Evidence map›Paper›PMID 21620704›Full record

ArticleCurrent biology : CB2011

Characterization of dip1p reveals a switch in Arp2/3-dependent actin assembly for fission yeast endocytosis.

Roshni Basu, Fred Chang

Open access · bronzeAbstract read
In one paragraph

Article in Current biology : CB, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.

0numbers the graph read from it
0cells of the map it votes in
39citing papers in PubMed
1.9field-weighted citation impact, top 16% 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

39 citing papers in PubMed, 66 citations in OpenAlex.

  1. Article
  2. Article
  3. Arp2/3-mediated bidirectional actin assembly by SPIN90 dimers.Nature structural & molecular biology · 2025
    Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. A CIE change in our understanding of endocytic mechanisms.Frontiers in cell and developmental biology · 2023
    Review
  9. Article
  10. Article
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  13. Article
  14. Article
  15. TheJournal of cell science · 2019
    Article
  16. Article
  17. Article
  18. Discovery of functional interactions among actin regulators by analysis of image fluctuations in an unperturbed motile cell system.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2018
    Review
  19. Article
  20. 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

2 authors at 1 institution in 1 country.

Roshni BasuDepartment of Microbiology & Immunology, Columbia University College of Physicians and Surgeons, New York, NY 10032, USA.
Fred Chang
Columbia University · US

Funding

ASSEMBLY AND PLACEMENT OF THE CELL DIVISION RINGR01GM056836 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI CHANG, FRED · 1998 to 2018
$7.4M
Nuclear Positioning and Microtubule OrganizationR01GM069670 · NIGMS · COLUMBIA UNIVERSITY HEALTH SCIENCES · PI CHANG, FRED · 2005 to 2012
$2.4M
NIGMS NIH HHS GM056836NIGMS NIH HHS GM069670NIGMS NIH HHS R01 GM056836NIGMS NIH HHS R01 GM069670
6 · The paper itself

Abstract

backgroundDuring endocytosis in yeast, a choreographed series of discrete local events at the plasma membrane lead to a rapid burst of actin polymerization and the subsequent internalization of an endocytic vesicle. What initiates Arp2/3-dependent actin polymerization in this process is not well understood.

resultsThe Schizosaccharomyces pombe WISH/DIP/SPIN90 ortholog dip1p is an actin-patch protein that regulates the temporal sequence of endocytic events. dip1Δ mutants exhibit a novel phenotype in which early events such as WASp localization occur normally but arrival of Arp2/3, actin polymerization, and subsequent steps are delayed and occur with apparently random timing. In studying this mutant, we demonstrate that positive feedback loops of WASp, rapid actin assembly, and Arp2/3 contribute to switch-like behavior that initiates actin polymerization. In the absence of dip1p, a subset of patches is activated concurrently with the "touch" of a neighboring endocytic vesicle.

conclusionsThese studies reveal a switch-like mechanism responsible for the initiation of actin assembly during endocytosis. This switch may be activated in at least two ways, through a dip1p-dependent mechanism and through contact with another endocytic vesicle.

Indexed as

Actin-Related Protein 2-3 ComplexActinsCell Cycle ProteinsEndocytosisForminsMicrofilament ProteinsPolymerizationSchizosaccharomycesSchizosaccharomyces pombe ProteinsActin-Related Protein 2-3 ComplexActinsCell Cycle ProteinsFOR3 protein, S pombeForminsMicrofilament ProteinsSchizosaccharomyces pombe ProteinsWsp1 protein, S pombe

Identifiers

PMID21620704
PMCPMC3121306
OpenAlexW2051593576

What Socratic holds

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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.