ArticleBiophysical journal2020
Myosin II Filament Dynamics in Actin Networks Revealed with Interferometric Scattering Microscopy.
Article in Biophysical journal, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
What it found
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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.
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Who cites it
6 citing papers in PubMed, 23 citations in OpenAlex.
- Bioinspired Membrane Interfaces: Controlling Actomyosin Architecture and Contractility.ACS applied materials & interfaces · 2023Article
- Actomyosin-Driven Division of a Synthetic Cell.ACS synthetic biology · 2022Review
- Reconstitution of Membrane-tethered Minimal Actin Cortices on Supported Lipid Bilayers.Journal of visualized experiments : JoVE · 2022Article
- Modelling of the dynamic polarizability of macromolecules for single-molecule optical biosensing.Scientific reports · 2022Article
- Mass-sensitive particle tracking to elucidate the membrane-associated MinDE reaction cycle.Nature methods · 2021Article
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Corrections and comments
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Authors and funding
8 authors at 3 institutions in 2 countries.
Funding
Abstract
The plasma membrane and the underlying cytoskeletal cortex constitute active platforms for a variety of cellular processes. Recent work has shown that the remodeling acto-myosin network modifies local membrane organization, but the molecular details are only partly understood because of difficulties with experimentally accessing the relevant time and length scales. Here, we use interferometric scattering microscopy to investigate a minimal acto-myosin network linked to a supported lipid bilayer membrane. Using the magnitude of the interferometric contrast, which is proportional to molecular mass, and fast acquisition rates, we detect and image individual membrane-attached actin filaments diffusing within the acto-myosin network and follow individual myosin II filament dynamics. We quantify myosin II filament dwell times and processivity as functions of ATP concentration, providing experimental evidence for the predicted ensemble behavior of myosin head domains. Our results show how decreasing ATP concentrations lead to both increasing dwell times of individual myosin II filaments and a global change from a remodeling to a contractile state of the acto-myosin network.
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Registered trials
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.