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Title[redir]:
Misregulation of autophagy and protein degradation systems in myopathies and muscular dystrophies | Journal of Cell Science | The Company of Biologists
Description:
Summary. A number of recent studies have highlighted the importance of autophagy and the ubiquitin-proteasome in the pathogenesis of muscle wasting in different types of inherited muscle disorders. Autophagy is crucial for the removal of dysfunctional organelles and protein aggregates, whereas the ubiquitin-proteasome is important for the quality control of proteins. Post-mitotic tissues, such as skeletal muscle, are particularly susceptible to aged or dysfunctional organelles and aggregation-prone proteins. Therefore, these degradation systems need to be carefully regulated in muscles. Indeed, excessive or defective activity of the autophagy lysosome or ubiquitin-proteasome leads to detrimental effects on muscle homeostasis. A growing number of studies link abnormalities in the regulation of these two pathways to myofiber degeneration and muscle weakness. Understanding the pathogenic role of these degradative systems in each inherited muscle disorder might provide novel therapeutic targets to counteract muscle wasting. In this Commentary, we will discuss the current view on the role of autophagy lysosome and ubiquitin-proteasome in the pathogenesis of myopathies and muscular dystrophies, and how alteration of these degradative systems contribute to muscle wasting in inherited muscle disorders. We will also discuss how modulating autophagy and proteasome might represent a promising strategy for counteracting muscle loss in different diseases.
Title[redir]:
Misregulation of autophagy and protein degradation systems in myopathies and muscular dystrophies | Journal of Cell Science | The Company of Biologists
Description:
Summary. A number of recent studies have highlighted the importance of autophagy and the ubiquitin-proteasome in the pathogenesis of muscle wasting in different types of inherited muscle disorders. Autophagy is crucial for the removal of dysfunctional organelles and protein aggregates, whereas the ubiquitin-proteasome is important for the quality control of proteins. Post-mitotic tissues, such as skeletal muscle, are particularly susceptible to aged or dysfunctional organelles and aggregation-prone proteins. Therefore, these degradation systems need to be carefully regulated in muscles. Indeed, excessive or defective activity of the autophagy lysosome or ubiquitin-proteasome leads to detrimental effects on muscle homeostasis. A growing number of studies link abnormalities in the regulation of these two pathways to myofiber degeneration and muscle weakness. Understanding the pathogenic role of these degradative systems in each inherited muscle disorder might provide novel therapeutic targets to counteract muscle wasting. In this Commentary, we will discuss the current view on the role of autophagy lysosome and ubiquitin-proteasome in the pathogenesis of myopathies and muscular dystrophies, and how alteration of these degradative systems contribute to muscle wasting in inherited muscle disorders. We will also discuss how modulating autophagy and proteasome might represent a promising strategy for counteracting muscle loss in different diseases.
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Keywords {🔍}
autophagy, muscle, google, scholarcrossref, disease, mice, protein, muscular, skeletal, cell, autophagic, lysosomal, proteins, role, muscles, proteasome, degradation, lysosomes, patients, diseases, myopathy, dystrophies, sandri, dystrophy, glycogen, trim, pompe, lysosome, studies, ubiquitin, membrane, mutations, accumulation, gene, flux, organelles, atrophy, type, collagen, myofiber, raben, inhibition, activation, open, ubiquitinproteasome, genes, danon, mouse, mdx, inherited,
Topics {✒️}
open menu collagen-vi-related diseases paved putative e3-ubiquitin-ligase gene including collagen-vi-related diseases pgc-1α activates lysosomal emery–dreyfuss muscular dystrophy emery-dreifuss muscular dystrophy fast-tracked decision making ubiquitin–e2 thio-ester jcs fast-track option atp-dependent activating enzyme collagen-vi-related diseases collagen vi-related diseases acid alpha-glucosidase deficiency gaa-deficient muscles prevents mediates protein–protein interactions mis-sense mutated dysferlin collagen vi-related myopathies ikkbeta/nf-kappab activation patient-derived muscle cells vitro tools muscle-wasting conditions grants severe early-onset form late-onset gsdii patients bio-nmd fp7-health-241665 feeding col6a1-null mice experimental myopathy induced highly reactive ubiquitin specific ubiquitin ligases cell science journal share enzyme replacement therapy x-linked vacuolar cardiomyopathy dystrophin-deficient mdx mice e3 ubiquitin ligase congenital muscular dystrophy ameliorates muscular dystrophy centrally nucleated fibers large glycogen-filled lysosomes lysosomal storage diseases amino acids inside proteasome-mediated protein degradation electron microscopy analyses excessive akt–mtor signaling late-onset forms collagen-vi-null search distinct microfilamentous network collagen vi deficiency
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ScholarlyArticle:
context:https://schema.org
id:https://journals.biologists.com/jcs/article/126/23/5325/54013/Misregulation-of-autophagy-and-protein-degradation
name:Misregulation of autophagy and protein degradation systems in myopathies and muscular dystrophies
datePublished:2013-12-01
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name:Journal of Cell Science
issn:
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url:https://dx.doi.org/10.1242/jcs.114041
keywords:
Autophagy
Duchenne
Dystrophy
Muscle wasting
Myopathy
Skeletal muscle
inLanguage:en
copyrightHolder:
copyrightYear:2025
publisher:
author:
name:Sandri, Marco
affiliation:1 Department of Biomedical Sciences, University of Padova , 35131 Padova , Italy 2 Dulbecco Telethon Institute, Venetian Institute of Molecular Medicine , 35129 Padova , Italy 3 Institute of Neuroscience, Consiglio Nazionale delle Ricerche , 35121 Padova , Italy 4 Department of Medicine, McGill University , Montreal, QC H3G 1Y6 , Canada
type:Person
name:Coletto, Luisa
affiliation:2 Dulbecco Telethon Institute, Venetian Institute of Molecular Medicine , 35129 Padova , Italy
type:Person
name:Grumati, Paolo
affiliation:5 Department of Molecular Medicine, University of Padova , 35131 Padova , Italy
type:Person
name:Bonaldo, Paolo
affiliation:5 Department of Molecular Medicine, University of Padova , 35131 Padova , Italy
type:Person
description:Summary. A number of recent studies have highlighted the importance of autophagy and the ubiquitin-proteasome in the pathogenesis of muscle wasting in different types of inherited muscle disorders. Autophagy is crucial for the removal of dysfunctional organelles and protein aggregates, whereas the ubiquitin-proteasome is important for the quality control of proteins. Post-mitotic tissues, such as skeletal muscle, are particularly susceptible to aged or dysfunctional organelles and aggregation-prone proteins. Therefore, these degradation systems need to be carefully regulated in muscles. Indeed, excessive or defective activity of the autophagy lysosome or ubiquitin-proteasome leads to detrimental effects on muscle homeostasis. A growing number of studies link abnormalities in the regulation of these two pathways to myofiber degeneration and muscle weakness. Understanding the pathogenic role of these degradative systems in each inherited muscle disorder might provide novel therapeutic targets to counteract muscle wasting. In this Commentary, we will discuss the current view on the role of autophagy lysosome and ubiquitin-proteasome in the pathogenesis of myopathies and muscular dystrophies, and how alteration of these degradative systems contribute to muscle wasting in inherited muscle disorders. We will also discuss how modulating autophagy and proteasome might represent a promising strategy for counteracting muscle loss in different diseases.
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headline:Misregulation of autophagy and protein degradation systems in myopathies and muscular dystrophies
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id:https://journals.biologists.com/jcs/issue/126/23
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issn:
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Periodical:
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issn:
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Person:
name:Sandri, Marco
affiliation:1 Department of Biomedical Sciences, University of Padova , 35131 Padova , Italy 2 Dulbecco Telethon Institute, Venetian Institute of Molecular Medicine , 35129 Padova , Italy 3 Institute of Neuroscience, Consiglio Nazionale delle Ricerche , 35121 Padova , Italy 4 Department of Medicine, McGill University , Montreal, QC H3G 1Y6 , Canada
name:Coletto, Luisa
affiliation:2 Dulbecco Telethon Institute, Venetian Institute of Molecular Medicine , 35129 Padova , Italy
name:Grumati, Paolo
affiliation:5 Department of Molecular Medicine, University of Padova , 35131 Padova , Italy
name:Bonaldo, Paolo
affiliation:5 Department of Molecular Medicine, University of Padova , 35131 Padova , Italy
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