Evidence map›Paper›PMID 21885283›Full record

ArticleCurrent biology : CB2011

Distinct roles for F-BAR proteins Cdc15p and Bzz1p in actin polymerization at sites of endocytosis in fission yeast.

Rajesh Arasada, Thomas D Pollard

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 64 papers.

0numbers the graph read from it
0cells of the map it votes in
64citing papers in PubMed
3.1field-weighted citation impact, top 8% 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

64 citing papers in PubMed, 97 citations in OpenAlex.

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

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.

Rajesh ArasadaDepartment of Molecular, Cellular and Developmental Biology, Yale University, New Haven, CT 06520-8103, USA.
Thomas D Pollard
Yale University · US

Funding

MOLECULAR MECHANISMS OF CELLULAR MOTILITYR01GM026338 · NIGMS · YALE UNIVERSITY · PI POLLARD, THOMAS D. · 1985 to 2020
$9.8M
Mechanism of cytokinesis in fission yeastR01GM026132 · NIGMS · YALE UNIVERSITY · PI POLLARD, THOMAS D. · 1985 to 2021
$8.8M
ACTIN-MYOSIN INTERACTIONS IN CELL MOTILITYR37GM026132 · NIGMS · SALK INSTITUTE FOR BIOLOGICAL STUDIES · PI POLLARD, THOMAS D. · 1988 to 1997
–
NIGMS NIH HHS GM-026132NIGMS NIH HHS GM-026338NIGMS NIH HHS R01 GM026132NIGMS NIH HHS R01 GM026338NIGMS NIH HHS R37 GM026132
6 · The paper itself

Abstract

backgroundGenetic analyses of budding and fission yeast identified >50 proteins that assemble at sites of clathrin-mediated endocytosis in structures called actin patches. These proteins include clathrin, clathrin-interacting proteins, actin binding proteins, and peripheral membrane proteins such as F-BAR proteins. Many questions remain regarding the interactions of these proteins, particularly the participation of F-BAR proteins in the assembly of actin filaments.

resultsOur microscopic and genetic interaction experiments on fission yeast show that F-BAR proteins Cdc15p and Bzz1p accumulate in two distinct zones on invaginating membrane tubules and interact with Myo1p and Wsp1p, nucleation-promoting factors for Arp2/3 complex. The two F-BAR proteins peak prior to movement of the actin patch and their accumulation in actin patches depends on the nucleation-promoting factors. At their peak local concentrations, we estimated the stoichiometries of the proteins in actin patches to be one Bzz1p per two Wsp1p and one Cdc15p per Myo1p. Purified Bzz1p has two SH3 domains that interact with Wsp1p and stimulate actin polymerization by Arp2/3 complex. Cells lacking either Cdc15p or Bzz1p assemble 3- to 5-fold less actin in patches (in spite of normal levels of Wsp1p, Myo1p, and Arp2/3 complex), and patches move shorter distances from the plasma membrane.

conclusionWe propose that during clathrin-mediated endocytosis, F-BAR proteins interact with nucleation-promoting factors to stimulate Arp2/3 complex in two different zones along the invaginating tubule. We further propose that polymerization of actin filaments in these two zones contributes to membrane scission.

Indexed as

Actin-Related Protein 2-3 ComplexActinsCell Cycle ProteinsCell MembraneClathrinCytoskeletonEndocytosisFungal ProteinsGTP-Binding ProteinsMicrofilament ProteinsMyosin Heavy ChainsPolymerizationSchizosaccharomycesSchizosaccharomyces pombe ProteinsActin-Related Protein 2-3 ComplexActinsBzz1 protein, S pombeCDC15 proteinCell Cycle ProteinsClathrinFungal ProteinsGTP-Binding ProteinsMicrofilament Proteinsmyo1 protein, S pombeMyosin Heavy ChainsSchizosaccharomyces pombe ProteinsWsp1 protein, S pombe

Identifiers

PMID21885283
PMCPMC3350781
OpenAlexW2090195270

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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.