Evidence map›Paper›PMID 27866892›Full record

ArticleCurrent biology : CB2016

Tropomyosin and Profilin Cooperate to Promote Formin-Mediated Actin Nucleation and Drive Yeast Actin Cable Assembly.

Salvatore L Alioto, Mikael V Garabedian, Danielle R Bellavance, Bruce L Goode

Open access · bronzeAbstract read
In one paragraph

Article in Current biology : CB, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
2.7field-weighted citation impact, top 9% 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

23 citing papers in PubMed, 28 citations in OpenAlex.

  1. Article
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  5. The sole essential low molecular weight tropomyosin isoform ofbioRxiv : the preprint server for biology · 2024
    Article
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  9. Celebrating 20 years of live single-actin-filament studies with five golden rules.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
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  11. Article
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  13. Genetically inspired in vitro reconstitution ofMolecular biology of the cell · 2020
    Article
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  16. Article
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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 1 institution in 1 country.

Salvatore L AliotoDepartment of Biology, Rosenstiel Basic Medical Science Research Center, Brandeis University, Waltham, MA 02454, USA.
Mikael V GarabedianDepartment of Biology, Rosenstiel Basic Medical Science Research Center, Brandeis University, Waltham, MA 02454, USA.
Danielle R BellavanceDepartment of Biology, Rosenstiel Basic Medical Science Research Center, Brandeis University, Waltham, MA 02454, USA.
Bruce L GoodeDepartment of Biology, Rosenstiel Basic Medical Science Research Center, Brandeis University, Waltham, MA 02454, USA. Electronic address: goode@brandeis.edu.
Brandeis University · US

Funding

Regulation of formins and cell polarity in yeastR01GM083137 · NIGMS · BRANDEIS UNIVERSITY · PI GOODE, BRUCE L · 2008 to 2019
$4.3M
NIGMS NIH HHS R01 GM083137
6 · The paper itself

Abstract

Tropomyosins comprise a large family of actin-binding proteins with critical roles in diverse actin-based processes [1], but our understanding of how they mechanistically contribute to actin filament dynamics has been limited. We addressed this question in S. cerevisiae, where tropomyosins (Tpm1 and Tpm2), profilin (Pfy1), and formins (Bni1 and Bnr1) are required for the assembly of an array of actin cables that facilitate polarized vesicle delivery and daughter cell growth. Formins drive cable formation by promoting actin nucleation and by accelerating actin filament elongation together with profilin [2]. In contrast, how tropomyosins contribute mechanistically to cable formation has been unclear, but genetic studies demonstrate that Tpm1 plays a more important role than Tpm2 [3, 4]. Here, we found that loss of TPM1 in strains lacking BNR1, but not BNI1, leads to severe defects in cable formation, polarized secretion, and cell growth, suggesting that TPM1 function is required for proper Bni1-mediated cable assembly. Furthermore, in vitro total internal reflection fluorescence (TIRF) microscopy demonstrated that Tpm1 strongly enhances Bni1-mediated, but not Bnr1-mediated, actin nucleation without affecting filament elongation rate, whereas Tpm2 has no effects on Bni1 or Bnr1. Tpm1 stimulation of Bni1-mediated nucleation also requires profilin and its interactions with both G-actin and formins. Together, these results demonstrate that yeast Tpm1 works in concert with profilin to promote formin-dependent nucleation of actin cables, thus expanding our understanding of how specific tropomyosin isoforms influence actin dynamics.

Indexed as

Actin CytoskeletonActinsGene Expression Regulation, FungalMicrofilament ProteinsProfilinsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsTropomyosinActinsMicrofilament ProteinsProfilinsSaccharomyces cerevisiae ProteinsTropomyosinactinforminprofilintropomyosinyeast

Identifiers

PMID27866892
PMCPMC5140752
OpenAlexW2551027749

What OpenQuestion holds

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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.