Evidence map›Paper›PMID 38464072›Full record

ArticlebioRxiv : the preprint server for biology2024

Deciphering Mechanochemical Influences of Emergent Actomyosin Crosstalk using QCM-D.

Emily M Kerivan, Victoria N Amari, William B Weeks, Leigh H Hardin, Lyle Tobin, Omayma Y Al Azzam, Dana N Reinemann

Open access · greenAbstract readPreprint
PubMed Full text at PMC Publisher
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, 1 citations in OpenAlex.

No citing paper in PubMed yet.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

7 authors at 1 institution in 1 country.

Emily M KerivanDepartment of Biomedical Engineering, University of Mississippi, University, MS, USA 38677.
Victoria N AmariDepartment of Biomedical Engineering, University of Mississippi, University, MS, USA 38677.
William B WeeksDepartment of Biomedical Engineering, University of Mississippi, University, MS, USA 38677.
Leigh H HardinDepartment of Biomedical Engineering, University of Mississippi, University, MS, USA 38677.
Lyle TobinDepartment of Biomedical Engineering, University of Mississippi, University, MS, USA 38677.
Omayma Y Al AzzamDepartment of Chemical Engineering, University of Mississippi, University, MS, USA 38677.
Dana N ReinemannDepartment of Biomedical Engineering, University of Mississippi, University, MS, USA 38677.ORCID 0000-0002-3516-3948
University of Mississippi · US

Funding

Biophysical Mechanisms of Force Transmission in Cytoskeletal EnsemblesR35GM147050 · NIGMS · UNIVERSITY OF MISSISSIPPI · PI Dana Nicole Reinemann · 2022 to 2026
$1.7M
NIGMS NIH HHS R35 GM147050
6 · The paper itself

Abstract

Purpose: Cytoskeletal protein ensembles exhibit emergent mechanics where behavior exhibited in teams is not necessarily the sum of the components' single molecule properties. In addition, filaments may act as force sensors that distribute feedback and influence motor protein behavior. To understand the design principles of such emergent mechanics, we developed an approach utilizing QCM-D to measure how actomyosin bundles respond mechanically to environmental variables that alter constituent myosin II motor behavior. Methods: QCM-D is used for the first time to probe alterations in actin-myosin bundle viscoelasticity due to changes in skeletal myosin II concentration and motor nucleotide state. Actomyosin bundles were constructed on a gold QCM-D sensor using a microfluidic setup, and frequency and dissipation change measurements were recorded for each component addition to decipher which assay constituents lead to changes in bundle structural compliancy. Results: Lowering myosin concentration is detected as lower shifts in frequency and dissipation, while the relative changes in frequency and dissipation shifts for both the first and second actin additions are relatively similar. Strikingly, buffer washes with different nucleotides (ATP vs. ADP) yielded unique signatures in frequency and dissipation shifts. As myosin II's ADP-bound state tightly binds actin filaments, we observe an increase in frequency and decrease in dissipation change, indicating a decrease in viscoelasticity, likely due to myosin's increased affinity for actin, conversion from an active motor to a static crosslinker, and ability to recruit additional actin filaments from the surface, making an overall more rigid sensor coating. However, lowering the ADP concentration results in increased system compliancy, indicating that transient crosslinking and retaining a balance of motor activity perhaps results in a more cooperative and productive force generating system. Conclusions: QCM-D can detect changes in actomyosin viscoelasticity due to molecular-level alterations, such as motor concentration and nucleotide state. These results provide support for actin's role as a mechanical force-feedback sensor and demonstrate a new approach for deciphering the feedback mechanisms that drive emergent cytoskeletal ensemble crosstalk and intracellular mechanosensing. This approach can be adapted to investigate environmental influences on more complex cytoskeletal ensemble mechanics, including addition of other motors, crosslinkers, and filament types.

Indexed as

Actincytoskeletal ensemblesforce feedbackmyosinQCM-D

Identifiers

PMID38464072
PMCPMC10925119
OpenAlexW4392388289

What Socratic holds

Textmetadata
LicenceCC BY-NC-ND
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 Socratic graph.