Evidence map›Paper›PMID 32424346›Full record

ArticleNature structural & molecular biology2020

A helical assembly of human ESCRT-I scaffolds reverse-topology membrane scission.

Thomas G Flower, Yoshinori Takahashi, Arpa Hudait, Kevin Rose, Nicholas Tjahjono, Alexander J Pak, Adam L Yokom, Xinwen Liang, Hong-Gang Wang, Fadila Bouamr and 2 more

Abstract read
In one paragraph

Article in Nature structural & molecular biology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 papers.

0numbers the graph read from it
0cells of the map it votes in
41citing 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

41 citing papers in PubMed.

  1. Article
  2. The Human Autophagy Core Complexes.Annual review of biochemistry · 2026
    Review
  3. Review
  4. ESCRT-III function in membrane fission and repair.Nature reviews. Molecular cell biology · 2026
    Review
  5. Article
  6. Review
  7. Article
  8. Article
  9. Article
  10. Review
  11. Article
  12. Article
  13. Article
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  15. Review
  16. Review
  17. Article
  18. Article
  19. Article
  20. Article
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

12 authors.

Thomas G FlowerDepartment of Molecular and Cell Biology and California Institute for Quantitative Biosciences, University of California, Berkeley, Berkeley, CA, USA.ORCID http://orcid.org/0000-0002-7890-6473
Yoshinori TakahashiDepartment of Pediatrics, Pennsylvania State College of Medicine, Hershey, PA, USA.ORCID http://orcid.org/0000-0002-8004-4817
Arpa HudaitDepartment of Chemistry, James Franck Institute, and Institute for Biophysical Dynamics, The University of Chicago, Chicago, IL, USA.ORCID http://orcid.org/0000-0002-4279-4000
Kevin RoseLaboratory of Molecular Microbiology, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, MD, USA.ORCID http://orcid.org/0000-0002-9373-4147
Nicholas TjahjonoDepartment of Molecular and Cell Biology and California Institute for Quantitative Biosciences, University of California, Berkeley, Berkeley, CA, USA.ORCID http://orcid.org/0000-0003-0743-3581
Alexander J PakDepartment of Chemistry, James Franck Institute, and Institute for Biophysical Dynamics, The University of Chicago, Chicago, IL, USA.
Adam L YokomDepartment of Molecular and Cell Biology and California Institute for Quantitative Biosciences, University of California, Berkeley, Berkeley, CA, USA.ORCID http://orcid.org/0000-0002-3746-7961
Xinwen LiangDepartment of Pediatrics, Pennsylvania State College of Medicine, Hershey, PA, USA.
Hong-Gang WangDepartment of Pediatrics, Pennsylvania State College of Medicine, Hershey, PA, USA.
Fadila BouamrLaboratory of Molecular Microbiology, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, MD, USA.
Gregory A VothDepartment of Chemistry, James Franck Institute, and Institute for Biophysical Dynamics, The University of Chicago, Chicago, IL, USA.
James H HurleyDepartment of Molecular and Cell Biology and California Institute for Quantitative Biosciences, University of California, Berkeley, Berkeley, CA, USA. jimhurley@berkeley.edu.ORCID http://orcid.org/0000-0001-5054-5445

Funding

User Training and OutreachP30GM124169 · NIGMS · UNIVERSITY OF CALIF-LAWRENC BERKELEY LAB · PI Jay C. Nix · 2017 to 2026
$28.6M
Virus TransmissionP50AI150464 · NIAID · UNIVERSITY OF UTAH · PI HOPE, THOMAS · 2019 to 2021
$14.9M
Biochemical, Biophysical, and Structural Mechanisms of HIV-1 Budding and ReleaseR37AI112442 · NIAID · UNIVERSITY OF CALIFORNIA BERKELEY · PI James H Hurley · 2019 to 2026
$4.3M
Non-canonical Caspase-8 Activation on Autophagosomal MembranesR01CA222349 · NCI · PENNSYLVANIA STATE UNIV HERSHEY MED CTR · PI HONG-GANG WANG · 2018 to 2026
$3.0M
Autophagosome closure by the ESCRT machineryR01GM127954 · NIGMS · PENNSYLVANIA STATE UNIV HERSHEY MED CTR · PI WANG, HONG-GANG · 2018 to 2025
$2.7M
Eliminating Critical Systematic Errors In Structural Biology With Next-Generation SimulationR01GM124149 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI HOLTON, JAMES M · 2017 to 2024
$2.5M
Biochemical, Biophysical, and Structural Mechanisms of HIV-1 Budding and ReleaseR01AI112442 · NIAID · UNIVERSITY OF CALIFORNIA BERKELEY · PI HURLEY, JAMES H · 2014 to 2018
$2.0M
Structure Analysis of Viral Assembly MechanismsR01GM128507 · NIGMS · UNIVERSITY OF VIRGINIA · PI YEAGER, MARK JAY · 2018 to 2019
$1.5M
Structure Analysis of Viral Assembly MechanismsR01AI150492 · NIAID · UNIVERSITY OF VIRGINIA · PI YEAGER, MARK JAY · 2020 to 2021
$1.2M
Computational Insights into Assembly, Budding, and Maturation during HIV-1 ReplicationF32AI150477 · NIAID · UNIVERSITY OF CHICAGO · PI PAK, ALEXANDER · 2019 to 2019
$64k
NCI NIH HHS R01 CA222349NIAID NIH HHS F32 AI150477NIAID NIH HHS P50 AI150464NIAID NIH HHS R01 AI112442NIAID NIH HHS R01 AI150492NIAID NIH HHS R37 AI112442NIGMS NIH HHS P30 GM124169NIGMS NIH HHS R01 GM124149NIGMS NIH HHS R01 GM127954NIGMS NIH HHS R01 GM128507
6 · The paper itself

Abstract

The ESCRT complexes drive membrane scission in HIV-1 release, autophagosome closure, multivesicular body biogenesis, cytokinesis, and other cell processes. ESCRT-I is the most upstream complex and bridges the system to HIV-1 Gag in virus release. The crystal structure of the headpiece of human ESCRT-I comprising TSG101-VPS28-VPS37B-MVB12A was determined, revealing an ESCRT-I helical assembly with a 12-molecule repeat. Electron microscopy confirmed that ESCRT-I subcomplexes form helical filaments in solution. Mutation of VPS28 helical interface residues blocks filament formation in vitro and autophagosome closure and HIV-1 release in human cells. Coarse-grained (CG) simulations of ESCRT assembly at HIV-1 budding sites suggest that formation of a 12-membered ring of ESCRT-I molecules is a geometry-dependent checkpoint during late stages of Gag assembly and HIV-1 budding and templates ESCRT-III assembly for membrane scission. These data show that ESCRT-I is not merely a bridging adaptor; it has an essential scaffolding and mechanical role in its own right.

Indexed as

Adaptor Proteins, Signal TransducingAmino Acid MotifsAutophagosomesCell MembraneCrystallizationCrystallography, X-RayDNA-Binding ProteinsEndosomal Sorting Complexes Required for Transportgag Gene Products, Human Immunodeficiency VirusHEK293 CellsHIV-1Host-Pathogen InteractionsHumansMolecular Dynamics SimulationPhosphoproteinsProtein ConformationAdaptor Proteins, Signal TransducingDNA-Binding ProteinsEndosomal Sorting Complexes Required for Transportgag Gene Products, Human Immunodeficiency VirusMVB12A protein, humanPhosphoproteinsTranscription FactorsTsg101 Proteinvacuolar protein sorting 37 homolog B, humanVPS28 protein, human

Identifiers

PMID32424346
PMCPMC7339825

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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.