Myosin: Formation and maintenance of thick filaments

Ojima, Koichi

doi:10.1111/asj.13226

Cited by 25 publications

(9 citation statements)

References 66 publications

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“…How interaction of MyBP-C with myosin enhances the SRX state is another fertile but challenging area of investigation, which may require cryo-electron tomography of thick filaments or intact myofibrils ( Burbaum et al, 2021 ) or single particle cryo-EM studies of MyBP-C–IHM complexes. Experiments suggest that thick filaments in muscle are in equilibrium with a pool of myosin monomer, which may play a role in thick filament assembly/disassembly during development, hypertrophy, and myosin turnover ( Saad et al, 1986 ; Katoh et al, 1998 ; Ojima, 2019 ). Myosin monomers at physiological ionic strength form IHMs with a folded tail structure and slow ATP turnover rate, which may act as a transport form from ribosome to filament ( Ankrett et al, 1991 ; Katoh et al, 1998 ; Jung et al, 2008 ).…”

Section: Future Directionsmentioning

confidence: 99%

Structural basis of the super- and hyper-relaxed states of myosin II

Craig

Padrón

2021

Journal of General Physiology

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Super-relaxation is a state of muscle thick filaments in which ATP turnover by myosin is much slower than that of myosin II in solution. This inhibited state, in equilibrium with a faster (relaxed) state, is ubiquitous and thought to be fundamental to muscle function, acting as a mechanism for switching off energy-consuming myosin motors when they are not being used. The structural basis of super-relaxation is usually taken to be a motif formed by myosin in which the two heads interact with each other and with the proximal tail forming an interacting-heads motif, which switches the heads off. However, recent studies show that even isolated myosin heads can exhibit this slow rate. Here, we review the role of head interactions in creating the super-relaxed state and show how increased numbers of interactions in thick filaments underlie the high levels of super-relaxation found in intact muscle. We suggest how a third, even more inhibited, state of myosin (a hyper-relaxed state) seen in certain species results from additional interactions involving the heads. We speculate on the relationship between animal lifestyle and level of super-relaxation in different species and on the mechanism of formation of the super-relaxed state. We also review how super-relaxed thick filaments are activated and how the super-relaxed state is modulated in healthy and diseased muscles.

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Section: Future Directionsmentioning

confidence: 99%

Structural basis of the super- and hyper-relaxed states of myosin II

Craig

Padrón

2021

Journal of General Physiology

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“…The tail domain is responsible for myosin coiled-coil dimerization and the bivalent nature of most myosins. These domains are also isoform-specific and can associate with various distinct cellular cargo, membrane-spanning motifs, as well as forming the shaft of the thick filament [ 64 , 65 , 66 , 67 ].…”

Section: Introduction To Myosin Structurementioning

confidence: 99%

The Central Role of the F-Actin Surface in Myosin Force Generation

Doran

Lehman

2021

Biology

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Actin is one of the most abundant and versatile proteins in eukaryotic cells. As discussed in many contributions to this Special Issue, its transition from a monomeric G-actin to a filamentous F-actin form plays a critical role in a variety of cellular processes, including control of cell shape and cell motility. Once polymerized from G-actin, F-actin forms the central core of muscle-thin filaments and acts as molecular tracks for myosin-based motor activity. The ATP-dependent cross-bridge cycle of myosin attachment and detachment drives the sliding of myosin thick filaments past thin filaments in muscle and the translocation of cargo in somatic cells. The variation in actin function is dependent on the variation in muscle and non-muscle myosin isoform behavior as well as interactions with a plethora of additional actin-binding proteins. Extensive work has been devoted to defining the kinetics of actin-based force generation powered by the ATPase activity of myosin. In addition, over the past decade, cryo-electron microscopy has revealed the atomic-evel details of the binding of myosin isoforms on the F-actin surface. Most accounts of the structural interactions between myosin and actin are described from the perspective of the myosin molecule. Here, we discuss myosin-binding to actin as viewed from the actin surface. We then describe conserved structural features of actin required for the binding of all or most myosin isoforms while also noting specific interactions unique to myosin isoforms.

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“…In this study, transcriptome and annotation identified nine families of flight muscle structural proteins in S. frugiperda , with myosin and actin showing higher number of transcripts ( Table 2 ). Myosin is a superfamily of molecular motors that move along the track of actin filaments, which accounts for 60% of the total protein of myofibrils and plays a role in muscle contraction [ 63 ]. One flightin-encoding gene was also found in S. frugiperda .…”

Section: Discussionmentioning

confidence: 99%

The Transcription of Flight Energy Metabolism Enzymes Declined with Aging While Enzyme Activity Increased in the Long-Distance Migratory Moth, Spodoptera frugiperda

et al. 2022

Insects

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Of all the things that can fly, the flight mechanisms of insects are possibly the least understood. By using RNAseq, we studied the aging-associated gene expression changes in the thorax of Spodoptera frugiperda females. Three possible flight energy metabolism pathways were constructed based on 32 key metabolic enzymes found in S. frugiperda. Differential expression analysis revealed up to 2000 DEGs within old females versus young ones. Expression and GO and KEGG enrichment analyses indicated that most genes and pathways related to energy metabolism and other biological processes, such as transport, redox, longevity and signaling pathway, were downregulated with aging. However, activity assay showed that the activities of all the five tested key enzymes increased with age. The age-associated transcriptional decrease and activity increase in these enzymes suggest that these enzymes are stable. S. frugiperda is a long-distance migrator, and a high activity of enzymes may be important to guarantee a high flight capacity. The activity ratio of GAPDH/HOAD ranged from 0.594 to 0.412, suggesting that lipid is the main fuel of this species, particularly in old individuals. Moreover, the expression of enzymes in the proline oxidation pathway increased with age, suggesting that this energy metabolic pathway also is important for this species or linked to some aging-specific processes. In addition, the expression of immunity- and repair-related genes also increased with age. This study established the overall transcriptome framework of the flight muscle and aging-associated expression change trajectories in an insect for the first time.

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Myosin: Formation and maintenance of thick filaments

Cited by 25 publications

References 66 publications

Structural basis of the super- and hyper-relaxed states of myosin II

Structural basis of the super- and hyper-relaxed states of myosin II

The Central Role of the F-Actin Surface in Myosin Force Generation

The Transcription of Flight Energy Metabolism Enzymes Declined with Aging While Enzyme Activity Increased in the Long-Distance Migratory Moth, Spodoptera frugiperda

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