RT Journal Article
T1 The ubiquitin proteasome system in neuromuscular disorders: moving beyond movement
A1 Bachiller, Sara
A1 Alonso-Bellido, Isabel M.
A1 Real, Luis Miguel
A1 Pérez-Villegas, E.
A1 Venero, José Luis
A1 Deierborg, Tomás
A1 Armengol Butrón de Mújica, José Ángel
A1 Ruiz, Rocío
K1 Ubiquitin
K1 Proteasome
K1 UPS
K1 Neuromuscular junction
K1 Synapse
K1 Neuromuscular disorder
AB 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 involvedinproteindegradation, amongothercellularfunctions. Throughacascadeofenzymatic 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.
PB MDPI
YR 2020
FD 2020-09-03
LK https://hdl.handle.net/10433/25770
UL https://hdl.handle.net/10433/25770
LA en
NO Int. J. Mol. Sci. 2020, 21, 6429
NO Departamento fisiología, anatomía y biología celular
DS RIO
RD May 9, 2026