Evidence map›Paper›PMID 27619977›Full record

ArticleeLife2016

Cooperation of the ER-shaping proteins atlastin, lunapark, and reticulons to generate a tubular membrane network.

Songyu Wang, Hanna Tukachinsky, Fabian B Romano, Tom A Rapoport

Abstract read
In one paragraph

Article in eLife, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 122 papers.

0numbers the graph read from it
0cells of the map it votes in
122citing 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

122 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. ATL2 Recruits TRAK1 to Promote Mitochondrial Transport at ER-Mitochondria Contact Sites.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026
    Article
  3. Article
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  6. Zika NS2B Protein: In Vitro Formation of Large Multimeric Networks.International journal of molecular sciences · 2026
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62 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

4 authors.

Songyu WangHoward Hughes Medical Institute, Harvard Medical School, Boston, United States.
Hanna TukachinskyHoward Hughes Medical Institute, Harvard Medical School, Boston, United States.
Fabian B RomanoHoward Hughes Medical Institute, Harvard Medical School, Boston, United States.
Tom A RapoportHoward Hughes Medical Institute, Harvard Medical School, Boston, United States.ORCID 0000-0001-9911-4216

Funding

Howard Hughes Medical Institute
6 · The paper itself

Abstract

In higher eukaryotes, the endoplasmic reticulum (ER) contains a network of membrane tubules, which transitions into sheets during mitosis. Network formation involves curvature-stabilizing proteins, including the reticulons (Rtns), as well as the membrane-fusing GTPase atlastin (ATL) and the lunapark protein (Lnp). Here, we have analyzed how these proteins cooperate. ATL is needed to not only form, but also maintain, the ER network. Maintenance requires a balance between ATL and Rtn, as too little ATL activity or too high Rtn4a concentrations cause ER fragmentation. Lnp only affects the abundance of three-way junctions and tubules. We suggest a model in which ATL-mediated fusion counteracts the instability of free tubule ends. ATL tethers and fuses tubules stabilized by the Rtns, and transiently sits in newly formed three-way junctions. Lnp subsequently moves into the junctional sheets and forms oligomers. Lnp is inactivated by mitotic phosphorylation, which contributes to the tubule-to-sheet conversion of the ER.

Indexed as

Organelle BiogenesisEndoplasmic ReticulumEukaryotaMembrane ProteinsMembrane Proteinscell biologyendoplasmic reticulumhumanmembrane structureorganelle morphologyxenopus

Identifiers

PMID27619977
PMCPMC5021524

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Registered trials

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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.