Evidence map›Paper›PMID 32078797›Full record

ArticleBiophysical journal2020

Molecular Simulation of Mechanical Properties and Membrane Activities of the ESCRT-III Complexes.

Taraknath Mandal, Wilson Lough, Saverio E Spagnolie, Anjon Audhya, Qiang Cui

Open access · bronzeAbstract read
In one paragraph

Article in Biophysical journal, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
1.7field-weighted citation impact, top 19% 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

11 citing papers in PubMed, 22 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Molecular mechanism of GTP binding- and dimerization-induced enhancement of Sar1-mediated membrane remodeling.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  6. Article
  7. Molecular Dynamics Simulations of Curved Lipid Membranes.International journal of molecular sciences · 2022
    Review
  8. Article
  9. Article
  10. Mechanisms of negative membrane curvature sensing and generation by ESCRT III subunit Snf7.Protein science : a publication of the Protein Society · 2020
    Article
  11. A Structural View on ESCRT-Mediated Abscission.Frontiers in cell and developmental biology · 2020
    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

5 authors at 3 institutions in 2 countries.

Taraknath MandalDepartment of Chemistry, Boston University, Boston, Massachusetts.
Wilson LoughDepartment of Mathematics.
Saverio E SpagnolieDepartment of Mathematics.
Anjon AudhyaDepartment of Biomolecular Chemistry, University of Wisconsin-Madison, Madison, Wisconsin.
Qiang CuiDepartments of Chemistry, Physics, and Biomedical Engineering, Boston University, Boston, Massachusetts. Electronic address: qiangcui@bu.edu.
Boston University · USToronto Metropolitan University · CAUniversity of Wisconsin–Madison · US

Funding

Molecular mechanisms that regulate vesicle formation and transportR35GM134865 · NIGMS · UNIVERSITY OF WISCONSIN-MADISON · PI Anjon Audhya · 2020 to 2026
$4.8M
NIGMS NIH HHS R35 GM134865
6 · The paper itself

Abstract

The endosomal sorting complex required for transport (ESCRT) machinery carries out the membrane scission reactions that are required for many biological processes throughout cells. How ESCRTs bind and deform cellular membranes and ultimately produce vesicles has been a matter of active research in recent years. In this study, we use fully atomistic molecular dynamics simulations to scrutinize the structural details of a filament composed of Vps32 protomers, a major component of ESCRT-III complexes. The simulations show that both hydrophobic and electrostatic interactions between monomers help maintain the structural stability of the filament, which exhibits an intrinsic bend and twist. Our findings suggest that the accumulation of bending and twisting stresses as the filament elongates on the membrane surface likely contributes to the driving force for membrane invagination. The filament exposes a large cationic surface that senses the negatively charged lipids in the membrane, and the N-terminal amphipathic helix of the monomers not only acts as a membrane anchor but also generates significant positive membrane curvature. Taking all results together, we discuss a plausible mechanism for membrane invagination driven by ESCRT-III.

Indexed as

EndocytosisEndosomal Sorting Complexes Required for TransportBiological TransportCell MembraneProtein TransportEndosomal Sorting Complexes Required for Transport

Identifiers

PMID32078797
PMCPMC7091516
OpenAlexW3005007698

What OpenQuestion holds

Textmetadata
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.