Evidence map›Paper›PMID 37966720›Full record

ArticleThe Journal of cell biology2024

Mechanism of actin capping protein recruitment and turnover during clathrin-mediated endocytosis.

Andrew K Lamb, Andres N Fernandez, Abdunaser Eadaim, Katelyn Johnson, Santiago M Di Pietro

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.

0numbers the graph read from it
0cells of the map it votes in
7citing papers in PubMed
1.9field-weighted citation impact, top 15% 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

7 citing papers in PubMed, 9 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Regulation of actin dynamics by Twinfilin.Current opinion in cell biology · 2025
    Review
  5. Article
  6. Review
  7. 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

5 authors at 1 institution in 1 country.

Andrew K LambDepartment of Biochemistry and Molecular Biology, Colorado State University, Fort Collins, CO, USA.ORCID 0000-0003-4495-1003
Andres N FernandezDepartment of Biochemistry and Molecular Biology, Colorado State University, Fort Collins, CO, USA.ORCID 0000-0001-8006-1724
Abdunaser EadaimDepartment of Biochemistry and Molecular Biology, Colorado State University, Fort Collins, CO, USA.ORCID 0009-0008-1649-1277
Katelyn JohnsonDepartment of Biochemistry and Molecular Biology, Colorado State University, Fort Collins, CO, USA.ORCID 0009-0008-4058-3534
Santiago M Di PietroDepartment of Biochemistry and Molecular Biology, Colorado State University, Fort Collins, CO, USA.ORCID 0000-0002-3372-8757
Colorado State University · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Clathrin-mediated endocytosis depends on polymerization of a branched actin network to provide force for membrane invagination. A key regulator in branched actin network formation is actin capping protein (CP), which binds to the barbed end of actin filaments to prevent the addition or loss of actin subunits. CP was thought to stochastically bind actin filaments, but recent evidence shows CP is regulated by a group of proteins containing CP-interacting (CPI) motifs. Importantly, how CPI motif proteins function together to regulate CP is poorly understood. Here, we show Aim21 and Bsp1 work synergistically to recruit CP to the endocytic actin network in budding yeast through their CPI motifs, which also allosterically modulate capping strength. In contrast, twinfilin works downstream of CP recruitment, regulating the turnover of CP through its CPI motif and a non-allosteric mechanism. Collectively, our findings reveal how three CPI motif proteins work together to regulate CP in a stepwise fashion during endocytosis.

Indexed as

Actin Capping ProteinsActinsEndocytosisSaccharomyces cerevisiae ProteinsActin CytoskeletonAdaptor Proteins, Vesicular TransportClathrinCytoskeletal ProteinsSaccharomyces cerevisiaeActin Capping ProteinsActinsAdaptor Proteins, Vesicular TransportAIM21 protein, S cerevisiaeBsp1 protein, S cerevisiaeClathrinCytoskeletal ProteinsSaccharomyces cerevisiae Proteins

Identifiers

PMID37966720
PMCPMC10651396
OpenAlexW4388697708

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.