Evidence map›Paper›PMID 31346091›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2019

Mechanical and kinetic factors drive sorting of F-actin cross-linkers on bundles.

Simon L Freedman, Cristian Suarez, Jonathan D Winkelman, David R Kovar, Gregory A Voth, Aaron R Dinner, Glen M Hocky

Abstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
–field-weighted citation impact
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

24 citing papers in PubMed.

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  17. Molecular Paradigms for Biological Mechanosensing.The journal of physical chemistry. B · 2021
    Article
  18. Article
  19. Article
  20. A strong nonequilibrium bound for sorting of cross-linkers on growing biopolymers.Proceedings of the National Academy of Sciences of the United States of America · 2021
    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

7 authors.

Simon L FreedmanDepartment of Engineering Sciences and Applied Mathematics, Northwestern University, Evanston, IL 60201.ORCID 0000-0001-6583-6683
Cristian SuarezDepartment of Molecular Genetics and Cell Biology, University of Chicago, Chicago, IL 60637.
Jonathan D WinkelmanDepartment of Physics, University of Chicago, Chicago, IL 60637.
David R KovarDepartment of Molecular Genetics and Cell Biology, University of Chicago, Chicago, IL 60637.
Gregory A VothJames Franck Institute, University of Chicago, Chicago, IL 60637.
Aaron R DinnerJames Franck Institute, University of Chicago, Chicago, IL 60637; dinner@uchicago.edu hockyg@nyu.edu.ORCID 0000-0001-8328-6427
Glen M HockyDepartment of Chemistry, New York University, New York, NY 10012 dinner@uchicago.edu hockyg@nyu.edu.ORCID 0000-0002-5637-0698

Funding

Mechanosensing in LIM Domain ProteinsF32GM122372 · NIGMS · UNIVERSITY OF CHICAGO · PI WINKELMAN, JONATHAN DAVID · 2017 to 2019
$179k
NIGMS NIH HHS F32 GM122372
6 · The paper itself

Abstract

In cells, actin-binding proteins (ABPs) sort to different regions to establish F-actin networks with diverse functions, including filopodia used for cell migration and contractile rings required for cell division. Recent experimental work uncovered a competition-based mechanism that may facilitate spatial localization of ABPs: binding of a short cross-linker protein to 2 actin filaments promotes the binding of other short cross-linkers and inhibits the binding of longer cross-linkers (and vice versa). We hypothesize this sorting arises because F-actin is semiflexible and cannot bend over short distances. We develop a mathematical theory and lattice models encompassing the most important physical parameters for this process and use coarse-grained simulations with explicit cross-linkers to characterize and test our predictions. Our theory and data predict an explicit dependence of cross-linker separation on bundle polymerization rate. We perform experiments that confirm this dependence, but with an unexpected cross-over in dominance of one cross-linker at high growth rates to the other at slow growth rates, and we investigate the origin of this cross-over with further simulations. The nonequilibrium mechanism that we describe can allow cells to organize molecular material to drive biological processes, and our results can guide the choice and design of cross-linkers for engineered protein-based materials.

Indexed as

Models, TheoreticalActin CytoskeletonActininActinsAnimalsCarrier ProteinsCell DivisionCell MovementKineticsMicrofilament ProteinsProtein BindingProtein TransportPseudopodiaActininActinsCarrier ProteinsMicrofilament Proteinscytoskeletonfascinmodelingsortingα-actinin

Identifiers

PMID31346091
PMCPMC6697872

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.