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Special Issue "Motile Function of Myosins in Cells and Tissues"

A special issue of International Journal of Molecular Sciences (ISSN 1422-0067). This special issue belongs to the section "Molecular Biology".

Deadline for manuscript submissions: closed (30 June 2019).

Special Issue Editors

Dr. Haruo Sugi
E-Mail Website
Guest Editor
Department of Physiology, Teikyo University, Itabashi-ku, Tokyo, Japan
Interests: physiology and biochemistry of skeletal; cardiac and smooth muscle myosins in health and in disease; compartive aspects of physiology and biochemistry of muscle and mechanism of locomotion; primitive; role of myosins in primitive motile systems; such as amoevoid movement; contractile ring formation; and other cellulr motile functions
Special Issues and Collections in MDPI journals
Dr. Susumu Minamisawa
E-Mail Website
Co-Guest Editor
Department of Cellular Physiology, Jikei University School of Medicine, Tokyo, Japan
Interests: cardiovascular development; calcium signaling; cardiac metabolism

Special Issue Information

Dear Colleagues,

Myosins constitute a large superfamily and perform a variety of motile functions at the tissue and cellular levels. In skeletal, cardiac, and smooth muscles, myosin forms myosin filaments to produce force and motion in muscle via cyclic interaction with actin filaments, coupled with ATP hydrolysis. Skeletal muscle performance can be enhanced through physical training, which has been studied intensively in the research field of exercise physiology. Cardiovascular activity is maintained by the motile function of cardiac and vascular muscles and has been studied widely in relation to cardiovascular diseases. In primitive motile systems, myosins play an essential role in the amoevoid movement of leucocytes, and cell division resulting from the contractile ring formation. While myosins producing the above motile function are called rower myosins due to their asynchronous attachment to, and detachment from, actin filaments, there are many kinds of myosins, which transport substances within the cells of animals, called porter myosins because of their processive motion along actin filaments.

The main purpose of this Special Issue is to give general readers an idea about the current status of research work on the motile function of myosins as well as remaining mysteries to be investigated in future.

Dr. Haruo Sugi
Dr. Susumu Minamisawa
Guest Editor

Manuscript Submission Information

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Keywords

  • skeletal muscle myosin
  • cardiac muscle myosin
  • smooth muscle myosin
  • muscular exercise and training effects
  • function of porter myosins
  • function of myosins in the amoevoid movement and contractile ring formation
  • other aspects of myosin function

Published Papers (7 papers)

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Research

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Article
X-ray Diffraction Studies on the Structural Origin of Dynamic Tension Recovery Following Ramp-Shaped Releases in High-Ca Rigor Muscle Fibers
Int. J. Mol. Sci. 2020, 21(4), 1244; https://0-doi-org.brum.beds.ac.uk/10.3390/ijms21041244 - 13 Feb 2020
Viewed by 614
Abstract
It is generally believed that during muscle contraction, myosin heads (M) extending from myosin filament attaches to actin filaments (A) to perform power stroke, associated with the reaction, A-M-ADP-Pi → A-M + ADP + Pi, so that myosin heads pass through the state [...] Read more.
It is generally believed that during muscle contraction, myosin heads (M) extending from myosin filament attaches to actin filaments (A) to perform power stroke, associated with the reaction, A-M-ADP-Pi → A-M + ADP + Pi, so that myosin heads pass through the state of A-M, i.e., rigor A-M complex. We have, however, recently found that: (1) an antibody to myosin head, completely covering actin-binding sites in myosin head, has no effect on Ca2+-activated tension in skinned muscle fibers; (2) skinned fibers exhibit distinct tension recovery following ramp-shaped releases (amplitude, 0.5% of Lo; complete in 5 ms); and (3) EDTA, chelating Mg ions, eliminate the tension recovery in low-Ca rigor fibers but not in high-Ca rigor fibers. These results suggest that A-M-ADP myosin heads in high-Ca rigor fibers have dynamic properties to produce the tension recovery following ramp-shaped releases, and that myosin heads do not pass through rigor A-M complex configuration during muscle contraction. To obtain information about the structural changes in A-M-ADP myosin heads during the tension recovery, we performed X-ray diffraction studies on high-Ca rigor skinned fibers subjected to ramp-shaped releases. X-ray diffraction patterns of the fibers were recorded before and after application of ramp-shaped releases. The results obtained indicate that during the initial drop in rigor tension coincident with the applied release, rigor myosin heads take up applied displacement by tilting from oblique to perpendicular configuration to myofilaments, and after the release myosin heads appear to rotate around the helical structure of actin filaments to produce the tension recovery. Full article
(This article belongs to the Special Issue Motile Function of Myosins in Cells and Tissues)
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Review

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Review
Myosin and Other Energy-Transducing ATPases: Structural Dynamics Studied by Electron Paramagnetic Resonance
Int. J. Mol. Sci. 2020, 21(2), 672; https://0-doi-org.brum.beds.ac.uk/10.3390/ijms21020672 - 20 Jan 2020
Cited by 1 | Viewed by 1127
Abstract
The objective of this article was to document the energy-transducing and regulatory interactions in supramolecular complexes such as motor, pump, and clock ATPases. The dynamics and structural features were characterized by motion and distance measurements using spin-labeling electron paramagnetic resonance (EPR) spectroscopy. In [...] Read more.
The objective of this article was to document the energy-transducing and regulatory interactions in supramolecular complexes such as motor, pump, and clock ATPases. The dynamics and structural features were characterized by motion and distance measurements using spin-labeling electron paramagnetic resonance (EPR) spectroscopy. In particular, we focused on myosin ATPase with actin–troponin–tropomyosin, neural kinesin ATPase with microtubule, P-type ion-motive ATPase, and cyanobacterial clock ATPase. Finally, we have described the relationships or common principles among the molecular mechanisms of various energy-transducing systems and how the large-scale thermal structural transition of flexible elements from one state to the other precedes the subsequent irreversible chemical reactions. Full article
(This article belongs to the Special Issue Motile Function of Myosins in Cells and Tissues)
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Review
Direct Sarcomere Modulators Are Promising New Treatments for Cardiomyopathies
Int. J. Mol. Sci. 2020, 21(1), 226; https://0-doi-org.brum.beds.ac.uk/10.3390/ijms21010226 - 28 Dec 2019
Cited by 1 | Viewed by 1354
Abstract
Mutations in sarcomere genes can cause both hypertrophic cardiomyopathy (HCM) and dilated cardiomyopathy (DCM). However, the complex genotype-phenotype relationships in pathophysiology of cardiomyopathies by gene or mutation location are not fully understood. In addition, it is still unclear how mutations within same molecule [...] Read more.
Mutations in sarcomere genes can cause both hypertrophic cardiomyopathy (HCM) and dilated cardiomyopathy (DCM). However, the complex genotype-phenotype relationships in pathophysiology of cardiomyopathies by gene or mutation location are not fully understood. In addition, it is still unclear how mutations within same molecule result in different clinical phenotypes such as HCM and DCM. To clarify how the initial functional insult caused by a subtle change in one protein component of the sarcomere with a given mutation is critical for the development of proper effective treatments for cardiomyopathies. Fortunately, recent technological advances and the development of direct sarcomere modulators have provided a more detailed understanding of the molecular mechanisms that govern the effects of specific mutations. The direct inhibition of sarcomere contractility may be able to suppress the development and progression of HCM with hypercontractile mutations and improve clinical parameters in patients with HCM. On the other hand, direct activation of sarcomere contractility appears to exert unexpected beneficial effects such as reverse remodeling and lower heart rate without increasing adverse cardiovascular events in patients with systolic heart failure due to DCM. Direct sarcomere modulators that can positively influence the natural history of cardiomyopathies represent promising treatment options. Full article
(This article belongs to the Special Issue Motile Function of Myosins in Cells and Tissues)
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Review
Unconventional Myosins: How Regulation Meets Function
Int. J. Mol. Sci. 2020, 21(1), 67; https://0-doi-org.brum.beds.ac.uk/10.3390/ijms21010067 - 20 Dec 2019
Cited by 14 | Viewed by 1459
Abstract
Unconventional myosins are multi-potent molecular motors that are assigned important roles in fundamental cellular processes. Depending on their mechano-enzymatic properties and structural features, myosins fulfil their roles by acting as cargo transporters along the actin cytoskeleton, molecular anchors or tension sensors. In order [...] Read more.
Unconventional myosins are multi-potent molecular motors that are assigned important roles in fundamental cellular processes. Depending on their mechano-enzymatic properties and structural features, myosins fulfil their roles by acting as cargo transporters along the actin cytoskeleton, molecular anchors or tension sensors. In order to perform such a wide range of roles and modes of action, myosins need to be under tight regulation in time and space. This is achieved at multiple levels through diverse regulatory mechanisms: the alternative splicing of various isoforms, the interaction with their binding partners, their phosphorylation, their applied load and the composition of their local environment, such as ions and lipids. This review summarizes our current knowledge of how unconventional myosins are regulated, how these regulatory mechanisms can adapt to the specific features of a myosin and how they can converge with each other in order to ensure the required tight control of their function. Full article
(This article belongs to the Special Issue Motile Function of Myosins in Cells and Tissues)
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Review
Current Understanding of Residual Force Enhancement: Cross-Bridge Component and Non-Cross-Bridge Component
Int. J. Mol. Sci. 2019, 20(21), 5479; https://0-doi-org.brum.beds.ac.uk/10.3390/ijms20215479 - 04 Nov 2019
Cited by 11 | Viewed by 972
Abstract
Muscle contraction is initiated by the interaction between actin and myosin filaments. The sliding of actin filaments relative to myosin filaments is produced by cross-bridge cycling, which is governed by the theoretical framework of the cross-bridge theory. The cross-bridge theory explains well a [...] Read more.
Muscle contraction is initiated by the interaction between actin and myosin filaments. The sliding of actin filaments relative to myosin filaments is produced by cross-bridge cycling, which is governed by the theoretical framework of the cross-bridge theory. The cross-bridge theory explains well a number of mechanical responses, such as isometric and concentric contractions. However, some experimental observations cannot be explained with the cross-bridge theory; for example, the increased isometric force after eccentric contractions. The steady-state, isometric force after an eccentric contraction is greater than that attained in a purely isometric contraction at the same muscle length and same activation level. This well-acknowledged and universally observed property is referred to as residual force enhancement (rFE). Since rFE cannot be explained by the cross-bridge theory, alternative mechanisms for explaining this force response have been proposed. In this review, we introduce the basic concepts of sarcomere length non-uniformity and titin elasticity, which are the primary candidates that have been used for explaining rFE, and discuss unresolved problems regarding these mechanisms, and how to proceed with future experiments in this exciting area of research. Full article
(This article belongs to the Special Issue Motile Function of Myosins in Cells and Tissues)
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Review
Roles of Myosin-Mediated Membrane Trafficking in TGF-β Signaling
Int. J. Mol. Sci. 2019, 20(16), 3913; https://0-doi-org.brum.beds.ac.uk/10.3390/ijms20163913 - 12 Aug 2019
Cited by 6 | Viewed by 1439
Abstract
Recent findings have revealed the role of membrane traffic in the signaling of transforming growth factor-β (TGF-β). These findings originate from the pivotal function of TGF-β in development, cell proliferation, tumor metastasis, and many other processes essential in malignancy. Actin and unconventional myosin [...] Read more.
Recent findings have revealed the role of membrane traffic in the signaling of transforming growth factor-β (TGF-β). These findings originate from the pivotal function of TGF-β in development, cell proliferation, tumor metastasis, and many other processes essential in malignancy. Actin and unconventional myosin have crucial roles in subcellular trafficking of receptors; research has also revealed a growing number of unconventional myosins that have crucial roles in TGF-β signaling. Unconventional myosins modulate the spatial organization of endocytic trafficking and tether membranes or transport them along the actin cytoskeletons. Current models do not fully explain how membrane traffic forms a bridge between TGF-β and the downstream effectors that produce its functional responsiveness, such as cell migration. In this review, we present a brief overview of the current knowledge of the TGF-β signaling pathway and the molecular components that comprise the core pathway as follows: ligands, receptors, and Smad mediators. Second, we highlight key role(s) of myosin motor-mediated protein trafficking and membrane domain segregation in the modulation of the TGF-β signaling pathway. Finally, we review future challenges and provide future prospects in this field. Full article
(This article belongs to the Special Issue Motile Function of Myosins in Cells and Tissues)
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Review
Physiological Significance of the Force-Velocity Relation in Skeletal Muscle and Muscle Fibers
Int. J. Mol. Sci. 2019, 20(12), 3075; https://0-doi-org.brum.beds.ac.uk/10.3390/ijms20123075 - 24 Jun 2019
Cited by 1 | Viewed by 1323
Abstract
The relation between the force (load) and the velocity of shortening (V) in contracting skeletal muscle is part of a rectangular hyperbola: (P + a) V = b(PoP); where Po is the maximum isometric force and [...] Read more.
The relation between the force (load) and the velocity of shortening (V) in contracting skeletal muscle is part of a rectangular hyperbola: (P + a) V = b(PoP); where Po is the maximum isometric force and a and b are constants. The force–velocity (P–V) relation suggests that muscle can regulate its energy output depending on the load imposed on it (Hill, 1938). After the establishment of the sliding filament mechanism (H.E. Huxley and Hanson, 1954), the PV relation has been regarded to reflect the cyclic interaction between myosin heads in myosin filaments and the corresponding myosin-binding sites in actin filaments, coupled with ATP hydrolysis (A.F. Huxley, 1957). In single skeletal muscle fibers, however, the PV relation deviates from the hyperbola at the high force region, indicating complicated characteristics of the cyclic actin–myosin interaction. To correlate the PV relation with kinetics of actin–myosin interaction, skinned muscle fibers have been developed, in which the surface membrane is removed to control chemical and ionic conditions around the 3D lattice of actin and myosin filaments. This article also deals with experimental methods with which the structural instability of skinned fibers can be overcome by applying parabolic decreases in fiber length. Full article
(This article belongs to the Special Issue Motile Function of Myosins in Cells and Tissues)
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