Evidence map›Paper›PMID 39405356›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2024

A role for cross-linking proteins in actin filament network organization and force generation.

Jennifer M Hill, Songlin Cai, Michael D Carver, David G Drubin

Abstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing 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

3 citing papers in PubMed.

  1. Article
  2. Review
  3. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

4 authors.

Jennifer M HillDepartment of Molecular and Cell Biology, University of California, Berkeley, CA 94720.ORCID 0009-0003-5065-6980
Songlin CaiDepartment of Molecular and Cell Biology, University of California, Berkeley, CA 94720.ORCID 0009-0002-8114-549X
Michael D CarverDepartment of Molecular and Cell Biology, University of California, Berkeley, CA 94720.ORCID 0000-0002-4336-9516
David G DrubinDepartment of Molecular and Cell Biology, University of California, Berkeley, CA 94720.ORCID 0000-0003-3002-6271

Funding

Nikon confocal system for improved spatio-dynamic analysis of endocytic trafficking eventsR35GM118149 · NIGMS · UNIVERSITY OF CALIFORNIA BERKELEY · PI DAVID G DRUBIN · 2016 to 2026
$12.0M
HHS | National Institutes of Health (NIH) R35GM118149NIGMS NIH HHS R35 GM118149
6 · The paper itself

Abstract

The high turgor pressure across the plasma membrane of yeasts creates a requirement for substantial force production by actin polymerization and myosin motor activity for clathrin-mediated endocytosis (CME). Endocytic internalization is severely impeded in the absence of fimbrin, an actin filament crosslinking protein called Sac6 in budding yeast. Here, we combine live-cell imaging and mathematical modeling to gain insights into the role of actin filament crosslinking proteins in force generation. Genetic manipulation showed that CME sites with more crosslinking proteins are more effective at internalization under high load. Simulations of an experimentally constrained, agent-based mathematical model recapitulate the result that endocytic networks with more double-bound fimbrin molecules internalize the plasma membrane against elevated turgor pressure more effectively. Networks with large numbers of crosslinks also have more growing actin filament barbed ends at the plasma membrane, where the addition of new actin monomers contributes to force generation and vesicle internalization. Our results provide a richer understanding of the crucial role played by actin filament crosslinking proteins during actin network force generation, highlighting the contribution of these proteins to the self-organization of the actin filament network and force generation under increased load.

Indexed as

Actin CytoskeletonEndocytosisMicrofilament ProteinsActinsCell MembraneClathrinMembrane GlycoproteinsModels, BiologicalSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsActinsClathrinMembrane GlycoproteinsMicrofilament ProteinsplastinSaccharomyces cerevisiae Proteinsactinclathrin-mediated endocytosiscrosslinking proteinsmathematical modeling

Identifiers

PMID39405356
PMCPMC11513903

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.