Evidence map›Paper›PMID 34166613›Full record

ArticleCell2021

Structural basis for VIPP1 oligomerization and maintenance of thylakoid membrane integrity.

Tilak Kumar Gupta, Sven Klumpe, Karin Gries, Steffen Heinz, Wojciech Wietrzynski, Norikazu Ohnishi, Justus Niemeyer, Benjamin Spaniol, Miroslava Schaffer, Anna Rast and 10 more

Open access · bronzeAbstract read
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In one paragraph

Article in Cell, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 75 papers.

0numbers the graph read from it
0cells of the map it votes in
75citing papers in PubMed
8.4field-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

75 citing papers in PubMed, 154 citations in OpenAlex.

  1. Article
  2. VIA1 is a conserved regulator of thylakoid membrane integrity that acts through VIPP1.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  3. Article
  4. Article
  5. Article
  6. Membrane interaction of cyanobacterial and chloroplast ESCRT-III proteins.The Plant journal : for cell and molecular biology · 2026
    Review
  7. Article
  8. Article
  9. Molecular structure of the ESCRT-III-based archaeal CdvAB cell division machinery.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  10. Article
  11. Article
  12. Review
  13. Article
  14. Article
  15. Article
  16. Article
  17. The bacterial ESCRT-III PspA rods thin lipid tubules and increase membrane curvature through helix α0 interactions.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  18. Review
  19. Article
  20. Article

15 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

20 authors at 8 institutions in 3 countries.

Tilak Kumar GuptaDepartment of Molecular Structural Biology, Max Planck Institute of Biochemistry, 82152 Martinsried, Germany.
Sven KlumpeDepartment of Molecular Structural Biology, Max Planck Institute of Biochemistry, 82152 Martinsried, Germany.
Karin GriesMolecular Biotechnology and Systems Biology, Technische Universität Kaiserslautern, 67663 Kaiserslautern, Germany.
Steffen HeinzDepartment of Molecular Plant Sciences, LMU Munich, 82152 Martinsried, Germany.
Wojciech WietrzynskiDepartment of Molecular Structural Biology, Max Planck Institute of Biochemistry, 82152 Martinsried, Germany; Helmholtz Pioneer Campus, Helmholtz Zentrum München, 85764 Neuherberg, Germany.
Norikazu OhnishiInstitute of Plant Science and Resources, Okayama University, Kurashiki, Okayama 710-0046, Japan.
Justus NiemeyerMolecular Biotechnology and Systems Biology, Technische Universität Kaiserslautern, 67663 Kaiserslautern, Germany.
Benjamin SpaniolMolecular Biotechnology and Systems Biology, Technische Universität Kaiserslautern, 67663 Kaiserslautern, Germany.
Miroslava SchafferDepartment of Molecular Structural Biology, Max Planck Institute of Biochemistry, 82152 Martinsried, Germany.
Anna RastDepartment of Molecular Structural Biology, Max Planck Institute of Biochemistry, 82152 Martinsried, Germany; Department of Molecular Plant Sciences, LMU Munich, 82152 Martinsried, Germany.
Matthias OstermeierDepartment of Molecular Plant Sciences, LMU Munich, 82152 Martinsried, Germany.
Mike StraussDepartment of Anatomy and Cell Biology, McGill University, Montreal, QC H3A 17C, Canada.
Jürgen M PlitzkoDepartment of Molecular Structural Biology, Max Planck Institute of Biochemistry, 82152 Martinsried, Germany.
Wolfgang BaumeisterDepartment of Molecular Structural Biology, Max Planck Institute of Biochemistry, 82152 Martinsried, Germany.
Till RudackBiospectroscopy, Center for Protein Diagnostics (PRODI), Ruhr University Bochum, 44801 Bochum, Germany; Department of Biophysics, Faculty of Biology & Biotechnology, Ruhr University Bochum, 44780 Bochum, Germany.
Wataru SakamotoInstitute of Plant Science and Resources, Okayama University, Kurashiki, Okayama 710-0046, Japan.
Jörg NickelsenDepartment of Molecular Plant Sciences, LMU Munich, 82152 Martinsried, Germany.
Jan M SchullerSYNMIKRO Research Center and Department of Chemistry, Philipps-University Marburg, 35032 Marburg, Germany. Electronic address: jan.schuller@synmikro.uni-marburg.de.
Michael SchrodaMolecular Biotechnology and Systems Biology, Technische Universität Kaiserslautern, 67663 Kaiserslautern, Germany. Electronic address: schroda@bio.uni-kl.de.
Benjamin D EngelDepartment of Molecular Structural Biology, Max Planck Institute of Biochemistry, 82152 Martinsried, Germany; Helmholtz Pioneer Campus, Helmholtz Zentrum München, 85764 Neuherberg, Germany; Department of Chemistry, Technical University of Munich, 85748 Garching, Germany. Electronic address: ben.engel@helmholtz-muenchen.de.
Max Planck Institute of Biochemistry · DEUniversity of Kaiserslautern · DELudwig-Maximilians-Universität München · DEHelmholtz Zentrum München · DEOkayama University · JPLoewe Center for Synthetic Microbiology · DEMcGill University · CARuhr University Bochum · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Vesicle-inducing protein in plastids 1 (VIPP1) is essential for the biogenesis and maintenance of thylakoid membranes, which transform light into life. However, it is unknown how VIPP1 performs its vital membrane-remodeling functions. Here, we use cryo-electron microscopy to determine structures of cyanobacterial VIPP1 rings, revealing how VIPP1 monomers flex and interweave to form basket-like assemblies of different symmetries. Three VIPP1 monomers together coordinate a non-canonical nucleotide binding pocket on one end of the ring. Inside the ring's lumen, amphipathic helices from each monomer align to form large hydrophobic columns, enabling VIPP1 to bind and curve membranes. In vivo mutations in these hydrophobic surfaces cause extreme thylakoid swelling under high light, indicating an essential role of VIPP1 lipid binding in resisting stress-induced damage. Using cryo-correlative light and electron microscopy (cryo-CLEM), we observe oligomeric VIPP1 coats encapsulating membrane tubules within the Chlamydomonas chloroplast. Our work provides a structural foundation for understanding how VIPP1 directs thylakoid biogenesis and maintenance.

Indexed as

Protein MultimerizationAmino Acid SequenceBacterial ProteinsBinding SitesCell MembraneChlamydomonasCryoelectron MicroscopyGreen Fluorescent ProteinsHydrophobic and Hydrophilic InteractionsLightLipidsModels, MolecularNucleotidesProtein BindingProtein Structure, SecondaryStress, PhysiologicalBacterial ProteinsGreen Fluorescent ProteinsLipidsNucleotidesChlamydomonasCLEMcryo-electron tomographycryo-EMESCRT-IIImembrane remodelingnucleotide hydrolysisphotosynthesisstress responseSynechocystisthylakoid biogenesis

Identifiers

PMID34166613
OpenAlexW3177379102

What OpenQuestion holds

Textmetadata
Read underepoch 390

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.