{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,8]],"date-time":"2026-09-08T02:29:57Z","timestamp":1788834597447,"version":"build-2803163510"},"reference-count":235,"publisher":"MDPI AG","issue":"10","license":[{"start":{"date-parts":[[2025,5,15]],"date-time":"2025-05-15T00:00:00Z","timestamp":1747267200000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"name":"British Heart Foundation Project","award":["PG\/23\/11511"],"award-info":[{"award-number":["PG\/23\/11511"]}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Cells"],"abstract":"<jats:p>The stability of the sarcolemma is severely impaired in a series of genetic neuromuscular diseases defined as muscular dystrophies. These are characterized by the centralization of skeletal muscle syncytial nuclei, the replacement of muscle fibers with fibrotic tissue, the release of inflammatory cytokines, and the disruption of muscle protein homeostasis, ultimately leading to necrosis and loss of muscle functionality. A specific subgroup of muscular dystrophies is associated with genetic defects in components of the dystrophin\u2013glycoprotein complex (DGC), which plays a crucial role in linking the cytosol to the skeletal muscle basement membrane. In these cases, dystrophin-associated proteins fail to correctly localize to the sarcolemma, resulting in dystrophy characterized by an uncontrolled increase in protein degradation, which can ultimately lead to cell death. In this review, we explore the role of intracellular degradative pathways\u2014primarily the ubiquitin\u2013proteasome and autophagy\u2013lysosome systems\u2014in the progression of DGC-linked muscular dystrophies. The DGC acts as a hub for numerous signaling pathways that regulate various cellular functions, including protein homeostasis. We examine whether the loss of structural stability within the DGC affects key signaling pathways that modulate protein recycling, with a particular emphasis on autophagy.<\/jats:p>","DOI":"10.3390\/cells14100721","type":"journal-article","created":{"date-parts":[[2025,5,15]],"date-time":"2025-05-15T08:56:55Z","timestamp":1747299415000},"page":"721","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":4,"title":["Misregulation of the Ubiquitin\u2013Proteasome System and Autophagy in Muscular Dystrophies Associated with the Dystrophin\u2013Glycoprotein Complex"],"prefix":"10.3390","volume":"14","author":[{"ORCID":"https:\/\/orcid.org\/0000-0002-2656-5849","authenticated-orcid":false,"given":"Manuela","family":"Bozzi","sequence":"first","affiliation":[{"name":"Dipartimento di Scienze Biotecnologiche di Base, Cliniche Intensivologiche e Perioperatorie, Sezione di Biochimica e Biochimica Clinica, Universit\u00e0 Cattolica del Sacro Cuore, Largo F. Vito 1, 00168 Roma, Italy"},{"name":"Istituto di Scienze e Tecnologie Chimiche \u201cGiulio Natta\u201d\u2014SCITEC (CNR), Largo F. Vito, 00168 Roma, Italy"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-2123-1516","authenticated-orcid":false,"given":"Francesca","family":"Sciandra","sequence":"additional","affiliation":[{"name":"Istituto di Scienze e Tecnologie Chimiche \u201cGiulio Natta\u201d\u2014SCITEC (CNR), Largo F. Vito, 00168 Roma, Italy"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Maria Giulia","family":"Bigotti","sequence":"additional","affiliation":[{"name":"Bristol Heart Institute, Bristol Royal Infirmary, Research Floor Level 7, Bristol BS2 8HW, UK"},{"name":"School of Biochemistry, University of Bristol, Bristol BS8 1TD, UK"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-4690-8826","authenticated-orcid":false,"given":"Andrea","family":"Brancaccio","sequence":"additional","affiliation":[{"name":"Istituto di Scienze e Tecnologie Chimiche \u201cGiulio Natta\u201d\u2014SCITEC (CNR), Largo F. Vito, 00168 Roma, Italy"},{"name":"School of Biochemistry, University of Bristol, Bristol BS8 1TD, UK"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"1968","published-online":{"date-parts":[[2025,5,15]]},"reference":[{"key":"ref_1","doi-asserted-by":"crossref","first-page":"291","DOI":"10.1152\/physrev.00028.2001","article-title":"Function and Genetics of Dystrophin and Dystrophin-Related Proteins in Muscle","volume":"82","author":"Blake","year":"2002","journal-title":"Physiol. Rev."},{"key":"ref_2","doi-asserted-by":"crossref","first-page":"191","DOI":"10.1016\/S0074-7696(07)65005-0","article-title":"Biology of the Striated Muscle Dystrophin-Glycoprotein Complex","volume":"265","author":"Ervasti","year":"2008","journal-title":"Int. Rev. Cytol."},{"key":"ref_3","doi-asserted-by":"crossref","first-page":"1223","DOI":"10.1002\/j.2040-4603.2015.tb00638.x","article-title":"The Dystrophin Complex: Structure, Function, and Implications for Therapy","volume":"5","author":"Gao","year":"2015","journal-title":"Compr. Physiol."},{"key":"ref_4","doi-asserted-by":"crossref","first-page":"27305","DOI":"10.1074\/jbc.270.45.27305","article-title":"Identification and Characterization of the Dystrophin Anchoring Site on \u03b2-Dystroglycan","volume":"270","author":"Jung","year":"1995","journal-title":"J. Biol. Chem."},{"key":"ref_5","doi-asserted-by":"crossref","first-page":"4590","DOI":"10.1046\/j.1432-1327.2001.02386.x","article-title":"Identification of the \u03b2-Dystroglycan Binding Epitope within the C-Terminal Region of \u03b1-Dystroglycan","volume":"268","author":"Sciandra","year":"2001","journal-title":"Eur. J. Biochem."},{"key":"ref_6","doi-asserted-by":"crossref","first-page":"696","DOI":"10.1038\/355696a0","article-title":"Primary Structure of Dystrophin-Associated Glycoproteins Linking Dystrophin to the Extracellular Matrix","volume":"355","author":"Ervasti","year":"1992","journal-title":"Nature"},{"key":"ref_7","doi-asserted-by":"crossref","first-page":"810","DOI":"10.1038\/nchembio.2146","article-title":"Structural Basis of Laminin Binding to the LARGE Glycans on Dystroglycan","volume":"12","author":"Briggs","year":"2016","journal-title":"Nat. Chem. Biol."},{"key":"ref_8","doi-asserted-by":"crossref","first-page":"1261","DOI":"10.1038\/s41586-024-08324-w","article-title":"Native DGC Structure Rationalizes Muscular Dystrophy-Causing Mutations","volume":"637","author":"Liu","year":"2025","journal-title":"Nature"},{"key":"ref_9","doi-asserted-by":"crossref","first-page":"1252","DOI":"10.1038\/s41586-024-08310-2","article-title":"Structure and Assembly of the Dystrophin Glycoprotein Complex","volume":"637","author":"Wan","year":"2025","journal-title":"Nature"},{"key":"ref_10","doi-asserted-by":"crossref","unstructured":"Wilson, D.G.S., Tinker, A., and Iskratsch, T. (2022). The Role of the Dystrophin Glycoprotein Complex in Muscle Cell Mechanotransduction. Commun. Biol., 5.","DOI":"10.1038\/s42003-022-03980-y"},{"key":"ref_11","doi-asserted-by":"crossref","unstructured":"Sciandra, F., Bozzi, M., and Bigotti, M.G. (2023). From Adhesion Complex to Signaling Hub: The Dual Role of Dystroglycan. Front. Mol. Biosci., 10.","DOI":"10.3389\/fmolb.2023.1325284"},{"key":"ref_12","doi-asserted-by":"crossref","first-page":"3058","DOI":"10.1111\/jcmm.14218","article-title":"A Molecular Overview of the Primary Dystroglycanopathies","volume":"23","author":"Brancaccio","year":"2019","journal-title":"J. Cell Mol. Med."},{"key":"ref_13","doi-asserted-by":"crossref","first-page":"2025","DOI":"10.1016\/S0140-6736(19)32910-1","article-title":"Muscular Dystrophies","volume":"394","author":"Mercuri","year":"2019","journal-title":"Lancet"},{"key":"ref_14","doi-asserted-by":"crossref","first-page":"141","DOI":"10.1186\/s13023-020-01430-8","article-title":"Global Epidemiology of Duchenne Muscular Dystrophy: An Updated Systematic Review and Meta-Analysis","volume":"15","author":"Crisafulli","year":"2020","journal-title":"Orphanet J. Rare Dis."},{"key":"ref_15","doi-asserted-by":"crossref","first-page":"783","DOI":"10.5692\/clinicalneurol.54.783","article-title":"Changes in Clinical Condition and Causes of Death of Inpatients with Duchenne Muscular Dystrophy in Japan from 1999 to 2012","volume":"54","author":"Saito","year":"2014","journal-title":"Rinsho Shinkeigaku"},{"key":"ref_16","doi-asserted-by":"crossref","first-page":"1363","DOI":"10.1056\/NEJM198805263182104","article-title":"Characterization of Dystrophin in Muscle-Biopsy Specimens from Patients with Duchenne\u2019s or Becker\u2019s Muscular Dystrophy","volume":"318","author":"Hoffman","year":"1988","journal-title":"N. Engl. J. Med."},{"key":"ref_17","doi-asserted-by":"crossref","unstructured":"Sheikh, O., and Yokota, T. (2020). Advances in Genetic Characterization and Genotype-Phenotype Correlation of Duchenne and Becker Muscular Dystrophy in the Personalized Medicine Era. J. Pers. Med., 10.","DOI":"10.3390\/jpm10030111"},{"key":"ref_18","doi-asserted-by":"crossref","first-page":"199","DOI":"10.1242\/jcs.02814","article-title":"Dystroglycan: From Biosynthesis to Pathogenesis of Human Disease","volume":"119","author":"Barresi","year":"2006","journal-title":"J. Cell Sci."},{"key":"ref_19","doi-asserted-by":"crossref","first-page":"165","DOI":"10.1038\/296165a0","article-title":"Effects of Duchenne Muscular Dystrophy on Muscle Protein Synthesis","volume":"296","author":"Rennie","year":"1982","journal-title":"Nature"},{"key":"ref_20","doi-asserted-by":"crossref","first-page":"1484","DOI":"10.1016\/0006-291X(92)90242-D","article-title":"Alterations of Protein Degradation and 2-D Protein Pattern in Muscle Cells of mdx and DMD Origin","volume":"189","author":"Rodemann","year":"1992","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"ref_21","doi-asserted-by":"crossref","first-page":"10909","DOI":"10.1074\/jbc.270.18.10909","article-title":"Calpains Are Activated in Necrotic Fibers from mdx Dystrophic Mice","volume":"270","author":"Spencer","year":"1995","journal-title":"J. Biol. Chem."},{"key":"ref_22","doi-asserted-by":"crossref","first-page":"1261","DOI":"10.1113\/jphysiol.2007.132191","article-title":"In Situ Measurements of Calpain Activity in Isolated Muscle Fibres from Normal and Dystrophin-Lacking mdx Mice","volume":"582","author":"Gailly","year":"2007","journal-title":"J. Physiol."},{"key":"ref_23","doi-asserted-by":"crossref","first-page":"595","DOI":"10.1007\/s004010000229","article-title":"Proteasome Expression in the Skeletal Muscles of Patients with Muscular Dystrophy","volume":"100","author":"Kumamoto","year":"2000","journal-title":"Acta Neuropathol."},{"key":"ref_24","doi-asserted-by":"crossref","first-page":"106","DOI":"10.1002\/(SICI)1097-4598(200001)23:1<106::AID-MUS14>3.0.CO;2-D","article-title":"Delay of Muscle Degeneration and Necrosis in mdx Mice by Calpain Inhibition","volume":"23","author":"Badalamente","year":"2000","journal-title":"Muscle Nerve"},{"key":"ref_25","doi-asserted-by":"crossref","first-page":"1663","DOI":"10.1016\/S0002-9440(10)63523-7","article-title":"Proteasome Inhibitor (MG-132) Treatment of mdx Mice Rescues the Expression and Membrane Localization of Dystrophin and Dystrophin-Associated Proteins","volume":"163","author":"Bonuccelli","year":"2003","journal-title":"Am. J. Pathol."},{"key":"ref_26","doi-asserted-by":"crossref","first-page":"1242","DOI":"10.4161\/cc.6.10.4182","article-title":"Localized Treatment with a Novel FDA-Approved Proteasome Inhibitor Blocks the Degradation of Dystrophin and Dystrophin-Associated Proteins in mdx Mice","volume":"6","author":"Bonuccelli","year":"2007","journal-title":"Cell Cycle"},{"key":"ref_27","doi-asserted-by":"crossref","first-page":"4190","DOI":"10.1096\/fj.07-099036","article-title":"Effect of Calpain and Proteasome Inhibition on Ca2+-Dependent Proteolysis and Muscle Histopathology in the mdx Mouse","volume":"22","author":"Briguet","year":"2008","journal-title":"FASEB J."},{"key":"ref_28","doi-asserted-by":"crossref","first-page":"237","DOI":"10.1016\/j.nmd.2006.01.013","article-title":"First Evaluation of the Potential Effectiveness in Muscular Dystrophy of a Novel Chimeric Compound, BN 82270, Acting as Calpain-Inhibitor and Anti-Oxidant","volume":"16","author":"Burdi","year":"2006","journal-title":"Neuromuscul. Disord."},{"key":"ref_29","doi-asserted-by":"crossref","unstructured":"Araujo, K.P.C., Bonuccelli, G., Duarte, C.N., Gaiad, T.P., Moreira, D.F., Feder, D., Belizario, J.E., Miglino, M.A., Lisanti, M.P., and Ambrosio, C.E. (2013). Bortezomib (PS-341) Treatment Decreases Inflammation and Partially Rescues the Expression of the Dystrophin-Glycoprotein Complex in GRMD Dogs. PLoS ONE, 8.","DOI":"10.1371\/journal.pone.0061367"},{"key":"ref_30","doi-asserted-by":"crossref","first-page":"11","DOI":"10.1111\/iep.12383","article-title":"Ixazomib, an Oral Proteasome Inhibitor, Exhibits Potential Effect in Dystrophin-Deficient mdx Mice","volume":"102","author":"Micheletto","year":"2021","journal-title":"Int. J. Exp. Pathol."},{"key":"ref_31","doi-asserted-by":"crossref","first-page":"1863","DOI":"10.2353\/ajpath.2010.090468","article-title":"Therapeutic Potential of Proteasome Inhibition in Duchenne and Becker Muscular Dystrophies","volume":"176","author":"Gazzerro","year":"2010","journal-title":"Am. J. Pathol."},{"key":"ref_32","doi-asserted-by":"crossref","unstructured":"Selsby, J., Morris, C., Morris, L., and Sweeney, L. (2012). A Proteasome Inhibitor Fails to Attenuate Dystrophic Pathology in mdx Mice. PLoS Curr., 4.","DOI":"10.1371\/4f84a944d8930"},{"key":"ref_33","doi-asserted-by":"crossref","first-page":"234","DOI":"10.1111\/apha.12114","article-title":"The Physiological Response of Protease Inhibition in Dystrophic Muscle","volume":"208","author":"Hollinger","year":"2013","journal-title":"Acta Physiol."},{"key":"ref_34","doi-asserted-by":"crossref","first-page":"5325","DOI":"10.1242\/jcs.114041","article-title":"Misregulation of Autophagy and Protein Degradation Systems in Myopathies and Muscular Dystrophies","volume":"126","author":"Sandri","year":"2013","journal-title":"J. Cell Sci."},{"key":"ref_35","doi-asserted-by":"crossref","first-page":"1431","DOI":"10.1007\/s00520-014-2552-1","article-title":"Treatment-Related Symptom Management in Patients with Multiple Myeloma: A Review","volume":"23","author":"Colson","year":"2015","journal-title":"Support. Care Cancer"},{"key":"ref_36","doi-asserted-by":"crossref","first-page":"251","DOI":"10.1007\/978-3-319-13150-4_10","article-title":"Treatment Strategies in Mantle Cell Lymphoma","volume":"165","author":"Maddocks","year":"2015","journal-title":"Cancer Treat. Res."},{"key":"ref_37","doi-asserted-by":"crossref","first-page":"353","DOI":"10.2146\/ajhp130281","article-title":"Carfilzomib: A Second-Generation Proteasome Inhibitor for the Treatment of Multiple Myeloma","volume":"72","author":"McBride","year":"2015","journal-title":"Am. J. Health Syst. Pharm."},{"key":"ref_38","doi-asserted-by":"crossref","first-page":"553","DOI":"10.1002\/mus.22125","article-title":"Regulation of the Calpain and Ubiquitin-Proteasome Systems in a Canine Model of Muscular Dystrophy","volume":"44","author":"Wadosky","year":"2011","journal-title":"Muscle Nerve"},{"key":"ref_39","doi-asserted-by":"crossref","first-page":"14440","DOI":"10.1073\/pnas.251541198","article-title":"Atrogin-1, a Muscle-Specific F-Box Protein Highly Expressed during Muscle Atrophy","volume":"98","author":"Gomes","year":"2001","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_40","doi-asserted-by":"crossref","first-page":"862","DOI":"10.1038\/labinvest.2016.63","article-title":"The Ubiquitin Ligase Tripartite-Motif-Protein 32 Is Induced in Duchenne Muscular Dystrophy","volume":"96","author":"Assereto","year":"2016","journal-title":"Lab. Investig."},{"key":"ref_41","doi-asserted-by":"crossref","unstructured":"Jeong, S.Y., Choi, J.H., Kim, J., Woo, J.S., and Lee, E.H. (2023). Tripartite Motif-Containing Protein 32 (TRIM32): What Does It Do for Skeletal Muscle?. Cells, 12.","DOI":"10.3390\/cells12162104"},{"key":"ref_42","doi-asserted-by":"crossref","first-page":"451","DOI":"10.1093\/hmg\/ddx414","article-title":"Mouse Models of Two Missense Mutations in Actin-Binding Domain 1 of Dystrophin Associated with Duchenne or Becker Muscular Dystrophy","volume":"27","author":"McCourt","year":"2018","journal-title":"Hum. Mol. Genet."},{"key":"ref_43","doi-asserted-by":"crossref","first-page":"1332","DOI":"10.1038\/s41556-020-00595-5","article-title":"The LncRNA H19 Alleviates Muscular Dystrophy by Stabilizing Dystrophin","volume":"22","author":"Zhang","year":"2020","journal-title":"Nat. Cell Biol."},{"key":"ref_44","doi-asserted-by":"crossref","first-page":"973","DOI":"10.1093\/hmg\/5.7.973","article-title":"A Cysteine 3340 Substitution in the Dystroglycan-Binding Domain of Dystrophin Associated with Duchenne Muscular Dystrophy, Mental Retardation and Absence of the ERG b-Wave","volume":"5","author":"Lenk","year":"1996","journal-title":"Hum. Mol. Genet."},{"key":"ref_45","doi-asserted-by":"crossref","first-page":"5419","DOI":"10.4049\/jimmunol.1101267","article-title":"IFN-\u03b3 Promotes Muscle Damage in the mdx Mouse Model of Duchenne Muscular Dystrophy by Suppressing M2 Macrophage Activation and Inhibiting Muscle Cell Proliferation","volume":"187","author":"Villalta","year":"2011","journal-title":"J. Immunol."},{"key":"ref_46","doi-asserted-by":"crossref","unstructured":"Tulangekar, A., and Sztal, T.E. (2021). Inflammation in Duchenne Muscular Dystrophy-Exploring the Role of Neutrophils in Muscle Damage and Regeneration. Biomedicines, 9.","DOI":"10.3390\/biomedicines9101366"},{"key":"ref_47","doi-asserted-by":"crossref","first-page":"96","DOI":"10.1128\/MCB.00622-13","article-title":"Identification of the Immunoproteasome as a Novel Regulator of Skeletal Muscle Differentiation","volume":"34","author":"Cui","year":"2014","journal-title":"Mol. Cell Biol."},{"key":"ref_48","doi-asserted-by":"crossref","first-page":"197","DOI":"10.1196\/annals.1341.018","article-title":"The Murine Cardiac 26S Proteasome: An Organelle Awaiting Exploration","volume":"1047","author":"Gomes","year":"2005","journal-title":"Ann. N. Y. Acad. Sci."},{"key":"ref_49","doi-asserted-by":"crossref","first-page":"74","DOI":"10.1016\/j.coi.2012.11.004","article-title":"The Immunoproteasome in Antigen Processing and Other Immunological Functions","volume":"25","author":"Basler","year":"2013","journal-title":"Curr. Opin. Immunol."},{"key":"ref_50","doi-asserted-by":"crossref","unstructured":"Liu, H.M., Ferrington, D.A., Baumann, C.W., and Thompson, L.V. (2016). Denervation-Induced Activation of the Standard Proteasome and Immunoproteasome. PLoS ONE, 11.","DOI":"10.1371\/journal.pone.0166831"},{"key":"ref_51","doi-asserted-by":"crossref","first-page":"191","DOI":"10.1007\/s10974-014-9385-x","article-title":"Immunoproteasome in Animal Models of Duchenne Muscular Dystrophy","volume":"35","author":"Chen","year":"2014","journal-title":"J. Muscle Res. Cell Motil."},{"key":"ref_52","doi-asserted-by":"crossref","first-page":"1898","DOI":"10.1038\/mt.2016.162","article-title":"Therapeutic Potential of Immunoproteasome Inhibition in Duchenne Muscular Dystrophy","volume":"24","author":"Farini","year":"2016","journal-title":"Mol. Ther."},{"key":"ref_53","doi-asserted-by":"crossref","unstructured":"Kwak, D., Wei, G., Thompson, L.V., and Kim, J.H. (2020). Short-Term ONX-0914 Administration: Performance and Muscle Phenotype in mdx Mice. Int. J. Environ. Res. Public. Health, 17.","DOI":"10.3390\/ijerph17145211"},{"key":"ref_54","doi-asserted-by":"crossref","unstructured":"Tripodi, L., Molinaro, D., Fortunato, F., Mella, C., Cassani, B., Torrente, Y., and Farini, A. (2022). Immunoproteasome Inhibition Ameliorates Aged Dystrophic Mouse Muscle Environment. Int. J. Mol. Sci., 23.","DOI":"10.3390\/ijms232314657"},{"key":"ref_55","doi-asserted-by":"crossref","first-page":"dmm044701","DOI":"10.1242\/dmm.044701","article-title":"Pathological Evaluation of Rats Carrying In-Frame Mutations in the Dystrophin Gene: A New Model of Becker Muscular Dystrophy","volume":"13","author":"Teramoto","year":"2020","journal-title":"DMM Dis. Models Mech."},{"key":"ref_56","doi-asserted-by":"crossref","first-page":"415","DOI":"10.1007\/s00418-004-0711-z","article-title":"Comparison of the Small Heat Shock Proteins \u03b1B-Crystallin, MKBP, HSP25, HSP20, and CvHSP in Heart and Skeletal Muscle","volume":"122","author":"Golenhofen","year":"2004","journal-title":"Histochem. Cell Biol."},{"key":"ref_57","doi-asserted-by":"crossref","first-page":"756","DOI":"10.1016\/j.jmb.2006.12.012","article-title":"Association of \u03b1B-Crystallin, a Small Heat Shock Protein, with Actin: Role in Modulating Actin Filament Dynamics in Vivo","volume":"366","author":"Singh","year":"2007","journal-title":"J. Mol. Biol."},{"key":"ref_58","doi-asserted-by":"crossref","unstructured":"Wattin, M., Gaweda, L., Muller, P., Baritaud, M., Scholtes, C., Lozano, C., Gieseler, K., and Kretz-Remy, C. (2018). Modulation of Protein Quality Control and Proteasome to Autophagy Switch in Immortalized Myoblasts from Duchenne Muscular Dystrophy Patients. Int. J. Mol. Sci., 19.","DOI":"10.3390\/ijms19010178"},{"key":"ref_59","doi-asserted-by":"crossref","first-page":"395","DOI":"10.1002\/humu.22758","article-title":"The TREAT-NMD DMD Global Database: Analysis of More than 7000 Duchenne Muscular Dystrophy Mutations","volume":"36","author":"Bladen","year":"2015","journal-title":"Hum. Mutat."},{"key":"ref_60","doi-asserted-by":"crossref","unstructured":"Gatto, F., Benemei, S., Piluso, G., and Bello, L. (2024). The Complex Landscape of DMD Mutations: Moving towards Personalized Medicine. Front. Genet., 15.","DOI":"10.3389\/fgene.2024.1360224"},{"key":"ref_61","doi-asserted-by":"crossref","first-page":"12414","DOI":"10.1073\/pnas.1508755112","article-title":"Disease-Proportional Proteasomal Degradation of Missense Dystrophins","volume":"112","author":"Talsness","year":"2015","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_62","doi-asserted-by":"crossref","first-page":"917","DOI":"10.2119\/molmed.2010.00256","article-title":"Rapamycin Ameliorates Dystrophic Phenotype in mdx Mouse Skeletal Muscle","volume":"17","author":"Eghtesad","year":"2011","journal-title":"Mol. Med."},{"key":"ref_63","doi-asserted-by":"crossref","first-page":"e418","DOI":"10.1038\/cddis.2012.159","article-title":"Autophagy as a New Therapeutic Target in Duchenne Muscular Dystrophy","volume":"3","author":"Morisi","year":"2012","journal-title":"Cell Death Dis."},{"key":"ref_64","doi-asserted-by":"crossref","unstructured":"Spitali, P., Grumati, P., Hiller, M., Chrisam, M., Aartsma-Rus, A., and Bonaldo, P. (2013). Autophagy Is Impaired in the Tibialis Anterior of Dystrophin Null Mice. PLoS Curr., 5.","DOI":"10.1371\/currents.md.e1226cefa851a2f079bbc406c0a21e80"},{"key":"ref_65","doi-asserted-by":"crossref","first-page":"1021","DOI":"10.1016\/j.mehy.2015.08.015","article-title":"Revisiting the Dystrophin-ATP Connection: How Half a Century of Research Still Implicates Mitochondrial Dysfunction in Duchenne Muscular Dystrophy Aetiology","volume":"85","author":"Timpani","year":"2015","journal-title":"Med. Hypotheses"},{"key":"ref_66","doi-asserted-by":"crossref","first-page":"C718","DOI":"10.1152\/ajpcell.00249.2022","article-title":"Mitochondrial Stress Responses in Duchenne Muscular Dystrophy: Metabolic Dysfunction or Adaptive Reprogramming?","volume":"323","author":"Bellissimo","year":"2022","journal-title":"Am. J. Physiol. Cell Physiol."},{"key":"ref_67","doi-asserted-by":"crossref","first-page":"e22851","DOI":"10.1096\/fj.202201489RR","article-title":"Increased Mitochondrial Ca2+ Contributes to Health Decline with Age and Duchene Muscular Dystrophy in C. elegans","volume":"37","author":"Higashitani","year":"2023","journal-title":"FASEB J."},{"key":"ref_68","doi-asserted-by":"crossref","unstructured":"Moore, T.M., Lin, A.J., Strumwasser, A.R., Cory, K., Whitney, K., Ho, T., Ho, T., Lee, J.L., Rucker, D.H., and Nguyen, C.Q. (2020). Mitochondrial Dysfunction Is an Early Consequence of Partial or Complete Dystrophin Loss in mdx Mice. Front. Physiol., 11.","DOI":"10.3389\/fphys.2020.00690"},{"key":"ref_69","doi-asserted-by":"crossref","first-page":"eabb0319","DOI":"10.1126\/scitranslmed.abb0319","article-title":"Urolithin A Improves Muscle Function by Inducing Mitophagy in Muscular Dystrophy","volume":"13","author":"Luan","year":"2021","journal-title":"Sci. Transl. Med."},{"key":"ref_70","doi-asserted-by":"crossref","first-page":"2047","DOI":"10.1096\/fj.13-237388","article-title":"Rapamycin Nanoparticles Target Defective Autophagy in Muscular Dystrophy to Enhance Both Strength and Cardiac Function","volume":"28","author":"Bibee","year":"2014","journal-title":"FASEB J."},{"key":"ref_71","doi-asserted-by":"crossref","first-page":"9179270","DOI":"10.1155\/2018\/9179270","article-title":"Resveratrol Decreases Oxidative Stress by Restoring Mitophagy and Improves the Pathophysiology of Dystrophin-Deficient mdx Mice","volume":"2018","author":"Sebori","year":"2018","journal-title":"Oxid. Med. Cell Longev."},{"key":"ref_72","doi-asserted-by":"crossref","first-page":"8408574","DOI":"10.1155\/2023\/8408574","article-title":"TRIM72 Alleviates Muscle Inflammation in mdx Mice via Promoting Mitophagy-Mediated NLRP3 Inflammasome Inactivation","volume":"2023","author":"Wu","year":"2023","journal-title":"Oxid. Med. Cell Longev."},{"key":"ref_73","doi-asserted-by":"crossref","first-page":"1039","DOI":"10.1038\/s44318-024-00356-2","article-title":"Two FAM134B Isoforms Differentially Regulate ER Dynamics during Myogenesis","volume":"44","author":"Buonomo","year":"2025","journal-title":"EMBO J."},{"key":"ref_74","doi-asserted-by":"crossref","first-page":"575","DOI":"10.1002\/jcp.20696","article-title":"Regulation of Phosphatidylinositol 3-Kinase (PI3K)\/Akt and Nuclear Factor-Kappa B Signaling Pathways in Dystrophin-Deficient Skeletal Muscle in Response to Mechanical Stretch","volume":"208","author":"Dogra","year":"2006","journal-title":"J. Cell Physiol."},{"key":"ref_75","doi-asserted-by":"crossref","first-page":"2580","DOI":"10.1016\/j.yexcr.2006.04.024","article-title":"Hypertrophic Response of Duchenne and Limb-Girdle Muscular Dystrophies Is Associated with Activation of Akt Pathway","volume":"312","author":"Peter","year":"2006","journal-title":"Exp. Cell Res."},{"key":"ref_76","doi-asserted-by":"crossref","first-page":"1009","DOI":"10.1038\/ncb1101-1009","article-title":"Mediation of IGF-1-Induced Skeletal Myotube Hypertrophy by PI(3)K\/Akt\/MTOR and PI(3)K\/Akt\/GSK3 Pathways","volume":"3","author":"Rommel","year":"2001","journal-title":"Nat. Cell Biol."},{"key":"ref_77","doi-asserted-by":"crossref","first-page":"1014","DOI":"10.1038\/ncb1101-1014","article-title":"Akt\/MTOR Pathway Is a Crucial Regulator of Skeletal Muscle Hypertrophy and Can Prevent Muscle Atrophy in Vivo","volume":"3","author":"Bodine","year":"2001","journal-title":"Nat. Cell Biol."},{"key":"ref_78","doi-asserted-by":"crossref","first-page":"318","DOI":"10.1093\/hmg\/ddn358","article-title":"Myogenic Akt Signaling Upregulates the Utrophin-Glycoprotein Complex and Promotes Sarcolemma Stability in Muscular Dystrophy","volume":"18","author":"Peter","year":"2009","journal-title":"Hum. Mol. Genet."},{"key":"ref_79","doi-asserted-by":"crossref","first-page":"471","DOI":"10.1016\/j.cell.2006.01.016","article-title":"TOR Signaling in Growth and Metabolism","volume":"124","author":"Wullschleger","year":"2006","journal-title":"Cell"},{"key":"ref_80","doi-asserted-by":"crossref","first-page":"274","DOI":"10.1016\/j.cell.2012.03.017","article-title":"MTOR Signaling in Growth Control and Disease","volume":"149","author":"Laplante","year":"2012","journal-title":"Cell"},{"key":"ref_81","doi-asserted-by":"crossref","first-page":"211","DOI":"10.1016\/S0014-5793(97)00240-8","article-title":"Insulin Activates Protein Kinase B, Inhibits Glycogen Synthase Kinase-3 and Activates Glycogen Synthase by Rapamycin-Insensitive Pathways in Skeletal Muscle and Adipose Tissue","volume":"406","author":"Cross","year":"1997","journal-title":"FEBS Lett."},{"key":"ref_82","doi-asserted-by":"crossref","first-page":"134","DOI":"10.1016\/j.yexcr.2015.07.005","article-title":"PI3K\/SGK1\/GSK3\u03b2 Signaling Pathway Is Involved in Inhibition of Autophagy in Neonatal Rat Cardiomyocytes Exposed to Hypoxia\/Reoxygenation by Hydrogen Sulfide","volume":"345","author":"Jiang","year":"2016","journal-title":"Exp. Cell Res."},{"key":"ref_83","doi-asserted-by":"crossref","first-page":"132","DOI":"10.1038\/ncb2152","article-title":"AMPK and MTOR Regulate Autophagy through Direct Phosphorylation of Ulk1","volume":"13","author":"Kim","year":"2011","journal-title":"Nat. Cell Biol."},{"key":"ref_84","doi-asserted-by":"crossref","first-page":"695","DOI":"10.1002\/jcb.23399","article-title":"AMPK Promotes Skeletal Muscle Autophagy through Activation of Forkhead FoxO3a and Interaction with Ulk1","volume":"113","author":"Sanchez","year":"2012","journal-title":"J. Cell Biochem."},{"key":"ref_85","doi-asserted-by":"crossref","first-page":"583","DOI":"10.1016\/j.ajpath.2012.04.004","article-title":"AMPK Activation Stimulates Autophagy and Ameliorates Muscular Dystrophy in the mdx Mouse Diaphragm","volume":"181","author":"Pauly","year":"2012","journal-title":"Am. J. Pathol."},{"key":"ref_86","doi-asserted-by":"crossref","first-page":"C110","DOI":"10.1152\/ajpcell.00183.2011","article-title":"Chronic AMPK Stimulation Attenuates Adaptive Signaling in Dystrophic Skeletal Muscle","volume":"302","author":"Ljubicic","year":"2012","journal-title":"Am. J. Physiol. Cell Physiol."},{"key":"ref_87","doi-asserted-by":"crossref","first-page":"e12944","DOI":"10.1111\/apha.12944","article-title":"Autophagic Dysfunction and Autophagosome Escape in the mdx Mus musculus Model of Duchenne Muscular Dystrophy","volume":"222","author":"Spaulding","year":"2018","journal-title":"Acta Physiol."},{"key":"ref_88","doi-asserted-by":"crossref","first-page":"1429","DOI":"10.1126\/science.1204592","article-title":"TFEB Links Autophagy to Lysosomal Biogenesis","volume":"332","author":"Settembre","year":"2011","journal-title":"Science"},{"key":"ref_89","doi-asserted-by":"crossref","first-page":"6670","DOI":"10.1038\/ncomms7670","article-title":"Regulation of Autophagy and the Ubiquitin-Proteasome System by the FoxO Transcriptional Network during Muscle Atrophy","volume":"6","author":"Milan","year":"2015","journal-title":"Nat. Commun."},{"key":"ref_90","doi-asserted-by":"crossref","first-page":"857","DOI":"10.1016\/S0092-8674(00)80595-4","article-title":"Akt Promotes Cell Survival by Phosphorylating and Inhibiting a Forkhead Transcription Factor","volume":"96","author":"Brunet","year":"1999","journal-title":"Cell"},{"key":"ref_91","doi-asserted-by":"crossref","first-page":"16741","DOI":"10.1074\/jbc.274.24.16741","article-title":"Negative Regulation of the Forkhead Transcription Factor FKHR by Akt","volume":"274","author":"Tang","year":"1999","journal-title":"J. Biol. Chem."},{"key":"ref_92","doi-asserted-by":"crossref","first-page":"1095","DOI":"10.1038\/emboj.2012.32","article-title":"A Lysosome-to-Nucleus Signalling Mechanism Senses and Regulates the Lysosome via MTOR and TFEB","volume":"31","author":"Settembre","year":"2012","journal-title":"EMBO J."},{"key":"ref_93","doi-asserted-by":"crossref","first-page":"903","DOI":"10.4161\/auto.19653","article-title":"MTORC1 Functions as a Transcriptional Regulator of Autophagy by Preventing Nuclear Transport of TFEB","volume":"8","author":"Martina","year":"2012","journal-title":"Autophagy"},{"key":"ref_94","doi-asserted-by":"crossref","first-page":"464","DOI":"10.1080\/15548627.2016.1271514","article-title":"Multistep Regulation of TFEB by MTORC1","volume":"13","author":"Konda","year":"2017","journal-title":"Autophagy"},{"key":"ref_95","doi-asserted-by":"crossref","unstructured":"Nakashima, R., Hosoda, R., Tatekoshi, Y., Iwahara, N., Saga, Y., and Kuno, A. (2024). Transcriptional Dysregulation of Autophagy in the Muscle of a Mouse Model of Duchenne Muscular Dystrophy. Sci. Rep., 14.","DOI":"10.1038\/s41598-024-51746-9"},{"key":"ref_96","doi-asserted-by":"crossref","first-page":"439","DOI":"10.1016\/j.bbadis.2011.01.002","article-title":"Activation of AKT Signaling Promotes Cell Growth and Survival in A7\u03b21 Integrin-Mediated Alleviation of Muscular Dystrophy","volume":"1812","author":"Boppart","year":"2011","journal-title":"Biochim. Biophys. Acta"},{"key":"ref_97","doi-asserted-by":"crossref","first-page":"1571","DOI":"10.1016\/j.ajpath.2024.04.006","article-title":"Leucyl-TRNA Synthetase Contributes to Muscle Weakness through Mammalian Target of Rapamycin Complex 1 Activation and Autophagy Suppression in a Mouse Model of Duchenne Muscular Dystrophy","volume":"194","author":"You","year":"2024","journal-title":"Am. J. Pathol."},{"key":"ref_98","doi-asserted-by":"crossref","first-page":"952","DOI":"10.1128\/MCB.21.3.952-965.2001","article-title":"Protein Kinase SGK Mediates Survival Signals by Phosphorylating the Forkhead Transcription Factor FKHRL1 (FOXO3a)","volume":"21","author":"Brunet","year":"2001","journal-title":"Mol. Cell Biol."},{"key":"ref_99","doi-asserted-by":"crossref","first-page":"2479","DOI":"10.1242\/jcs.001222","article-title":"Dynamic FoxO Transcription Factors","volume":"120","author":"Huang","year":"2007","journal-title":"J. Cell Sci."},{"key":"ref_100","doi-asserted-by":"crossref","first-page":"20589","DOI":"10.1074\/jbc.M412357200","article-title":"Nuclear Trapping of the Forkhead Transcription Factor FoxO1 via Sirt-Dependent Deacetylation Promotes Expression of Glucogenetic Genes","volume":"280","author":"Frescas","year":"2005","journal-title":"J. Biol. Chem."},{"key":"ref_101","doi-asserted-by":"crossref","first-page":"44","DOI":"10.1016\/j.stemcr.2014.04.015","article-title":"Aging-like Phenotype and Defective Lineage Specification in SIRT1-Deleted Hematopoietic Stem and Progenitor Cells","volume":"3","author":"Bigarella","year":"2014","journal-title":"Stem Cell Rep."},{"key":"ref_102","doi-asserted-by":"crossref","unstructured":"Kuno, A., Hosoda, R., Sebori, R., Hayashi, T., Sakuragi, H., Tanabe, M., and Horio, Y. (2018). Resveratrol Ameliorates Mitophagy Disturbance and Improves Cardiac Pathophysiology of Dystrophin-Deficient mdx Mice. Sci. Rep., 8.","DOI":"10.1038\/s41598-018-33930-w"},{"key":"ref_103","doi-asserted-by":"crossref","first-page":"2","DOI":"10.1186\/s13395-024-00371-1","article-title":"Aminoguanidine Hemisulfate Improves Mitochondrial Autophagy, Oxidative Stress, and Muscle Force in Duchenne Muscular Dystrophy via the AKT\/FOXO1 Pathway in mdx Mice","volume":"15","author":"Sun","year":"2025","journal-title":"Skelet. Muscle"},{"key":"ref_104","doi-asserted-by":"crossref","first-page":"1381","DOI":"10.1038\/s41467-020-14895-9","article-title":"A Signaling Hub of Insulin Receptor, Dystrophin Glycoprotein Complex and Plakoglobin Regulates Muscle Size","volume":"11","author":"Aweida","year":"2020","journal-title":"Nat. Commun."},{"key":"ref_105","doi-asserted-by":"crossref","first-page":"644","DOI":"10.1002\/mus.10258","article-title":"Inhibition of Dystroglycan Binding to Laminin Disrupts the PI3K\/AKT Pathway and Survival Signaling in Muscle Cells","volume":"26","author":"Langenbach","year":"2002","journal-title":"Muscle Nerve"},{"key":"ref_106","doi-asserted-by":"crossref","first-page":"402","DOI":"10.1002\/jcp.21684","article-title":"Dystrophin Glycoprotein Complex-Associated G\u03b2\u03b3 Subunits Activate Phosphatidylinositol-3-Kinase\/Akt Signaling in Skeletal Muscle in a Laminin-Dependent Manner","volume":"219","author":"Xiong","year":"2009","journal-title":"J. Cell Physiol."},{"key":"ref_107","doi-asserted-by":"crossref","first-page":"1207","DOI":"10.1083\/jcb.152.6.1207","article-title":"Enhanced Expression of the \u03b17\u03b21 Integrin Reduces Muscular Dystrophy and Restores Viability in Dystrophic Mice","volume":"152","author":"Burkin","year":"2001","journal-title":"J. Cell Biol."},{"key":"ref_108","doi-asserted-by":"crossref","first-page":"2873","DOI":"10.1242\/jcs.110.22.2873","article-title":"Altered Expression of the \u03b17\u03b21 Integrin in Human and Murine Muscular Dystrophies","volume":"110","author":"Hodges","year":"1997","journal-title":"J. Cell Sci."},{"key":"ref_109","doi-asserted-by":"crossref","first-page":"209","DOI":"10.1016\/S0012-1606(03)00304-X","article-title":"The Muscle Integrin Binding Protein (MIBP) Interacts with \u03b17\u03b21 Integrin and Regulates Cell Adhesion and Laminin Matrix Deposition","volume":"261","author":"Li","year":"2003","journal-title":"Dev. Biol."},{"key":"ref_110","doi-asserted-by":"crossref","first-page":"350","DOI":"10.1016\/S0960-8966(00)00203-0","article-title":"Massive Muscle Cell Degeneration in the Early Stage of Merosin-Deficient Congenital Muscular Dystrophy","volume":"11","author":"Hayashi","year":"2001","journal-title":"Neuromuscul. Disord."},{"key":"ref_111","doi-asserted-by":"crossref","first-page":"33","DOI":"10.1016\/S0014-5793(97)01007-7","article-title":"Laminin \u03b12 Chain-Null Mutant Mice by Targeted Disruption of the Lama2 Gene: A New Model of Merosin (Laminin 2)-Deficient Congenital Muscular Dystrophy","volume":"415","author":"Miyagoe","year":"1997","journal-title":"FEBS Lett."},{"key":"ref_112","doi-asserted-by":"crossref","first-page":"C1660-5","DOI":"10.1152\/ajpcell.00317.2005","article-title":"\u03b17\u03b21-Integrin Regulates Mechanotransduction and Prevents Skeletal Muscle Injury","volume":"290","author":"Boppart","year":"2006","journal-title":"Am. J. Physiol. Cell Physiol."},{"key":"ref_113","doi-asserted-by":"crossref","first-page":"jcs230425","DOI":"10.1242\/jcs.230425","article-title":"YAP\/TAZ Functions and Their Regulation at a Glance","volume":"133","author":"Pocaterra","year":"2020","journal-title":"J. Cell Sci."},{"key":"ref_114","doi-asserted-by":"crossref","first-page":"577","DOI":"10.1146\/annurev-biochem-013118-111829","article-title":"The Hippo Pathway: Biology and Pathophysiology","volume":"88","author":"Ma","year":"2019","journal-title":"Annu. Rev. Biochem."},{"key":"ref_115","doi-asserted-by":"crossref","first-page":"802","DOI":"10.1038\/nrm3896","article-title":"Mechanotransduction and Extracellular Matrix Homeostasis","volume":"15","author":"Humphrey","year":"2014","journal-title":"Nat. Rev. Mol. Cell Biol."},{"key":"ref_116","doi-asserted-by":"crossref","first-page":"888","DOI":"10.1038\/s41556-018-0142-z","article-title":"YAP\/TAZ Upstream Signals and Downstream Responses","volume":"20","author":"Totaro","year":"2018","journal-title":"Nat. Cell Biol."},{"key":"ref_117","doi-asserted-by":"crossref","first-page":"6048","DOI":"10.1038\/ncomms7048","article-title":"The Hippo Pathway Effector YAP Is a Critical Regulator of Skeletal Muscle Fibre Size","volume":"6","author":"Watt","year":"2015","journal-title":"Nat. Commun."},{"key":"ref_118","doi-asserted-by":"crossref","first-page":"C48","DOI":"10.1152\/ajpcell.00432.2018","article-title":"Differential YAP Nuclear Signaling in Healthy and Dystrophic Skeletal Muscle","volume":"317","author":"Iyer","year":"2019","journal-title":"Am. J. Physiol. Cell Physiol."},{"key":"ref_119","doi-asserted-by":"crossref","first-page":"E41","DOI":"10.1152\/ajpendo.00389.2012","article-title":"Muscle Protein Synthesis, MTORC1\/MAPK\/Hippo Signaling, and Capillary Density Are Altered by Blocking of Myostatin and Activins","volume":"304","author":"Hulmi","year":"2013","journal-title":"Am. J. Physiol. Endocrinol. Metab."},{"key":"ref_120","doi-asserted-by":"crossref","unstructured":"Vita, G.L., Polito, F., Oteri, R., Arrigo, R., Ciranni, A.M., Musumeci, O., Messina, S., Rodolico, C., Di Giorgio, R.M., and Vita, G. (2018). Hippo Signaling Pathway Is Altered in Duchenne Muscular Dystrophy. PLoS ONE, 13.","DOI":"10.1371\/journal.pone.0205514"},{"key":"ref_121","doi-asserted-by":"crossref","first-page":"e2205536119","DOI":"10.1073\/pnas.2205536119","article-title":"Dystrophin Missense Mutations Alter Focal Adhesion Tension and Mechanotransduction","volume":"119","author":"Ramirez","year":"2022","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_122","doi-asserted-by":"crossref","first-page":"263","DOI":"10.5607\/en21008","article-title":"Altered Gene Expression Profiles in Neural Stem Cells Derived from Duchenne Muscular Dystrophy Patients with Intellectual Disability","volume":"30","author":"Koo","year":"2021","journal-title":"Exp. Neurobiol."},{"key":"ref_123","doi-asserted-by":"crossref","first-page":"17848","DOI":"10.1073\/pnas.1908228116","article-title":"Cell Phenotypic Plasticity Requires Autophagic Flux Driven by YAP\/TAZ Mechanotransduction","volume":"116","author":"Totaro","year":"2019","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_124","doi-asserted-by":"crossref","first-page":"15","DOI":"10.1016\/j.devcel.2013.03.005","article-title":"The TBC\/RabGAP Armus Coordinates Rac1 and Rab7 Functions during Autophagy","volume":"25","author":"Carroll","year":"2013","journal-title":"Dev. Cell"},{"key":"ref_125","doi-asserted-by":"crossref","first-page":"3044","DOI":"10.1128\/MCB.00085-15","article-title":"Leucine-Rich Repeat Kinase 1 Regulates Autophagy through Turning On TBC1D2-Dependent Rab7 Inactivation","volume":"35","author":"Toyofuku","year":"2015","journal-title":"Mol. Cell Biol."},{"key":"ref_126","doi-asserted-by":"crossref","first-page":"1717","DOI":"10.1242\/jcs.113.10.1717","article-title":"Adhesion-Dependent Tyrosine Phosphorylation of \u03b2-Dystroglycan Regulates Its Interaction with Utrophin","volume":"113","author":"James","year":"2000","journal-title":"J. Cell Sci."},{"key":"ref_127","doi-asserted-by":"crossref","first-page":"227","DOI":"10.1038\/nature22979","article-title":"Dystrophin-Glycoprotein Complex Sequesters Yap to Inhibit Cardiomyocyte Proliferation","volume":"547","author":"Morikawa","year":"2017","journal-title":"Nature"},{"key":"ref_128","doi-asserted-by":"crossref","first-page":"7110","DOI":"10.1021\/bi0271289","article-title":"Localization of Phospho-\u03b2-Dystroglycan (PY892) to an Intracellular Vesicular Compartment in Cultured Cells and Skeletal Muscle Fibers in Vivo","volume":"42","author":"Sotgia","year":"2003","journal-title":"Biochemistry"},{"key":"ref_129","doi-asserted-by":"crossref","first-page":"179","DOI":"10.1038\/nature22978","article-title":"The Extracellular Matrix Protein Agrin Promotes Heart Regeneration in Mice","volume":"547","author":"Bassat","year":"2017","journal-title":"Nature"},{"key":"ref_130","doi-asserted-by":"crossref","first-page":"130","DOI":"10.1016\/j.matbio.2015.02.005","article-title":"Role of Gelatinases in Pathological and Physiological Processes Involving the Dystrophin-Glycoprotein Complex","volume":"44\u201346","author":"Bozzi","year":"2015","journal-title":"Matrix Biol."},{"key":"ref_131","doi-asserted-by":"crossref","first-page":"103","DOI":"10.1016\/j.ceb.2015.08.005","article-title":"Rho GTPase Signalling in Cell Migration","volume":"36","author":"Ridley","year":"2015","journal-title":"Curr. Opin. Cell Biol."},{"key":"ref_132","doi-asserted-by":"crossref","unstructured":"Schmidt, S.I., Blaabjerg, M., Freude, K., and Meyer, M. (2022). RhoA Signaling in Neurodegenerative Diseases. Cells, 11.","DOI":"10.3390\/cells11091520"},{"key":"ref_133","doi-asserted-by":"crossref","first-page":"9","DOI":"10.1016\/j.brainres.2015.12.002","article-title":"Fasudil, a Rho Kinase Inhibitor, Promotes the Autophagic Degradation of A53T \u03b1-Synuclein by Activating the JNK 1\/Bcl-2\/Beclin 1 Pathway","volume":"1632","author":"Liu","year":"2016","journal-title":"Brain Res."},{"key":"ref_134","doi-asserted-by":"crossref","first-page":"2694","DOI":"10.1016\/j.cellsig.2014.08.019","article-title":"The Role of PI3K\/AKT\/MTOR Pathway in the Modulation of Autophagy and the Clearance of Protein Aggregates in Neurodegeneration","volume":"26","year":"2014","journal-title":"Cell Signal"},{"key":"ref_135","doi-asserted-by":"crossref","first-page":"341","DOI":"10.1007\/s004410000243","article-title":"Small Guanosine Triphosphatase Rho\/Rho-Associated Kinase as a Novel Regulator of Intracellular Redistribution of Lysosomes in Invasive Tumor Cells","volume":"301","author":"Nishimura","year":"2000","journal-title":"Cell Tissue Res."},{"key":"ref_136","doi-asserted-by":"crossref","first-page":"189","DOI":"10.1023\/A:1021702812146","article-title":"A Role for Small GTPase RhoA in Regulating Intracellular Membrane Traffic of Lysosomes in Invasive Rat Hepatoma Cells","volume":"34","author":"Nishimura","year":"2002","journal-title":"Histochem. J."},{"key":"ref_137","doi-asserted-by":"crossref","first-page":"1880","DOI":"10.1002\/jcsm.13278","article-title":"RhoA\/ROCK Signalling Activated by ARHGEF3 Promotes Muscle Weakness via Autophagy in Dystrophic mdx Mice","volume":"14","author":"You","year":"2023","journal-title":"J. Cachexia Sarcopenia Muscle"},{"key":"ref_138","doi-asserted-by":"crossref","first-page":"3619","DOI":"10.1096\/fj.13-233460","article-title":"RhoA Mediates Defective Stem Cell Function and Heterotopic Ossification in Dystrophic Muscle of Mice","volume":"27","author":"Mu","year":"2013","journal-title":"FASEB J."},{"key":"ref_139","doi-asserted-by":"crossref","first-page":"1373","DOI":"10.1002\/jcsm.12923","article-title":"RhoA\/ROCK2 Signalling Is Enhanced by PDGF-AA in Fibro-Adipogenic Progenitor Cells: Implications for Duchenne Muscular Dystrophy","volume":"13","author":"Pons","year":"2022","journal-title":"J. Cachexia Sarcopenia Muscle"},{"key":"ref_140","doi-asserted-by":"crossref","first-page":"11711","DOI":"10.1074\/jbc.270.20.11711","article-title":"SH3 Domain-Mediated Interaction of Dystroglycan and Grb2","volume":"270","author":"Yang","year":"1995","journal-title":"J. Biol. Chem."},{"key":"ref_141","doi-asserted-by":"crossref","first-page":"C500","DOI":"10.1152\/ajpcell.00529.2001","article-title":"Dystrophin-Glycoprotein Complex and Ras and Rho GTPase Signaling Are Altered in Muscle Atrophy","volume":"283","author":"Chockalingam","year":"2002","journal-title":"Am. J. Physiol. Cell Physiol."},{"key":"ref_142","doi-asserted-by":"crossref","first-page":"39287","DOI":"10.1074\/jbc.M305551200","article-title":"Skeletal Muscle Signaling Pathway through the Dystrophin Glycoprotein Complex and Rac1","volume":"278","author":"Oak","year":"2003","journal-title":"J. Biol. Chem."},{"key":"ref_143","doi-asserted-by":"crossref","first-page":"1378","DOI":"10.1042\/BST20120103","article-title":"Rho Family GTPases","volume":"40","author":"Hall","year":"2012","journal-title":"Biochem. Soc. Trans."},{"key":"ref_144","doi-asserted-by":"crossref","first-page":"654","DOI":"10.1016\/j.stem.2019.08.007","article-title":"Wnt4 from the Niche Controls the Mechano-Properties and Quiescent State of Muscle Stem Cells","volume":"25","author":"Eliazer","year":"2019","journal-title":"Cell Stem Cell"},{"key":"ref_145","doi-asserted-by":"crossref","first-page":"1509","DOI":"10.2353\/ajpath.2008.071009","article-title":"L-Arginine Decreases Inflammation and Modulates the Nuclear Factor-KappaB\/Matrix Metalloproteinase Cascade in mdx Muscle Fibers","volume":"172","author":"Hnia","year":"2008","journal-title":"Am. J. Pathol."},{"key":"ref_146","doi-asserted-by":"crossref","first-page":"102","DOI":"10.1096\/fj.03-0453com","article-title":"Loss of Dystrophin Causes Aberrant Mechanotransduction in Skeletal Muscle Fibers","volume":"18","author":"Kumar","year":"2004","journal-title":"FASEB J."},{"key":"ref_147","doi-asserted-by":"crossref","first-page":"503","DOI":"10.1177\/153537020422900608","article-title":"Altered Activity of Signaling Pathways in Diaphragm and Tibialis Anterior Muscle of Dystrophic Mice","volume":"229","author":"Lang","year":"2004","journal-title":"Exp. Biol. Med."},{"key":"ref_148","doi-asserted-by":"crossref","first-page":"1278","DOI":"10.1016\/S0960-9822(01)00397-9","article-title":"Activation of JNK1 Contributes to Dystrophic Muscle Pathogenesis","volume":"11","author":"Kolodziejczyk","year":"2001","journal-title":"Curr. Biol."},{"key":"ref_149","doi-asserted-by":"crossref","first-page":"1937","DOI":"10.1096\/fj.04-1859fje","article-title":"Glucocorticoid Treatment Alleviates Dystrophic Myofiber Pathology by Activation of the Calcineurin\/NF-AT Pathway","volume":"18","author":"Chakkalakal","year":"2004","journal-title":"FASEB J."},{"key":"ref_150","doi-asserted-by":"crossref","first-page":"326","DOI":"10.1016\/j.bbadis.2004.12.003","article-title":"Up-Regulation of Mitogen Activated Protein Kinases in mdx Skeletal Muscle Following Chronic Treadmill Exercise","volume":"1740","author":"Nakamura","year":"2005","journal-title":"Biochim. Biophys. Acta"},{"key":"ref_151","doi-asserted-by":"crossref","first-page":"484","DOI":"10.1038\/sj.embor.7400140","article-title":"Dystroglycan, a Scaffold for the ERK-MAP Kinase Cascade","volume":"5","author":"Spence","year":"2004","journal-title":"EMBO Rep."},{"key":"ref_152","doi-asserted-by":"crossref","unstructured":"Huang, Y., Zhen, Y., Chen, Y., Sui, S., and Zhang, L. (2023). Unraveling the Interplay between RAS\/RAF\/MEK\/ERK Signaling Pathway and Autophagy in Cancer: From Molecular Mechanisms to Targeted Therapy. Biochem. Pharmacol., 217.","DOI":"10.1016\/j.bcp.2023.115842"},{"key":"ref_153","doi-asserted-by":"crossref","first-page":"21412","DOI":"10.1074\/jbc.M109.026013","article-title":"A Non-Canonical MEK\/ERK Signaling Pathway Regulates Autophagy via Regulating Beclin 1","volume":"284","author":"Wang","year":"2009","journal-title":"J. Biol. Chem."},{"key":"ref_154","doi-asserted-by":"crossref","unstructured":"Wei, Z., Hu, X., Wu, Y., Zhou, L., Zhao, M., and Lin, Q. (2024). Molecular Mechanisms Underlying Initiation and Activation of Autophagy. Biomolecules, 14.","DOI":"10.3390\/biom14121517"},{"key":"ref_155","doi-asserted-by":"crossref","first-page":"620","DOI":"10.1038\/s41591-019-0367-9","article-title":"Protective Autophagy Elicited by RAF\u2192MEK\u2192ERK Inhibition Suggests a Treatment Strategy for RAS-Driven Cancers","volume":"25","author":"Kinsey","year":"2019","journal-title":"Nat. Med."},{"key":"ref_156","doi-asserted-by":"crossref","first-page":"89","DOI":"10.1016\/j.canlet.2011.11.015","article-title":"Targeting Cathepsin S Induces Tumor Cell Autophagy via the EGFR-ERK Signaling Pathway","volume":"317","author":"Chen","year":"2012","journal-title":"Cancer Lett."},{"key":"ref_157","doi-asserted-by":"crossref","first-page":"340","DOI":"10.1016\/j.yexcr.2014.08.001","article-title":"Raf\/MEK\/ERK Can Regulate Cellular Levels of LC3B and SQSTM1\/P62 at Expression Levels","volume":"327","author":"Kim","year":"2014","journal-title":"Exp. Cell Res."},{"key":"ref_158","doi-asserted-by":"crossref","first-page":"458","DOI":"10.1002\/jcp.1041520304","article-title":"Cytoskeletal Elements Are Required for the Formation and Maturation of Autophagic Vacuoles","volume":"152","author":"Aplin","year":"1992","journal-title":"J. Cell Physiol."},{"key":"ref_159","doi-asserted-by":"crossref","first-page":"5843","DOI":"10.1091\/mbc.e05-07-0629","article-title":"The Actin Cytoskeleton Is Required for Selective Types of Autophagy, but Not Nonspecific Autophagy, in the Yeast Saccharomyces cerevisiae","volume":"16","author":"Reggiori","year":"2005","journal-title":"Mol. Biol. Cell"},{"key":"ref_160","doi-asserted-by":"crossref","first-page":"1590","DOI":"10.4161\/auto.21459","article-title":"The Actin Cytoskeleton Participates in the Early Events of Autophagosome Formation upon Starvation Induced Autophagy","volume":"8","author":"Aguilera","year":"2012","journal-title":"Autophagy"},{"key":"ref_161","doi-asserted-by":"crossref","first-page":"482","DOI":"10.1016\/j.bbrc.2013.06.111","article-title":"Proteomics Analysis of Autophagy-Deficient Atg7\u2212\/\u2212 MEFs Reveals a Close Relationship between F-Actin and Autophagy","volume":"437","author":"Zhuo","year":"2013","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"ref_162","doi-asserted-by":"crossref","first-page":"433","DOI":"10.1152\/physrev.00026.2002","article-title":"Actin Binding Proteins: Regulation of Cytoskeletal Microfilaments","volume":"83","author":"Chhabra","year":"2003","journal-title":"Physiol. Rev."},{"key":"ref_163","doi-asserted-by":"crossref","unstructured":"Sarkar, S., Olsen, A.L., Sygnecka, K., Lohr, K.M., and Feany, M.B. (2021). \u03b1-Synuclein Impairs Autophagosome Maturation through Abnormal Actin Stabilization. PLoS Genet., 17.","DOI":"10.1371\/journal.pgen.1009359"},{"key":"ref_164","doi-asserted-by":"crossref","first-page":"9238","DOI":"10.1038\/s41467-024-53389-w","article-title":"Accumulation of F-Actin Drives Brain Aging and Limits Healthspan in Drosophila","volume":"15","author":"Schmid","year":"2024","journal-title":"Nat. Commun."},{"key":"ref_165","doi-asserted-by":"crossref","first-page":"119","DOI":"10.1152\/physiolgenomics.90370.2008","article-title":"Muscle Genome-Wide Expression Profiling during Disease Evolution in mdx Mice","volume":"37","author":"Marotta","year":"2009","journal-title":"Physiol. Genom."},{"key":"ref_166","doi-asserted-by":"crossref","first-page":"R318","DOI":"10.1016\/j.cub.2017.02.061","article-title":"The Cytoskeleton-Autophagy Connection","volume":"27","author":"Kast","year":"2017","journal-title":"Curr. Biol."},{"key":"ref_167","doi-asserted-by":"crossref","first-page":"1112","DOI":"10.1038\/ncb3215","article-title":"CapZ Regulates Autophagosomal Membrane Shaping by Promoting Actin Assembly inside the Isolation Membrane","volume":"17","author":"Mi","year":"2015","journal-title":"Nat. Cell Biol."},{"key":"ref_168","doi-asserted-by":"crossref","first-page":"1094","DOI":"10.1038\/ncb3224","article-title":"Actin Shapes the Autophagosome","volume":"17","author":"Holland","year":"2015","journal-title":"Nat. Cell Biol."},{"key":"ref_169","doi-asserted-by":"crossref","first-page":"4566","DOI":"10.1074\/jbc.RA117.001446","article-title":"A PH-like Domain of the Rab12 Guanine Nucleotide Exchange Factor DENND3 Binds Actin and Is Required for Autophagy","volume":"293","author":"Xu","year":"2018","journal-title":"J. Biol. Chem."},{"key":"ref_170","doi-asserted-by":"crossref","first-page":"1853","DOI":"10.15252\/embj.201593148","article-title":"Autophagosome-Lysosome Fusion in Neurons Requires INPP5E, a Protein Associated with Joubert Syndrome","volume":"35","author":"Hasegawa","year":"2016","journal-title":"EMBO J."},{"key":"ref_171","doi-asserted-by":"crossref","first-page":"969","DOI":"10.1038\/emboj.2009.405","article-title":"HDAC6 Controls Autophagosome Maturation Essential for Ubiquitin-Selective Quality-Control Autophagy","volume":"29","author":"Lee","year":"2010","journal-title":"EMBO J."},{"key":"ref_172","doi-asserted-by":"crossref","first-page":"878","DOI":"10.1111\/tra.12410","article-title":"Myosins, Actin and Autophagy","volume":"17","author":"Kruppa","year":"2016","journal-title":"Traffic"},{"key":"ref_173","doi-asserted-by":"crossref","first-page":"7888","DOI":"10.1038\/ncomms8888","article-title":"Actin Nucleation by WH2 Domains at the Autophagosome","volume":"6","author":"Coutts","year":"2015","journal-title":"Nat. Commun."},{"key":"ref_174","doi-asserted-by":"crossref","first-page":"8045","DOI":"10.1038\/ncomms9045","article-title":"Transcriptional Regulation of Annexin A2 Promotes Starvation-Induced Autophagy","volume":"6","author":"Moreau","year":"2015","journal-title":"Nat. Commun."},{"key":"ref_175","doi-asserted-by":"crossref","first-page":"2685","DOI":"10.1038\/emboj.2013.189","article-title":"WASH Inhibits Autophagy through Suppression of Beclin 1 Ubiquitination","volume":"32","author":"Xia","year":"2013","journal-title":"EMBO J."},{"key":"ref_176","doi-asserted-by":"crossref","first-page":"3828","DOI":"10.1038\/ncomms4828","article-title":"Mutation in VPS35 Associated with Parkinson\u2019s Disease Impairs WASH Complex Association and Inhibits Autophagy","volume":"5","author":"Zavodszky","year":"2014","journal-title":"Nat. Commun."},{"key":"ref_177","doi-asserted-by":"crossref","first-page":"7","DOI":"10.1038\/nrm3492","article-title":"New Insights into the Regulation and Cellular Functions of the ARP2\/3 Complex","volume":"14","author":"Rotty","year":"2013","journal-title":"Nat. Rev. Mol. Cell Biol."},{"key":"ref_178","doi-asserted-by":"crossref","first-page":"1702","DOI":"10.1080\/15548627.2015.1073434","article-title":"WHAMM Links Actin Assembly via the Arp2\/3 Complex to Autophagy","volume":"11","author":"Kast","year":"2015","journal-title":"Autophagy"},{"key":"ref_179","doi-asserted-by":"crossref","first-page":"478","DOI":"10.1016\/j.tibs.2016.03.004","article-title":"The WH2 Domain and Actin Nucleation: Necessary but Insufficient","volume":"41","author":"Dominguez","year":"2016","journal-title":"Trends Biochem. Sci."},{"key":"ref_180","doi-asserted-by":"crossref","first-page":"1791","DOI":"10.1016\/j.cub.2015.05.042","article-title":"WHAMM Directs the Arp2\/3 Complex to the ER for Autophagosome Biogenesis through an Actin Comet Tail Mechanism","volume":"25","author":"Kast","year":"2015","journal-title":"Curr. Biol."},{"key":"ref_181","doi-asserted-by":"crossref","first-page":"1209","DOI":"10.1083\/jcb.150.5.1209","article-title":"The Dystrophin Complex Forms a Mechanically Strong Link between the Sarcolemma and Costameric Actin","volume":"150","author":"Rybakova","year":"2000","journal-title":"J. Cell Biol."},{"key":"ref_182","doi-asserted-by":"crossref","first-page":"661","DOI":"10.1083\/jcb.135.3.661","article-title":"A New Model for the Interaction of Dystrophin with F-Actin","volume":"135","author":"Rybakova","year":"1996","journal-title":"J. Cell Biol."},{"key":"ref_183","doi-asserted-by":"crossref","first-page":"28419","DOI":"10.1074\/jbc.273.43.28419","article-title":"A Cluster of Basic Repeats in the Dystrophin Rod Domain Binds F-Actin through an Electrostatic Interaction","volume":"273","author":"Amann","year":"1998","journal-title":"J. Biol. Chem."},{"key":"ref_184","doi-asserted-by":"crossref","first-page":"363","DOI":"10.1083\/jcb.200905048","article-title":"Dystrophin Is a Microtubule-Associated Protein","volume":"186","author":"Prins","year":"2009","journal-title":"J. Cell Biol."},{"key":"ref_185","doi-asserted-by":"crossref","first-page":"1259","DOI":"10.1083\/jcb.144.6.1259","article-title":"Extensive but Coordinated Reorganization of the Membrane Skeleton in Myofibers of Dystrophic (mdx) Mice","volume":"144","author":"Williams","year":"1999","journal-title":"J. Cell Biol."},{"key":"ref_186","doi-asserted-by":"crossref","first-page":"5385","DOI":"10.1073\/pnas.0600980103","article-title":"Cytoplasmic Gamma-Actin Contributes to a Compensatory Remodeling Response in Dystrophin-Deficient Muscle","volume":"103","author":"Hanft","year":"2006","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_187","doi-asserted-by":"crossref","first-page":"353","DOI":"10.4161\/cc.6.3.3819","article-title":"Recruitment of Dbl by Ezrin and Dystroglycan Drives Membrane Proximal Cdc42 Activation and Filopodia Formation","volume":"6","author":"Batchelor","year":"2007","journal-title":"Cell Cycle"},{"key":"ref_188","doi-asserted-by":"crossref","first-page":"1657","DOI":"10.1093\/hmg\/ddh170","article-title":"Ezrin-Dependent Regulation of the Actin Cytoskeleton by \u03b2 -Dystroglycan","volume":"13","author":"Spence","year":"2004","journal-title":"Hum. Mol. Genet."},{"key":"ref_189","doi-asserted-by":"crossref","first-page":"329","DOI":"10.1042\/bj20030808","article-title":"Direct Interaction of \u03b2-Dystroglycan with F-Actin","volume":"375","author":"Chen","year":"2003","journal-title":"Biochem. J."},{"key":"ref_190","doi-asserted-by":"crossref","first-page":"2182","DOI":"10.1016\/j.bbadis.2017.05.025","article-title":"\u03b1-Dystroglycan Hypoglycosylation Affects Cell Migration by Influencing \u03b2-Dystroglycan Membrane Clustering and Filopodia Length: A Multiscale Confocal Microscopy Analysis","volume":"1863","author":"Palmieri","year":"2017","journal-title":"Biochim. Biophys. Acta Mol. Basis Dis."},{"key":"ref_191","doi-asserted-by":"crossref","unstructured":"Thompson, O., Kleino, I., Crimaldi, L., Gimona, M., Saksela, K., and Winder, S.J. (2008). Dystroglycan, Tks5 and Src Mediated Assembly of Podosomes in Myoblasts. PLoS ONE, 3.","DOI":"10.1371\/journal.pone.0003638"},{"key":"ref_192","doi-asserted-by":"crossref","unstructured":"Sciandra, F., Desiderio, C., Vincenzoni, F., Viscuso, S., Bozzi, M., H\u00fcbner, W., Jimenez-Gutierrez, G.E., Cisneros, B., and Brancaccio, A. (2024). Analysis of the GFP-Labelled \u03b2-Dystroglycan Interactome in HEK-293 Transfected Cells Reveals Novel Intracellular Networks. Biochem. Biophys. Res. Commun., 703.","DOI":"10.1016\/j.bbrc.2024.149656"},{"key":"ref_193","doi-asserted-by":"crossref","first-page":"11534","DOI":"10.1038\/ncomms11534","article-title":"ISPD Produces CDP-Ribitol Used by FKTN and FKRP to Transfer Ribitol Phosphate onto \u03b1-Dystroglycan","volume":"7","author":"Gerin","year":"2016","journal-title":"Nat. Commun."},{"key":"ref_194","doi-asserted-by":"crossref","unstructured":"Kanagawa, M. (2021). Dystroglycanopathy: From Elucidation of Molecular and Pathological Mechanisms to Development of Treatment Methods. Int. J. Mol. Sci., 22.","DOI":"10.3390\/ijms222313162"},{"key":"ref_195","doi-asserted-by":"crossref","first-page":"e14473","DOI":"10.7554\/eLife.14473","article-title":"The Functional O-Mannose Glycan on \u03b1-Dystroglycan Contains a Phospho-Ribitol Primed for Matriglycan Addition","volume":"5","author":"Praissman","year":"2016","journal-title":"eLife"},{"key":"ref_196","doi-asserted-by":"crossref","first-page":"e03943","DOI":"10.7554\/eLife.03943","article-title":"B4GAT1 Is the Priming Enzyme for the LARGE-Dependent Functional Glycosylation of \u03b1-Dystroglycan","volume":"3","author":"Praissman","year":"2014","journal-title":"eLife"},{"key":"ref_197","doi-asserted-by":"crossref","first-page":"93","DOI":"10.1126\/science.1214115","article-title":"Dystroglycan Function Requires Xylosyl- and Glucuronyltransferase Activities of LARGE","volume":"335","author":"Inamori","year":"2012","journal-title":"Science"},{"key":"ref_198","doi-asserted-by":"crossref","first-page":"24618","DOI":"10.1074\/jbc.M116.751917","article-title":"The Muscular Dystrophy Gene TMEM5 Encodes a Ribitol \u03921,4-Xylosyltransferase Required for the Functional Glycosylation of Dystroglycan","volume":"291","author":"Manya","year":"2016","journal-title":"J. Biol. Chem."},{"key":"ref_199","doi-asserted-by":"crossref","first-page":"e03941","DOI":"10.7554\/eLife.03941","article-title":"The Glucuronyltransferase B4GAT1 Is Required for Initiation of LARGE-Mediated \u03b1-Dystroglycan Functional Glycosylation","volume":"3","author":"Willer","year":"2014","journal-title":"eLife"},{"key":"ref_200","doi-asserted-by":"crossref","unstructured":"Dempsey, C.E., Bigotti, M.G., Adams, J.C., and Brancaccio, A. (2019). Analysis of \u03b1-Dystroglycan\/LG Domain Binding Modes: Investigating Protein Motifs That Regulate the Affinity of Isolated LG Domains. Front. Mol. Biosci., 6.","DOI":"10.3389\/fmolb.2019.00018"},{"key":"ref_201","doi-asserted-by":"crossref","first-page":"1198","DOI":"10.1086\/324412","article-title":"Mutations in the Fukutin-Related Protein Gene (FKRP) Cause a Form of Congenital Muscular Dystrophy with Secondary Laminin \u03b12 Deficiency and Abnormal Glycosylation of \u03b1-Dystroglycan","volume":"69","author":"Brockington","year":"2001","journal-title":"Am. J. Hum. Genet."},{"key":"ref_202","doi-asserted-by":"crossref","first-page":"2851","DOI":"10.1093\/hmg\/10.25.2851","article-title":"Mutations in the Fukutin-Related Protein Gene (FKRP) Identify Limb Girdle Muscular Dystrophy 2I as a Milder Allelic Variant of Congenital Muscular Dystrophy MDC1C","volume":"10","author":"Brockington","year":"2001","journal-title":"Hum. Mol. Genet."},{"key":"ref_203","doi-asserted-by":"crossref","first-page":"388","DOI":"10.1038\/28653","article-title":"An Ancient Retrotransposal Insertion Causes Fukuyama-Type Congenital Muscular Dystrophy","volume":"394","author":"Kobayashi","year":"1998","journal-title":"Nature"},{"key":"ref_204","doi-asserted-by":"crossref","first-page":"1033","DOI":"10.1086\/342975","article-title":"Mutations in the O-Mannosyltransferase Gene POMT1 Give Rise to the Severe Neuronal Migration Disorder Walker-Warburg Syndrome","volume":"71","author":"Currier","year":"2002","journal-title":"Am. J. Hum. Genet."},{"key":"ref_205","doi-asserted-by":"crossref","first-page":"519","DOI":"10.1111\/nan.12684","article-title":"Protein Homeostasis in LGMDR9 (LGMD2I)\u2014The Role of Ubiquitin\u2013Proteasome and Autophagy\u2013Lysosomal System","volume":"47","author":"Franekova","year":"2021","journal-title":"Neuropathol. Appl. Neurobiol."},{"key":"ref_206","doi-asserted-by":"crossref","first-page":"1704","DOI":"10.1126\/science.1065874","article-title":"Identification of Ubiquitin Ligases Required for Skeletal Muscle Atrophy","volume":"294","author":"Bodine","year":"2001","journal-title":"Science"},{"key":"ref_207","doi-asserted-by":"crossref","first-page":"3319","DOI":"10.1093\/hmg\/11.26.3319","article-title":"Functional Requirements for Fukutin-Related Protein in the Golgi Apparatus","volume":"11","author":"Esapa","year":"2002","journal-title":"Hum. Mol. Genet."},{"key":"ref_208","doi-asserted-by":"crossref","first-page":"295","DOI":"10.1093\/hmg\/ddi026","article-title":"Fukutin-Related Protein Mutations That Cause Congenital Muscular Dystrophy Result in ER-Retention of the Mutant Protein in Cultured Cells","volume":"14","author":"Esapa","year":"2005","journal-title":"Hum. Mol. Genet."},{"key":"ref_209","doi-asserted-by":"crossref","unstructured":"Esapa, C.T., McIlhinney, R.A.J., Waite, A.J., Benson, M.A., Mirzayan, J., Piko, H., Herczegfalvi, \u00c1., Horvath, R., Karcagi, V., and Walter, M.C. (2023). Misfolding of Fukutin-Related Protein (FKRP) Variants in Congenital and Limb Girdle Muscular Dystrophies. Front. Mol. Biosci., 10.","DOI":"10.3389\/fmolb.2023.1279700"},{"key":"ref_210","doi-asserted-by":"crossref","first-page":"dmm050594","DOI":"10.1242\/dmm.050594","article-title":"The Missense Mutation C667F in Murine \u03b2-Dystroglycan Causes Embryonic Lethality, Myopathy and Blood-Brain Barrier Destabilization","volume":"17","author":"Tan","year":"2024","journal-title":"Dis. Model. Mech."},{"key":"ref_211","doi-asserted-by":"crossref","unstructured":"Henriques, S.F., Patissier, C., Bourg, N., Fecchio, C., Sandona, D., Marsolier, J., and Richard, I. (2018). Different Outcome of Sarcoglycan Missense Mutation between Human and Mouse. PLoS ONE, 13.","DOI":"10.1371\/journal.pone.0191274"},{"key":"ref_212","doi-asserted-by":"crossref","first-page":"20","DOI":"10.1186\/s13395-016-0091-9","article-title":"Four-Week Rapamycin Treatment Improves Muscular Dystrophy in a Fukutin-Deficient Mouse Model of Dystroglycanopathy","volume":"6","author":"Foltz","year":"2016","journal-title":"Skelet. Muscle"},{"key":"ref_213","doi-asserted-by":"crossref","first-page":"2752","DOI":"10.1016\/j.stemcr.2021.09.009","article-title":"Defective Autophagy and Increased Apoptosis Contribute toward the Pathogenesis of FKRP-Associated Muscular Dystrophies","volume":"16","author":"Bincoletto","year":"2021","journal-title":"Stem Cell Rep."},{"key":"ref_214","doi-asserted-by":"crossref","first-page":"619","DOI":"10.1016\/j.nmd.2017.02.015","article-title":"Limb Girdle Muscular Dystrophy Type 2I: No Correlation between Clinical Severity, Histopathology and Glycosylated \u03b1-Dystroglycan Levels in Patients Homozygous for Common FKRP Mutation","volume":"27","author":"Alhamidi","year":"2017","journal-title":"Neuromuscul. Disord."},{"key":"ref_215","doi-asserted-by":"crossref","first-page":"1874","DOI":"10.1002\/humu.23827","article-title":"Functional and Cellular Localization Diversity Associated with Fukutin-Related Protein Patient Genetic Variants","volume":"40","author":"Henriques","year":"2019","journal-title":"Hum. Mutat."},{"key":"ref_216","doi-asserted-by":"crossref","first-page":"e315","DOI":"10.1212\/NXG.0000000000000315","article-title":"Clinical, Genetic, and Pathologic Characterization of FKRP Mexican Founder Mutation c.1387A>G","volume":"5","author":"Lee","year":"2019","journal-title":"Neurol. Genet."},{"key":"ref_217","doi-asserted-by":"crossref","first-page":"1122","DOI":"10.1111\/j.1462-5822.2012.01784.x","article-title":"Binding of Lassa Virus Perturbs Extracellular Matrix-Induced Signal Transduction via Dystroglycan","volume":"14","author":"Rojek","year":"2012","journal-title":"Cell Microbiol."},{"key":"ref_218","doi-asserted-by":"crossref","first-page":"34667","DOI":"10.1074\/jbc.273.52.34667","article-title":"Assembly of the Sarcoglycan Complex. Insights for Muscular Dystrophy","volume":"273","author":"Holt","year":"1998","journal-title":"J. Biol. Chem."},{"key":"ref_219","doi-asserted-by":"crossref","first-page":"e28","DOI":"10.1017\/S1462399409001203","article-title":"Sarcoglycanopathies: Molecular Pathogenesis and Therapeutic Prospects","volume":"11","author":"Betto","year":"2009","journal-title":"Expert. Rev. Mol. Med."},{"key":"ref_220","doi-asserted-by":"crossref","first-page":"660","DOI":"10.1111\/ene.14592","article-title":"Clinical Correlations and Long-Term Follow-up in 100 Patients with Sarcoglycanopathies","volume":"28","author":"Wahbi","year":"2021","journal-title":"Eur. J. Neurol."},{"key":"ref_221","doi-asserted-by":"crossref","first-page":"596","DOI":"10.1093\/brain\/awab301","article-title":"Clinical and Genetic Spectrum of a Large Cohort of Patients with \u03b4-Sarcoglycan Muscular Dystrophy","volume":"145","author":"Bruno","year":"2022","journal-title":"Brain"},{"key":"ref_222","doi-asserted-by":"crossref","first-page":"1214","DOI":"10.1093\/hmg\/ddn029","article-title":"Mannosidase I Inhibition Rescues the Human \u03b1-Sarcoglycan R77C Recurrent Mutation","volume":"17","author":"Bartoli","year":"2008","journal-title":"Hum. Mol. Genet."},{"key":"ref_223","doi-asserted-by":"crossref","first-page":"429","DOI":"10.1002\/humu.21659","article-title":"Rescue of Sarcoglycan Mutations by Inhibition of Endoplasmic Reticulum Quality Control Is Associated with Minimal Structural Modifications","volume":"33","author":"Soheili","year":"2012","journal-title":"Hum. Mutat."},{"key":"ref_224","doi-asserted-by":"crossref","first-page":"170","DOI":"10.2353\/ajpath.2008.071146","article-title":"Inhibition of Proteasome Activity Promotes the Correct Localization of Disease-Causing \u03b1-Sarcoglycan Mutants in HEK-293 Cells Constitutively Expressing \u03b2-, \u03b3-, and \u03b4-Sarcoglycan","volume":"173","author":"Gastaldello","year":"2008","journal-title":"Am. J. Pathol."},{"key":"ref_225","doi-asserted-by":"crossref","first-page":"3746","DOI":"10.1093\/hmg\/ddu088","article-title":"Unveiling the Degradative Route of the V247M \u03b1-Sarcoglycan Mutant Responsible for LGMD-2D","volume":"23","author":"Bianchini","year":"2014","journal-title":"Hum. Mol. Genet."},{"key":"ref_226","doi-asserted-by":"crossref","first-page":"102459","DOI":"10.1016\/j.coph.2024.102459","article-title":"Advanced Therapeutic Approaches in Sarcoglycanopathies","volume":"76","author":"Scano","year":"2024","journal-title":"Curr Opin Pharmacol"},{"key":"ref_227","doi-asserted-by":"crossref","unstructured":"Carotti, M., Scano, M., Fancello, I., Richard, I., Risato, G., Bensalah, M., Soardi, M., and Sandon\u00e0, D. (2020). Combined Use of CFTR Correctors in LGMD2D Myotubes Improves Sarcoglycan Complex Recovery. Int. J. Mol. Sci., 21.","DOI":"10.3390\/ijms21051813"},{"key":"ref_228","doi-asserted-by":"crossref","first-page":"499","DOI":"10.1093\/hmg\/ddab260","article-title":"CFTR Corrector C17 Is Effective in Muscular Dystrophy, in Vivo Proof of Concept in LGMDR3","volume":"31","author":"Scano","year":"2022","journal-title":"Hum. Mol. Genet."},{"key":"ref_229","doi-asserted-by":"crossref","first-page":"216","DOI":"10.1038\/ng1095-216","article-title":"Mutations in the Laminin \u03b12-Chain Gene (LAMA2) Cause Merosin-Deficient Congenital Muscular Dystrophy","volume":"11","author":"Zhang","year":"1995","journal-title":"Nat. Genet."},{"key":"ref_230","doi-asserted-by":"crossref","first-page":"877","DOI":"10.2169\/internalmedicine.9588-17","article-title":"A Homozygous LAMA2 Mutation of c.818G>A Caused Partial Merosin Deficiency in a Japanese Patient","volume":"57","author":"Kubota","year":"2018","journal-title":"Intern. Med."},{"key":"ref_231","doi-asserted-by":"crossref","first-page":"91","DOI":"10.1038\/sj.ejhg.5200743","article-title":"Merosin-Deficient Congenital Muscular Dystrophy, Autosomal Recessive (MDC1A, MIM#156225, LAMA2 Gene Coding for \u03b12 Chain of Laminin)","volume":"10","author":"Allamand","year":"2002","journal-title":"Eur. J. Hum. Genet."},{"key":"ref_232","doi-asserted-by":"crossref","first-page":"541","DOI":"10.1093\/hmg\/ddq499","article-title":"Proteasome Inhibition Improves the Muscle of Laminin \u03b12 Chain-Deficient Mice","volume":"20","author":"Carmignac","year":"2011","journal-title":"Hum. Mol. Genet."},{"key":"ref_233","doi-asserted-by":"crossref","first-page":"1518","DOI":"10.1016\/j.ajpath.2014.01.019","article-title":"Bortezomib Partially Improves Laminin \u03b12 Chain-Deficient Muscular Dystrophy","volume":"184","author":"Holmberg","year":"2014","journal-title":"Am. J. Pathol."},{"key":"ref_234","doi-asserted-by":"crossref","first-page":"4891","DOI":"10.1093\/hmg\/ddr427","article-title":"Autophagy Is Increased in Laminin \u03b12 Chain-Deficient Muscle and Its Inhibition Improves Muscle Morphology in a Mouse Model of MDC1A","volume":"20","author":"Carmignac","year":"2011","journal-title":"Hum. Mol. Genet."},{"key":"ref_235","doi-asserted-by":"crossref","first-page":"11501","DOI":"10.4081\/ejtm.2023.11501","article-title":"Autophagy Increase in Merosin-Deficient Congenital Muscular Dystrophy Type 1A","volume":"33","author":"Mastrapasqua","year":"2023","journal-title":"Eur. J. Transl. Myol."}],"container-title":["Cells"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/www.mdpi.com\/2073-4409\/14\/10\/721\/pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2025,10,9]],"date-time":"2025-10-09T17:33:18Z","timestamp":1760031198000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.mdpi.com\/2073-4409\/14\/10\/721"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2025,5,15]]},"references-count":235,"journal-issue":{"issue":"10","published-online":{"date-parts":[[2025,5]]}},"alternative-id":["cells14100721"],"URL":"https:\/\/doi.org\/10.3390\/cells14100721","relation":{},"ISSN":["2073-4409"],"issn-type":[{"value":"2073-4409","type":"electronic"}],"subject":[],"published":{"date-parts":[[2025,5,15]]}}}