Evidence map›Paper›PMID 39185238›Full record

ArticlebioRxiv : the preprint server for biology2024

Myosin forces elicit an F-actin structural landscape that mediates mechanosensitive protein recognition.

Ayala G Carl, Matthew J Reynolds, Pinar S Gurel, Donovan Y Z Phua, Xiaoyu Sun, Lin Mei, Keith Hamilton, Yasuharu Takagi, Alex J Noble, James R Sellers and 1 more

Abstract readPreprint
In one paragraph

Article in bioRxiv : the preprint server for biology, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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

0 citing papers in PubMed.

No citing paper in PubMed yet.

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

11 authors.

Ayala G CarlLaboratory of Structural Biophysics and Mechanobiology, The Rockefeller University, New York, NY, USA.
Matthew J ReynoldsLaboratory of Structural Biophysics and Mechanobiology, The Rockefeller University, New York, NY, USA.ORCID 0000-0002-2501-9280
Pinar S GurelLaboratory of Structural Biophysics and Mechanobiology, The Rockefeller University, New York, NY, USA.ORCID 0000-0003-1956-2591
Donovan Y Z PhuaLaboratory of Structural Biophysics and Mechanobiology, The Rockefeller University, New York, NY, USA.ORCID 0000-0002-5520-3732
Xiaoyu SunLaboratory of Structural Biophysics and Mechanobiology, The Rockefeller University, New York, NY, USA.
Lin MeiLaboratory of Structural Biophysics and Mechanobiology, The Rockefeller University, New York, NY, USA.ORCID 0000-0002-5056-4547
Keith HamiltonLaboratory of Structural Biophysics and Mechanobiology, The Rockefeller University, New York, NY, USA.
Yasuharu TakagiLaboratory of Molecular Physiology, Cell and Developmental Biology Center, National Heart, Lung, and Blood Institute, NIH, Bethesda, MD, USA.
Alex J NobleSimons Electron Microscopy Center, New York Structural Biology Center, New York, NY, USA.ORCID 0000-0001-8634-2279
James R SellersLaboratory of Molecular Physiology, Cell and Developmental Biology Center, National Heart, Lung, and Blood Institute, NIH, Bethesda, MD, USA.
Gregory M AlushinLaboratory of Structural Biophysics and Mechanobiology, The Rockefeller University, New York, NY, USA.ORCID 0000-0001-7250-4484

Funding

Mechanosensing Via Cytoskeletal StrainDP5OD017885 · OD · ROCKEFELLER UNIVERSITY · PI ALUSHIN, GREGORY M · 2016 to 2019
$1.7M
Structural Mechanisms of Cytoskeletal Force-SensingR01GM141044 · NIGMS · ROCKEFELLER UNIVERSITY · PI ALUSHIN, GREGORY M · 2021 to 2024
$1.5M
EXPRESSION STUDIES OF OTHER UNCONVENTIONAL MYOSINSZ01HL004232 · NHLBI · NATIONAL HEART, LUNG, AND BLOOD INSTITUTE · PI SELLERS, JAMES R. · 2000 to 2008
$1.2M
Tri-Institutional PhD Program in Chemical BiologyT32GM115327 · NIGMS · WEILL MEDICAL COLL OF CORNELL UNIV · PI TAN, DEREK S · 2015 to 2019
$741k
THE ROLE OF CTGF IN SUBEPITHELIAL FIBROSIS IN ASTHMAK08HL004232 · NHLBI · BOSTON UNIVERSITY MEDICAL CAMPUS · PI RISHIKOF, DAVID C · 2000 to 2004
$625k
Structural Studies of Type II Cadherins on Membranes by Cryo-Electron TomographyF32GM128303 · NIGMS · NEW YORK STRUCTURAL BIOLOGY CENTER · PI NOBLE, ALEX JAMES · 2018 to 2019
$120k
Structural and Molecular Mechanisms of Stress Fiber RepairF31HL165906 · NHLBI · ROCKEFELLER UNIVERSITY · PI PHUA, DONOVAN YONG ZHI · 2022 to 2023
$94k
Intramural NIH HHS Z01 HL004232NHLBI NIH HHS F31 HL165906NHLBI NIH HHS K08 HL004232NIGMS NIH HHS F32 GM128303NIGMS NIH HHS R01 GM141044NIGMS NIH HHS T32 GM115327NIH HHS DP5 OD017885
6 · The paper itself

Abstract

Cells mechanically interface with their surroundings through cytoskeleton-linked adhesions, allowing them to sense physical cues that instruct development and drive diseases such as cancer. Contractile forces generated by myosin motor proteins mediate these mechanical signal transduction processes through unclear protein structural mechanisms. Here, we show that myosin forces elicit structural changes in actin filaments (F-actin) that modulate binding by the mechanosensitive adhesion protein α-catenin. Using correlative cryo-fluorescence microscopy and cryo-electron tomography, we identify F-actin featuring domains of nanoscale oscillating curvature at cytoskeleton-adhesion interfaces enriched in zyxin, a marker of actin-myosin generated traction forces. We next introduce a reconstitution system for visualizing F-actin in the presence of myosin forces with cryo-electron microscopy, which reveals morphologically similar superhelical F-actin spirals. In simulations, transient forces mimicking tugging and release of filaments by motors produce spirals, supporting a mechanistic link to myosin's ATPase mechanochemical cycle. Three-dimensional reconstruction of spirals uncovers extensive asymmetric remodeling of F-actin's helical lattice. This is recognized by α-catenin, which cooperatively binds along individual strands, preferentially engaging interfaces featuring extended inter-subunit distances while simultaneously suppressing rotational deviations to regularize the lattice. Collectively, we find that myosin forces can deform F-actin, generating a conformational landscape that is detected and reciprocally modulated by a mechanosensitive protein, providing a direct structural glimpse at active force transduction through the cytoskeleton.

Indexed as

Actincryo-electron microscopymechanobiologymechanotransductionmyosin

Identifiers

PMID39185238
PMCPMC11343212

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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.