Evidence map›Paper›PMID 21839918›Full record

ArticleDevelopmental cell2011

The myosin passenger protein Smy1 controls actin cable structure and dynamics by acting as a formin damper.

Melissa Chesarone-Cataldo, Christophe Guérin, Jerry H Yu, Roland Wedlich-Soldner, Laurent Blanchoin, Bruce L Goode

Open access · bronzeAbstract read
In one paragraph

Article in Developmental cell, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 papers.

0numbers the graph read from it
0cells of the map it votes in
41citing 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

41 citing papers in PubMed, 63 citations in OpenAlex.

  1. Article
  2. Length control emerges from cytoskeletal network geometry.Proceedings of the National Academy of Sciences of the United States of America · 2024
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  3. Article
  4. Length control emerges from cytoskeletal network geometry.bioRxiv : the preprint server for biology · 2023
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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

6 authors at 3 institutions in 3 countries.

Melissa Chesarone-CataldoDepartment of Biology and Rosenstiel Basic Medical Science Research Center, Brandeis University, Waltham, MA 02454, USA.
Christophe Guérin
Jerry H Yu
Roland Wedlich-Soldner
Laurent Blanchoin
Bruce L Goode
Brandeis University · USInstitut National de la Recherche Agronomique · MAMax Planck Society · DE

Funding

Regulation of formins and cell polarity in yeastR01GM083137 · NIGMS · BRANDEIS UNIVERSITY · PI GOODE, BRUCE L · 2008 to 2019
$4.3M
NIGMS NIH HHS GM083137NIGMS NIH HHS R01 GM083137
6 · The paper itself

Abstract

Formins are a conserved family of proteins with robust effects in promoting actin nucleation and elongation. However, the mechanisms restraining formin activities in cells to generate actin networks with particular dynamics and architectures are not well understood. In S. cerevisiae, formins assemble actin cables, which serve as tracks for myosin-dependent intracellular transport. Here, we show that the kinesin-like myosin passenger-protein Smy1 interacts with the FH2 domain of the formin Bnr1 to decrease rates of actin filament elongation, which is distinct from the formin displacement activity of Bud14. In vivo analysis of smy1Δ mutants demonstrates that this "damper" mechanism is critical for maintaining proper actin cable architecture, dynamics, and function. We directly observe Smy1-3GFP being transported by myosin V and transiently pausing at the neck in a manner dependent on Bnr1. These observations suggest that Smy1 is part of a negative feedback mechanism that detects cable length and prevents overgrowth.

Indexed as

ActinsCytoskeletal ProteinsDose-Response Relationship, DrugGene Expression RegulationGreen Fluorescent ProteinsMicrofilament ProteinsMolecular Sequence DataMutationMyosin Type VProtein Structure, TertiaryProtein TransportSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsActinsBNR1 protein, S cerevisiaeBud14 protein, S cerevisiaeCytoskeletal ProteinsGreen Fluorescent ProteinsMicrofilament ProteinsMyosin Type VSaccharomyces cerevisiae Proteins

Identifiers

PMID21839918
PMCPMC3157649
OpenAlexW2071012173

What OpenQuestion holds

Textmetadata
LicenceTDM
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.