release plug-containing damaged membranes from the cell. Further, frontotemporal dementia (FTD)- and amyotrophic lateral sclerosis (ALS)-associated mutations in the ESCRT-III protein, CHMP2B, and the annexin protein, ANXA11, compromise plasma membrane repair, suggesting that defects in this process may contribute to these pathologies. These data present an integrated "sealing and healing" model of membrane repair.

Indexed as

Amyotrophic Lateral SclerosisAnnexinsCell MembraneEndosomal Sorting Complexes Required for TransportFrontotemporal DementiaHumansMutationAnnexinsCHMP2B protein, humanEndosomal Sorting Complexes Required for TransportALSannexinANXA11CHMP2BESCRT-IIIFTDmembrane repairpore-forming toxin

Identifiers

PMID42349418
PMCPMC13374510

What Socratic holds

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LicenceCC BY
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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 Socratic graph.