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The Ubiquitin Proteasome System in Neuromuscular Disorders: Moving Beyond Movement

Experimental Neuroinflammation Laboratory, Department of Experimental Medical Science, Lund University, Sölvegatan 19, 221 84 Lund, Sweden
Departamento de Bioquímica y Biología Molecular, Facultad de Farmacia, Universidad de Sevilla/Instituto de Biomedicina de Sevilla-Hospital Universitario Virgen del Rocío/CSIC/Universidad de Sevilla, 41012 Sevilla, Spain
Unidad Clínica de Enfermedades Infecciosas, Hospital Universitario de Valme, 41014 Sevilla, Spain
Departamento de Especialidades Quirúrgicas, Bioquímica e Inmunología, Facultad de Medicina, 29071 Universidad de Málaga, Spain
Departamento de Fisiología, Anatomía y Biología Celular, Universidad Pablo de Olavide, 41013 Sevilla, Spain
Author to whom correspondence should be addressed.
These authors contributed equally to the work.
Int. J. Mol. Sci. 2020, 21(17), 6429;
Received: 14 July 2020 / Revised: 30 August 2020 / Accepted: 31 August 2020 / Published: 3 September 2020
(This article belongs to the Section Molecular Biology)
Neuromuscular disorders (NMDs) affect 1 in 3000 people worldwide. There are more than 150 different types of NMDs, where the common feature is the loss of muscle strength. These disorders are classified according to their neuroanatomical location, as motor neuron diseases, peripheral nerve diseases, neuromuscular junction diseases, and muscle diseases. Over the years, numerous studies have pointed to protein homeostasis as a crucial factor in the development of these fatal diseases. The ubiquitin–proteasome system (UPS) plays a fundamental role in maintaining protein homeostasis, being involved in protein degradation, among other cellular functions. Through a cascade of enzymatic reactions, proteins are ubiquitinated, tagged, and translocated to the proteasome to be degraded. Within the ubiquitin system, we can find three main groups of enzymes: E1 (ubiquitin-activating enzymes), E2 (ubiquitin-conjugating enzymes), and E3 (ubiquitin–protein ligases). Only the ubiquitinated proteins with specific chain linkages (such as K48) will be degraded by the UPS. In this review, we describe the relevance of this system in NMDs, summarizing the UPS proteins that have been involved in pathological conditions and neuromuscular disorders, such as Spinal Muscular Atrophy (SMA), Charcot–Marie–Tooth disease (CMT), or Duchenne Muscular Dystrophy (DMD), among others. A better knowledge of the processes involved in the maintenance of proteostasis may pave the way for future progress in neuromuscular disorder studies and treatments. View Full-Text
Keywords: ubiquitin; proteasome; UPS; neuromuscular junction; synapse; neuromuscular disorder ubiquitin; proteasome; UPS; neuromuscular junction; synapse; neuromuscular disorder
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MDPI and ACS Style

Bachiller, S.; Alonso-Bellido, I.M.; Real, L.M.; Pérez-Villegas, E.M.; Venero, J.L.; Deierborg, T.; Armengol, J.Á.; Ruiz, R. The Ubiquitin Proteasome System in Neuromuscular Disorders: Moving Beyond Movement. Int. J. Mol. Sci. 2020, 21, 6429.

AMA Style

Bachiller S, Alonso-Bellido IM, Real LM, Pérez-Villegas EM, Venero JL, Deierborg T, Armengol JÁ, Ruiz R. The Ubiquitin Proteasome System in Neuromuscular Disorders: Moving Beyond Movement. International Journal of Molecular Sciences. 2020; 21(17):6429.

Chicago/Turabian Style

Bachiller, Sara, Isabel M. Alonso-Bellido, Luis M. Real, Eva M. Pérez-Villegas, José L. Venero, Tomas Deierborg, José Á. Armengol, and Rocío Ruiz. 2020. "The Ubiquitin Proteasome System in Neuromuscular Disorders: Moving Beyond Movement" International Journal of Molecular Sciences 21, no. 17: 6429.

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