Evidence map›Paper›PMID 40587263›Full record

ReviewBiochemical Society transactions2025

Connecting tubules: mechanisms of endoplasmic reticulum membrane fusion.

Eunhong Jang, Youngsoo Jun

Abstract readReview
In one paragraph

Review in Biochemical Society transactions, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing 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

2 citing papers in PubMed.

  1. Rab10 Promotes Atlastin-Mediated Endoplasmic Reticulum Membrane Fusion.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2026
    Article
  2. 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

2 authors.

Eunhong JangDepartment of Life Sciences, Gwangju Institute of Science and Technology, Gwangju 61005, Republic of Korea.ORCID 0000-0002-3368-7940
Youngsoo JunIntegrated Institute of Biomedical Research, Gwangju Institute of Science and Technology, Gwangju 61005, Republic of Korea.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Atlastins (ATLs) are integral dynamin-like GTPases that are critical for the formation and maintenance of the endoplasmic reticulum (ER) network, one of the most complex and essential organelles in eukaryotic cells. The ER, which is composed of interconnected tubules and sheets, serves vital functions, including calcium storage, protein and lipid synthesis, and inter-organelle communication. Homotypic membrane fusion, mediated by ATLs, ensures the tubular structure of the ER by generating and stabilizing three-way junctions. Humans express three ATL paralogs, called ATL1, ATL2, and ATL3, which have distinct expression patterns and regulatory mechanisms. Mutations in these proteins are linked to hereditary sensory neuropathies and hereditary spastic paraplegia, highlighting their critical importance in cellular and neuronal health. Here, we review recent studies providing insights into how ATLs are regulated by their N- and C-terminal extensions, as well as how extrinsic factors potentially regulate the activities of ATLs to establish and maintain the normal ER structure.

Indexed as

Endoplasmic ReticulumGTP PhosphohydrolasesMembrane FusionAnimalsGTP-Binding ProteinsHumansMembrane ProteinsSpastic Paraplegia, HereditaryATL1 protein, humanGTP-Binding ProteinsGTP PhosphohydrolasesMembrane Proteinsendoplasmic reticulumGTPasesmembrane fusionorganelle biogenesis

Identifiers

PMID40587263
PMCPMC12312388

What OpenQuestion holds

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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 OpenQuestion graph.