Evidence map›Paper›PMID 35760780›Full record

ArticleNature communications2022

Molecular mechanics underlying flat-to-round membrane budding in live secretory cells.

Wonchul Shin, Ben Zucker, Nidhi Kundu, Sung Hoon Lee, Bo Shi, Chung Yu Chan, Xiaoli Guo, Jonathan T Harrison, Jaymie Moore Turechek, Jenny E Hinshaw and 2 more

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
1.6field-weighted citation impact, top 17% 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

13 citing papers in PubMed, 20 citations in OpenAlex.

  1. Article
  2. Solvent-Mediated Dewetting Principles for Cell-Sized Liposome Formation.Small (Weinheim an der Bergstrasse, Germany) · 2026
    Article
  3. Article
  4. Membrane Merger Dynamics in Exocytosis and Endocytosis.Advances in experimental medicine and biology · 2026
    Review
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Review
  12. Review
  13. Multiple Roles of Actin in Exo- and Endocytosis.Frontiers in synaptic neuroscience · 2022
    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

12 authors at 4 institutions in 3 countries.

Wonchul Shin *National Institute of Neurological Disorders and Stroke, Bethesda, MD, USA.
Ben Zucker *Department of Physiology and Pharmacology, Sackler Faculty of Medicine, Tel Aviv University, 69978, Ramat Aviv, Israel.ORCID http://orcid.org/0000-0002-1433-9801
Nidhi Kundu *Structural Cell Biology Section, Laboratory of Cell and Molecular Biology, National Institute of Diabetes and Digestive and Kidney Diseases, Bethesda, MD, USA.
Sung Hoon LeeChung-Ang University, 84 Heukseok-ro, Dongjak-gu, Seoul, 06974, Republic of Korea.
Bo ShiNational Institute of Neurological Disorders and Stroke, Bethesda, MD, USA.
Chung Yu ChanNational Institute of Neurological Disorders and Stroke, Bethesda, MD, USA.ORCID http://orcid.org/0000-0001-6726-5087
Xiaoli GuoNational Institute of Neurological Disorders and Stroke, Bethesda, MD, USA.
Jonathan T HarrisonStructural Cell Biology Section, Laboratory of Cell and Molecular Biology, National Institute of Diabetes and Digestive and Kidney Diseases, Bethesda, MD, USA.
Jaymie Moore TurechekNational Institute of Neurological Disorders and Stroke, Bethesda, MD, USA.
Jenny E HinshawStructural Cell Biology Section, Laboratory of Cell and Molecular Biology, National Institute of Diabetes and Digestive and Kidney Diseases, Bethesda, MD, USA. jennyh@niddk.nih.gov.
Michael M KozlovDepartment of Physiology and Pharmacology, Sackler Faculty of Medicine, Tel Aviv University, 69978, Ramat Aviv, Israel. michk@tauex.tau.ac.il.ORCID http://orcid.org/0000-0002-0891-4785
Ling-Gang WuNational Institute of Neurological Disorders and Stroke, Bethesda, MD, USA. wul@ninds.nih.gov.ORCID http://orcid.org/0000-0003-4261-7079
National Institute of Neurological Disorders and Stroke · USNational Institute of Diabetes and Digestive and Kidney Diseases · USTel Aviv University · ILChung-Ang University · KR

Funding

Synaptic Vesicle ExocytosisZIANS003009 · NINDS · NATIONAL INSTITUTE OF NEUROLOGICAL DISORDERS AND STROKE · PI WU, LING GANG · 2009 to 2025
$31.2M
Synaptic Vesicle EndocytosisZIANS003105 · NINDS · NATIONAL INSTITUTE OF NEUROLOGICAL DISORDERS AND STROKE · PI WU, LING GANG · 2009 to 2025
$30.9M
Structure And Function Of Dynamin, A 100kd GTPase Involved In EndocytosisZIADK060100 · NIDDK · NATIONAL INSTITUTE OF DIABETES AND DIGESTIVE AND KIDNEY DISEASES · PI HINSHAW, JENNY E · 2009 to 2025
$10.8M
Synaptic Vesicle Exocytosis and EndocytosisZ01NS003009 · NINDS · NEUROLOGICAL DISORDERS AND STROKE · PI WU, LING GANG · 2004 to 2008
$4.9M
Structure /Function Of Dynamin, A GTPase in EndocytosisZ01DK060100 · NIDDK · NATIONAL INSTITUTE OF DIABETES AND DIGESTIVE AND KIDNEY DISEASES · PI HINSHAW, JENNY E · 1996 to 2008
$657k
Intramural NIH HHS Z01 DK060100Intramural NIH HHS Z01 NS003009Intramural NIH HHS ZIA NS003009Intramural NIH HHS ZIA NS003105
6 · The paper itself

Abstract

Membrane budding entails forces to transform flat membrane into vesicles essential for cell survival. Accumulated studies have identified coat-proteins (e.g., clathrin) as potential budding factors. However, forces mediating many non-coated membrane buddings remain unclear. By visualizing proteins in mediating endocytic budding in live neuroendocrine cells, performing in vitro protein reconstitution and physical modeling, we discovered how non-coated-membrane budding is mediated: actin filaments and dynamin generate a pulling force transforming flat membrane into Λ-shape; subsequently, dynamin helices surround and constrict Λ-profile's base, transforming Λ- to Ω-profile, and then constrict Ω-profile's pore, converting Ω-profiles to vesicles. These mechanisms control budding speed, vesicle size and number, generating diverse endocytic modes differing in these parameters. Their impact is widespread beyond secretory cells, as the unexpectedly powerful functions of dynamin and actin, previously thought to mediate fission and overcome tension, respectively, may contribute to many dynamin/actin-dependent non-coated-membrane buddings, coated-membrane buddings, and other membrane remodeling processes.

Indexed as

ActinsEndocytosisCell MembraneClathrinCoated Pits, Cell-MembraneDynaminsActinsClathrinDynamins

Identifiers

PMID35760780
PMCPMC9237132
OpenAlexW4283707476

What Socratic 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 Socratic graph.