Smith, Quentin M, Inchingolo, Alessio V, Mihailescu, Madalina-Daniela, Dai, Hongsheng, Kad, Neil M (2021) Single-molecule imaging reveals the concerted release of myosin from regulated thin filaments. eLife, . Article Number e69184. ISSN 2050-084X. (doi:10.7554/eLife.69184) (KAR id:90476)
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Official URL: https://doi.org/10.7554/eLife.69184 |
Abstract
Regulated thin filaments (RTFs) tightly control striated muscle contraction through calcium binding to troponin, which enables tropomyosin to expose myosin-binding sites on actin. Myosin binding holds tropomyosin in an open position, exposing more myosin-binding sites on actin, leading to cooperative activation. At lower calcium levels, troponin and tropomyosin turn off the thin filament; however, this is antagonised by the high local concentration of myosin, questioning how the thin filament relaxes. To provide molecular details of deactivation, we used single-molecule imaging of green fluorescent protein (GFP)-tagged myosin-S1 (S1-GFP) to follow the activation of RTF tightropes. In sub-maximal activation conditions, RTFs are not fully active, enabling direct observation of deactivation in real time. We observed that myosin binding occurs in a stochastic step-wise fashion; however, an unexpectedly large probability of multiple contemporaneous detachments is observed. This suggests that deactivation of the thin filament is a coordinated active process.
Item Type: | Article |
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DOI/Identification number: | 10.7554/eLife.69184 |
Uncontrolled keywords: | Regulated thin filmanets, RTFs, myosin |
Subjects: | Q Science > QD Chemistry > QD431 Organic Chemistry- Biochemistry- Proteins, peptides, amino acids |
Divisions: | Divisions > Division of Natural Sciences > Biosciences |
Depositing User: | Neil Kad |
Date Deposited: | 29 Sep 2021 16:17 UTC |
Last Modified: | 14 Nov 2022 23:13 UTC |
Resource URI: | https://kar.kent.ac.uk/id/eprint/90476 (The current URI for this page, for reference purposes) |
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