Evidence map›Paper›PMID 18347067›Full record

ArticleThe Journal of cell biology2008

Distinct acto/myosin-I structures associate with endocytic profiles at the plasma membrane.

Fatima-Zahra Idrissi, Helga Grötsch, Isabel M Fernández-Golbano, Cristina Presciatto-Baschong, Howard Riezman, María-Isabel Geli

Abstract read
In one paragraph

Article in The Journal of cell biology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 80 papers.

0numbers the graph read from it
0cells of the map it votes in
80citing 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

80 citing papers in PubMed.

  1. The 50-nm Free Vesicles Visible inCurrent issues in molecular biology · 2025
    Article
  2. Article
  3. Article
  4. Review
  5. Endocytic myosin-1 is a force-insensitive, power-generating motor.bioRxiv : the preprint server for biology · 2023
    Article
  6. Self-organizing actin networks drive sequential endocytic protein recruitment and vesicle release on synthetic lipid bilayers.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  7. Article
  8. Article
  9. Load adaptation by endocytic actin networks.Molecular biology of the cell · 2022
    Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. TheJournal of cell science · 2019
    Article
  17. Article
  18. Review
  19. Article
  20. Article

20 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

6 authors.

Fatima-Zahra IdrissiInstituto de Biología Molecular de Barcelona, Consejo Superior de Investigaciones Científicas, 08028 Barcelona, Spain.
Helga Grötsch
Isabel M Fernández-Golbano
Cristina Presciatto-Baschong
Howard Riezman
María-Isabel Geli

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Endocytosis in yeast requires actin and clathrin. Live cell imaging has previously shown that massive actin polymerization occurs concomitant with a slow 200-nm inward movement of the endocytic coat (Kaksonen, M., Y. Sun, and D.G. Drubin. 2003. Cell. 115:475-487). However, the nature of the primary endocytic profile in yeast and how clathrin and actin cooperate to generate an endocytic vesicle is unknown. In this study, we analyze the distribution of nine different proteins involved in endocytic uptake along plasma membrane invaginations using immunoelectron microscopy. We find that the primary endocytic profiles are tubular invaginations of up to 50 nm in diameter and 180 nm in length, which accumulate the endocytic coat components at the tip. Interestingly, significant actin labeling is only observed on invaginations longer than 50 nm, suggesting that initial membrane bending occurs before initiation of the slow inward movement. We also find that in the longest profiles, actin and the myosin-I Myo5p form two distinct structures that might be implicated in vesicle fission.

Indexed as

Actin CytoskeletonActinsCell MembraneCytoskeletonEndocytosisMicroscopy, ImmunoelectronMyosin Type IProtein TransportSaccharomyces cerevisiaeTransport VesiclesActinsMyosin Type I

Identifiers

PMID18347067
PMCPMC2290847

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Registered trials

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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.