Evidence map›Paper›PMID 22949647›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2012

Ultrastructural dynamics of proteins involved in endocytic budding.

Fatima-Zahra Idrissi, Anabel Blasco, Anna Espinal, María Isabel Geli

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 55 papers.

0numbers the graph read from it
0cells of the map it votes in
55citing papers in PubMed
3.5field-weighted citation impact, top 7% 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

55 citing papers in PubMed, 82 citations in OpenAlex.

  1. Article
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  6. Article
  7. Endocytic myosin-1 is a force-insensitive, power-generating motor.bioRxiv : the preprint server for biology · 2023
    Article
  8. Article
  9. Regulation of membrane scission in yeast endocytosis.Molecular biology of the cell · 2022
    Article
  10. Load adaptation by endocytic actin networks.Molecular biology of the cell · 2022
    Article
  11. Endocytic proteins with prion-like domains form viscoelastic condensates that enable membrane remodeling.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  12. Article
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  16. Review
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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

4 authors at 2 institutions in 1 country.

Fatima-Zahra IdrissiDepartment of Cell Biology, Instituto de Biología Molecular de Barcelona (CSIC), 08028 Barcelona, Spain.
Anabel Blasco
Anna Espinal
María Isabel Geli
Institut de Biologia Molecular de Barcelona · ESUniversitat Autònoma de Barcelona · ES

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Fluorescence live-cell imaging has temporally resolved the conserved choreography of more than 30 proteins involved in clathrin and actin-mediated endocytic budding from the plasma membrane. However, the resolution of these studies is insufficient to unveil how the endocytic machinery actually drives membrane deformation in vivo. In this study, we use quantitative immuno-EM to introduce the temporal dimension to the ultrastructural analysis of membrane budding and define changes in the topography of the lipid bilayer coupled to the dynamics of endocytic proteins with unprecedented spatiotemporal resolution. Using this approach, we frame the emergence of membrane curvature with respect to the recruitment of endocytic factors and show that constriction of the invaginations correlates with translocation of membrane-sculpting proteins. Furthermore, we show that initial bending of the plasma membrane is independent of actin and clathrin polymerization and precedes building of an actin cap branched by the Arp2/3 complex. Finally, our data indicate that constriction and additional elongation of the endocytic profiles require the mechanochemical activity of the myosins-I. Altogether, this work provides major insights into the molecular mechanisms driving membrane deformation in a cellular context.

Indexed as

Actin-Related Protein 2-3 ComplexCell MembraneEndocytosisMyosin Type ISaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsActin-Related Protein 2-3 ComplexMyosin Type ISaccharomyces cerevisiae Proteins

Identifiers

PMID22949647
PMCPMC3465411
OpenAlexW2061306397

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.