Evidence map›Paper›PMID 33495454›Full record

ArticleNature communications2021

Mechanism of membrane-curvature generation by ER-tubule shaping proteins.

Ning Wang, Lindsay D Clark, Yuan Gao, Michael M Kozlov, Tom Shemesh, Tom A Rapoport

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 54 papers.

0numbers the graph read from it
0cells of the map it votes in
54citing papers in PubMed
8.0field-weighted citation impact, top 1% 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

54 citing papers in PubMed, 95 citations in OpenAlex.

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  15. Organelle abnormalities in Alzheimer's disease.Organelle (Tucson, Ariz.) · 2025
    Article
  16. Visualizing ER-phagy and ER architecture in vivo.The Journal of cell biology · 2024
    Article
  17. Article
  18. Article
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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 at 3 institutions in 2 countries.

Ning WangHoward Hughes Medical Institute and Department of Cell Biology, Harvard Medical School, Boston, MA, 02115, USA.
Lindsay D ClarkHoward Hughes Medical Institute and Department of Cell Biology, Harvard Medical School, Boston, MA, 02115, USA.ORCID 0000-0001-6879-6883
Yuan GaoHoward Hughes Medical Institute and Department of Cell Biology, Harvard Medical School, Boston, MA, 02115, USA.
Michael M KozlovDepartment of Physiology and Pharmacology, Sackler Faculty of Medicine, Tel Aviv University, Tel Aviv, 69978, Israel.ORCID 0000-0002-0891-4785
Tom ShemeshFaculty of Biology, Technion-Israel Institute of Technology, Haifa, 32000, Israel.
Tom A RapoportHoward Hughes Medical Institute and Department of Cell Biology, Harvard Medical School, Boston, MA, 02115, USA. tom_rapoport@hms.harvard.edu.ORCID 0000-0001-9911-4216
Howard Hughes Medical Institute · USTechnion – Israel Institute of Technology · ILTel Aviv University · IL

Funding

Howard Hughes Medical Institute
6 · The paper itself

Abstract

The endoplasmic reticulum (ER) network consists of tubules with high membrane curvature in cross-section, generated by the reticulons and REEPs. These proteins have two pairs of trans-membrane (TM) segments, followed by an amphipathic helix (APH), but how they induce curvature is poorly understood. Here, we show that REEPs form homodimers by interaction within the membrane. When overexpressed or reconstituted at high concentrations with phospholipids, REEPs cause extreme curvature through their TMs, generating lipoprotein particles instead of vesicles. The APH facilitates curvature generation, as its mutation prevents ER network formation of reconstituted proteoliposomes, and synthetic L- or D-amino acid peptides abolish ER network formation in Xenopus egg extracts. In Schizosaccharomyces japonicus, the APH is required for reticulon's exclusive ER-tubule localization and restricted mobility. Thus, the TMs and APH cooperate to generate high membrane curvature. We propose that the formation of splayed REEP/reticulon dimers is responsible for ER tubule formation.

Indexed as

AnimalsCell MembraneEndoplasmic ReticulumFungal ProteinsLipoproteinsMembrane ProteinsMicroscopy, ElectronMutationProtein MultimerizationSchizosaccharomycesXenopus ProteinsFungal ProteinsLipoproteinsMembrane ProteinsXenopus Proteins

Identifiers

PMID33495454
PMCPMC7835363
OpenAlexW3121357345

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.