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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: 30 May 2024 | Viewed by 3077

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

Manuscripts should be submitted online at www.mdpi.com by registering and logging in to this website. Once you are registered, click here to go to the submission form. Manuscripts can be submitted until the deadline. All submissions that pass pre-check are peer-reviewed. Accepted papers will be published continuously in the journal (as soon as accepted) and will be listed together on the special issue website. Research articles, review articles as well as short communications are invited. For planned papers, a title and short abstract (about 100 words) can be sent to the Editorial Office for announcement on this website.

Submitted manuscripts should not have been published previously, nor be under consideration for publication elsewhere (except conference proceedings papers). All manuscripts are thoroughly refereed through a single-blind peer-review process. A guide for authors and other relevant information for submission of manuscripts is available on the Instructions for Authors page. International Journal of Molecular Sciences is an international peer-reviewed open access semimonthly journal published by MDPI.

Please visit the Instructions for Authors page before submitting a manuscript. There is an Article Processing Charge (APC) for publication in this open access journal. For details about the APC please see here. Submitted papers should be well formatted and use good English. Authors may use MDPI's English editing service prior to publication or during author revisions.

Keywords

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

Published Papers (2 papers)

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Research

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 - 05 Oct 2023
Cited by 2 | Viewed by 1322
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 - 09 May 2023
Cited by 3 | Viewed by 1342
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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