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Muscle Proteins, Functions and Interactions
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Muscle Proteins, Functions and Interactions

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

Deadline for manuscript submissions: closed (30 May 2024) | Viewed by 7037

Special Issue Editor

Prof. Dr. Massimo Reconditi

E-Mail Website
Guest Editor
Department of Experimental and Clinical Medicine, University of Florence, 50134 Florence, Italy
Interests: muscle physiology; mathematical modelling of muscle contraction; mechanics and structure of molecular motors
Special Issues, Collections and Topics in MDPI journals

Special Issue Information

Dear Colleagues,

The main function of striated muscle is to shorten and generate force through the cyclic interaction between actin and myosin, fuelled by ATP hydrolysis. Many other proteins are involved in the regulation of the contraction and in preserving the structure and homogeneity of the sarcomere. These functions are brought about through protein-protein interactions, in a complex interplay that leads to the emergent properties of the sarcomere.

The aim of this Special Issue is to host original research papers and reviews on the proteins at work in striated muscle and on their role in promoting, assisting and regulating the contractile function.

Without intending to be exclusive, the papers collected in this issue could report studies on topics such as actomyosin interactions, thin and thick filament-based regulation, cytoskeletal anchoring proteins, and physiological or pharmacological modulation of protein function. Any of this investigation could be aimed at understanding either the normal functioning or pathological condition.

Prof. Dr. Massimo Reconditi
Guest Editor

Manuscript Submission Information

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Keywords

  • muscle contraction
  • muscle regulation
  • myosin
  • actin
  • titin
  • troponin
  • tropomyosin
  • Z-line
  • M-line
  • sarcomere

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Published Papers (5 papers)

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Research

17 pages, 5532 KiB  
Article
Two Forms of Thick Filament in the Flight Muscle of Drosophila melanogaster
by Hosna Rastegarpouyani, Alimohammad Hojjatian and Kenneth A. Taylor
Int. J. Mol. Sci. 2024, 25(20), 11313; https://doi.org/10.3390/ijms252011313 - 21 Oct 2024
Viewed by 397
Abstract
Invertebrate striated muscle myosin filaments are highly variable in structure. The best characterized myosin filaments are those found in insect indirect flight muscle (IFM) in which the flight-powering muscles are not attached directly to the wings. Four insect orders, Hemiptera, Diptera, Hymenoptera, and [...] Read more.
Invertebrate striated muscle myosin filaments are highly variable in structure. The best characterized myosin filaments are those found in insect indirect flight muscle (IFM) in which the flight-powering muscles are not attached directly to the wings. Four insect orders, Hemiptera, Diptera, Hymenoptera, and Coleoptera, have evolved IFM. IFM thick filaments from the first three orders have highly similar myosin arrangements but differ significantly among their non-myosin proteins. The cryo-electron microscopy of isolated IFM myosin filaments from the Dipteran Drosophila melanogaster described here revealed the coexistence of two distinct filament types, one presenting a tubular backbone like in previous work and the other a solid backbone. Inside an annulus of myosin tails, tubular filaments show no noticeable densities; solid filaments show four paired paramyosin densities. Both myosin heads of the tubular filaments are disordered; solid filaments have one completely and one partially immobilized head. Tubular filaments have the protein stretchin-klp on their surface; solid filaments do not. Two proteins, flightin and myofilin, are identifiable in all the IFM filaments previously determined. In Drosophila, flightin assumes two conformations, being compact in solid filaments and extended in tubular filaments. Nearly identical solid filaments occur in the large water bug Lethocerus indicus, which flies infrequently. The Drosophila tubular filaments occur in younger flies, and the solid filaments appear in older flies, which fly less frequently if at all, suggesting that the solid filament form is correlated with infrequent muscle use. We suggest that the solid form is designed to conserve ATP when the muscle is not in active use. Full article
(This article belongs to the Special Issue Muscle Proteins, Functions and Interactions)
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27 pages, 3222 KiB  
Article
Cost-Efficient Expression of Human Cardiac Myosin Heavy Chain in C2C12 Cells with a Non-Viral Transfection Reagent
by Albin E. Berg, Lok Priya Velayuthan, Alf Månsson and Marko Ušaj
Int. J. Mol. Sci. 2024, 25(12), 6747; https://doi.org/10.3390/ijms25126747 - 19 Jun 2024
Viewed by 1043
Abstract
Production of functional myosin heavy chain (MHC) of striated muscle myosin II for studies of isolated proteins requires mature muscle (e.g., C2C12) cells for expression. This is important both for fundamental studies of molecular mechanisms and for investigations of deleterious diseases like cardiomyopathies [...] Read more.
Production of functional myosin heavy chain (MHC) of striated muscle myosin II for studies of isolated proteins requires mature muscle (e.g., C2C12) cells for expression. This is important both for fundamental studies of molecular mechanisms and for investigations of deleterious diseases like cardiomyopathies due to mutations in the MHC gene (MYH7). Generally, an adenovirus vector is used for transfection, but recently we demonstrated transfection by a non-viral polymer reagent, JetPrime. Due to the rather high costs of JetPrime and for the sustainability of the virus-free expression method, access to more than one transfection reagent is important. Here, we therefore evaluate such a candidate substance, GenJet. Using the human cardiac β-myosin heavy chain (β-MHC) as a model system, we found effective transfection of C2C12 cells showing a transfection efficiency nearly as good as with the JetPrime reagent. This was achieved following a protocol developed for JetPrime because a manufacturer-recommended application protocol for GenJet to transfect cells in suspension did not perform well. We demonstrate, using in vitro motility assays and single-molecule ATP turnover assays, that the protein expressed and purified from cells transfected with the GenJet reagent is functional. The purification yields reached were slightly lower than in JetPrime-based purifications, but they were achieved at a significantly lower cost. Our results demonstrate the sustainability of the virus-free method by showing that more than one polymer-based transfection reagent can generate useful amounts of active MHC. Particularly, we suggest that GenJet, due to its current ~4-fold lower cost, is useful for applications requiring larger amounts of a given MHC variant. Full article
(This article belongs to the Special Issue Muscle Proteins, Functions and Interactions)
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15 pages, 3093 KiB  
Article
Inflammatory Cytokine-Induced Muscle Atrophy and Weakness Can Be Ameliorated by an Inhibition of TGF-β-Activated Kinase-1
by Mai Kanai, Byambasuren Ganbaatar, Itsuro Endo, Yukiyo Ohnishi, Jumpei Teramachi, Hirofumi Tenshin, Yoshiki Higa, Masahiro Hiasa, Yukari Mitsui, Tomoyo Hara, Shiho Masuda, Hiroki Yamagami, Yuki Yamaguchi, Ken-ichi Aihara, Mayu Sebe, Rie Tsutsumi, Hiroshi Sakaue, Toshio Matsumoto and Masahiro Abe
Int. J. Mol. Sci. 2024, 25(11), 5715; https://doi.org/10.3390/ijms25115715 - 24 May 2024
Viewed by 1217
Abstract
Chronic inflammation causes muscle wasting. Because most inflammatory cytokine signals are mediated via TGF-β-activated kinase-1 (TAK1) activation, inflammatory cytokine-induced muscle wasting may be ameliorated by the inhibition of TAK1 activity. The present study was undertaken to clarify whether TAK1 inhibition can ameliorate inflammation-induced [...] Read more.
Chronic inflammation causes muscle wasting. Because most inflammatory cytokine signals are mediated via TGF-β-activated kinase-1 (TAK1) activation, inflammatory cytokine-induced muscle wasting may be ameliorated by the inhibition of TAK1 activity. The present study was undertaken to clarify whether TAK1 inhibition can ameliorate inflammation-induced muscle wasting. SKG/Jcl mice as an autoimmune arthritis animal model were treated with a small amount of mannan as an adjuvant to enhance the production of TNF-α and IL-1β. The increase in these inflammatory cytokines caused a reduction in muscle mass and strength along with an induction of arthritis in SKG/Jcl mice. Those changes in muscle fibers were mediated via the phosphorylation of TAK1, which activated the downstream signaling cascade via NF-κB, p38 MAPK, and ERK pathways, resulting in an increase in myostatin expression. Myostatin then reduced the expression of muscle proteins not only via a reduction in MyoD1 expression but also via an enhancement of Atrogin-1 and Murf1 expression. TAK1 inhibitor, LL-Z1640-2, prevented all the cytokine-induced changes in muscle wasting. Thus, TAK1 inhibition can be a new therapeutic target of not only joint destruction but also muscle wasting induced by inflammatory cytokines. Full article
(This article belongs to the Special Issue Muscle Proteins, Functions and Interactions)
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21 pages, 4797 KiB  
Article
Structure of the Drosophila melanogaster Flight Muscle Myosin Filament at 4.7 Å Resolution Reveals New Details of Non-Myosin Proteins
by Fatemeh Abbasi Yeganeh, Hosna Rastegarpouyani, Jiawei Li and Kenneth A. Taylor
Int. J. Mol. Sci. 2023, 24(19), 14936; https://doi.org/10.3390/ijms241914936 - 5 Oct 2023
Cited by 3 | Viewed by 1967
Abstract
Striated muscle thick filaments are composed of myosin II and several non-myosin proteins which define the filament length and modify its function. Myosin II has a globular N-terminal motor domain comprising its catalytic and actin-binding activities and a long α-helical, coiled tail [...] Read more.
Striated muscle thick filaments are composed of myosin II and several non-myosin proteins which define the filament length and modify its function. Myosin II has a globular N-terminal motor domain comprising its catalytic and actin-binding activities and a long α-helical, coiled tail that forms the dense filament backbone. Myosin alone polymerizes into filaments of irregular length, but striated muscle thick filaments have defined lengths that, with thin filaments, define the sarcomere structure. The motor domain structure and function are well understood, but the myosin filament backbone is not. Here we report on the structure of the flight muscle thick filaments from Drosophila melanogaster at 4.7 Å resolution, which eliminates previous ambiguities in non-myosin densities. The full proximal S2 region is resolved, as are the connecting densities between the Ig domains of stretchin-klp. The proteins, flightin, and myofilin are resolved in sufficient detail to build an atomic model based on an AlphaFold prediction. Our results suggest a method by which flightin and myofilin cooperate to define the structure of the thick filament and explains a key myosin mutation that affects flightin incorporation. Drosophila is a genetic model organism for which our results can define strategies for functional testing. Full article
(This article belongs to the Special Issue Muscle Proteins, Functions and Interactions)
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19 pages, 4547 KiB  
Article
Using Multiscale Simulations as a Tool to Interpret Equatorial X-ray Fiber Diffraction Patterns from Skeletal Muscle
by Momcilo Prodanovic, Yiwei Wang, Srboljub M. Mijailovich and Thomas Irving
Int. J. Mol. Sci. 2023, 24(10), 8474; https://doi.org/10.3390/ijms24108474 - 9 May 2023
Cited by 4 | Viewed by 1776
Abstract
Synchrotron small-angle X-ray diffraction is the method of choice for nm-scale structural studies of striated muscle under physiological conditions and on millisecond time scales. The lack of generally applicable computational tools for modeling X-ray diffraction patterns from intact muscles has been a significant [...] Read more.
Synchrotron small-angle X-ray diffraction is the method of choice for nm-scale structural studies of striated muscle under physiological conditions and on millisecond time scales. The lack of generally applicable computational tools for modeling X-ray diffraction patterns from intact muscles has been a significant barrier to exploiting the full potential of this technique. Here, we report a novel “forward problem” approach using the spatially explicit computational simulation platform MUSICO to predict equatorial small-angle X-ray diffraction patterns and the force output simultaneously from resting and isometrically contracting rat skeletal muscle that can be compared to experimental data. The simulation generates families of thick–thin filament repeating units, each with their individually predicted occupancies of different populations of active and inactive myosin heads that can be used to generate 2D-projected electron density models based on known Protein Data Bank structures. We show how, by adjusting only a few selected parameters, we can achieve a good correspondence between experimental and predicted X-ray intensities. The developments presented here demonstrate the feasibility of combining X-ray diffraction and spatially explicit modeling to form a powerful hypothesis-generating tool that can be used to motivate experiments that can reveal emergent properties of muscle. Full article
(This article belongs to the Special Issue Muscle Proteins, Functions and Interactions)
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