Evidence map›Paper›PMID 30266808›Full record

ArticleThe Journal of biological chemistry2018

Dissection of two parallel pathways for formin-mediated actin filament elongation.

Laura A Sherer, Mark E Zweifel, Naomi Courtemanche

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
0.9field-weighted citation impact, top 28% 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

11 citing papers in PubMed, 14 citations in OpenAlex.

  1. Article
  2. Review
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  11. Profilin choreographs actin and microtubules in cells and cancer.International review of cell and molecular biology · 2020
    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

3 authors at 1 institution in 1 country.

Laura A ShererFrom the Department of Genetics, Cell and Developmental Biology, University of Minnesota, Minneapolis, Minnesota 55455.
Mark E ZweifelFrom the Department of Genetics, Cell and Developmental Biology, University of Minnesota, Minneapolis, Minnesota 55455.
Naomi CourtemancheFrom the Department of Genetics, Cell and Developmental Biology, University of Minnesota, Minneapolis, Minnesota 55455. Electronic address: ncourtem@umn.edu.
University of Minnesota · US

Funding

Molecular mechanisms of bundled actin structure assembly by forminsR01GM122787 · NIGMS · UNIVERSITY OF MINNESOTA · PI Naomi Courtemanche · 2017 to 2026
$2.7M
NIGMS NIH HHS R01 GM122787
6 · The paper itself

Abstract

Formins direct the elongation of unbranched actin filaments that are incorporated into a diverse set of cytoskeletal structures. Elongation of formin-bound filaments occurs along two parallel pathways. The formin homology 2 (FH2) pathway allows actin monomers to bind directly to barbed ends bound by dimeric FH2 domains. The formin homology 1 (FH1) pathway involves transfer of profilin-bound actin to the barbed end from polyproline tracts located in the disordered FH1 domains. Here, we used a total internal reflection fluorescence (TIRF) microscopy-based fluorescence approach to determine the fraction of actin subunits incorporated via the FH1 and FH2 pathways during filament elongation mediated by two formins. We found that the fraction of filament elongation that occurs via each pathway directly depends on the efficiency of the other pathway, indicating that these two pathways compete with each other for subunit addition by formins. We conclude that this competition allows formins to compensate for changes in the efficiency of one pathway by adjusting the frequency of subunit addition via the other, thus increasing the overall robustness of formin-mediated actin polymerization.

Indexed as

ActinsAnimalsCarboxylic AcidsCell Cycle ProteinsChickensCytoskeletal ProteinsFluorescenceFluorescent DyesMicrofilament ProteinsMicroscopy, FluorescenceProfilinsProtein BindingProtein DomainsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSchizosaccharomycesActinsBni1 protein, S cerevisiaeCarboxylic AcidsCdc12 protein, S pombeCDC3 protein, S cerevisiaecdc3 protein, S pombeCell Cycle ProteinsCytoskeletal ProteinsFluorescent DyesMicrofilament ProteinsOregon Green 488 carboxylic acidProfilinsSaccharomyces cerevisiae ProteinsSchizosaccharomyces pombe Proteinsactinactin polymerizationBni1Cdc12cytoskeletonfluorescenceforminformin homology domainprofilinTIRF microscopy

Identifiers

PMID30266808
PMCPMC6240877
OpenAlexW2894067513

What OpenQuestion holds

Textmetadata
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.