Evidence map›Paper›PMID 32075907›Full record

ArticleThe Journal of biological chemistry2020

Competition for delivery of profilin-actin to barbed ends limits the rate of formin-mediated actin filament elongation.

Mark E Zweifel, Naomi Courtemanche

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing 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

19 citing papers in PubMed, 28 citations in OpenAlex.

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  19. Profilin choreographs actin and microtubules in cells and cancer.International review of cell and molecular biology · 2020
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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

2 authors at 1 institution in 1 country.

Mark E ZweifelDepartment of Genetics, Cell Biology and Development, University of Minnesota, Minneapolis, Minnesota 55455.
Naomi CourtemancheDepartment of Genetics, Cell Biology and Development, University of Minnesota, Minneapolis, Minnesota 55455 ncourtem@umn.edu.ORCID 0000-0003-4374-4782
University of Minnesota · US

Funding

TRAINING PROGRAM IN MUSCLE RESEARCHT32AR007612 · NIAMS · UNIVERSITY OF MINNESOTA TWIN CITIES · PI JAMES M ERVASTI, DAWN A LOWE · 2001 to 2026
$11.3M
Molecular mechanisms of bundled actin structure assembly by forminsR01GM122787 · NIGMS · UNIVERSITY OF MINNESOTA · PI Naomi Courtemanche · 2017 to 2026
$2.7M
NIAMS NIH HHS T32 AR007612NIGMS NIH HHS R01 GM122787
6 · The paper itself

Abstract

Formins direct the elongation of unbranched actin filaments by binding their barbed ends and processively stepping onto incoming actin monomers to incorporate them into the filament. Binding of profilin to actin monomers creates profilin-actin complexes, which then bind polyproline tracts located in formin homology 1 (FH1) domains. Diffusion of these natively disordered domains enables direct delivery of profilin-actin to the barbed end, speeding the rate of filament elongation. In this study, we investigated the mechanism of coordinated actin delivery from the multiple polyproline tracts in formin FH1 domains. We found that each polyproline tract can efficiently mediate polymerization, but that all tracts do not generate the same rate of elongation. In WT FH1 domains, the multiple polyproline tracts compete to deliver profilin-actin to the barbed end. This competition ultimately limits the rate of formin-mediated elongation. We propose that intrinsic properties of the filament-binding FH2 domain tune the efficiency of FH1-mediated elongation by directly regulating the rate of monomer incorporation at the barbed end. A strong correlation between competitive FH1-mediated profilin-actin delivery and FH2-regulated gating of the barbed end effectively limits the elongation rate, thereby obviating the need for evolutionary optimization of FH1 domain sequences.

Indexed as

Actin CytoskeletonActinsAmino Acid SequenceAnimalsCell Cycle ProteinsChickensCytoskeletal ProteinsMicrofilament ProteinsMicroscopy, FluorescenceMutagenesisPeptidesProfilinsProtein DomainsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsTime-Lapse ImagingActinsBni1 protein, S cerevisiaeCDC12 protein, S cerevisiaeCell Cycle ProteinsCytoskeletal ProteinsMicrofilament ProteinsPeptidespolyprolineProfilinsSaccharomyces cerevisiae Proteinsactinfluorescenceforminmicroscopypolyproline tractprofilin

Identifiers

PMID32075907
PMCPMC7135983
OpenAlexW3007996606

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.