The lysosomal membrane protein Sidt2 is a vital regulator of mitochondrial quality control in skeletal muscle.
Animals
Autophagy
/ physiology
Cell Line
Cell Membrane
Gene Expression Regulation
Genetic Predisposition to Disease
Lysosomes
Mice
Mice, Knockout
Microscopy, Electron, Transmission
Mitochondria, Muscle
/ metabolism
Muscle, Skeletal
/ cytology
Muscular Diseases
/ genetics
Nucleotide Transport Proteins
/ genetics
Sidt2
autophagy
mitochondria
myopathy
quality control
Journal
FASEB journal : official publication of the Federation of American Societies for Experimental Biology
ISSN: 1530-6860
Titre abrégé: FASEB J
Pays: United States
ID NLM: 8804484
Informations de publication
Date de publication:
04 2021
04 2021
Historique:
revised:
18
10
2020
received:
28
02
2020
accepted:
11
11
2020
entrez:
14
3
2021
pubmed:
15
3
2021
medline:
20
7
2021
Statut:
ppublish
Résumé
The role of Sidt2 in the process of glucose and lipid metabolism has been recently reported. However, whether Sidt2 is involved in the metabolic regulation in skeletal muscle remains unknown. In this study, for the first time, using skeletal muscle-selective Sidt2 knockout mice, we found that Sidt2 was vital for the quality control of mitochondria in mouse skeletal muscle. These mice showed significantly reduced muscle tolerance and structurally abnormal mitochondria. Deletion of the Sidt2 gene resulted in decreased expression of mitochondrial fusion protein 2 (Mfn2) and Dynamin-related protein 1 (Drp1), as well as peroxisome proliferator-activated receptor γ coactivator-1 (PGC1-α). In addition, the clearance of damaged mitochondria in skeletal muscle was inhibited upon Sidt2 deletion, which was caused by blockade of autophagy flow. Mechanistically, the fusion of autophagosomes and lysosomes was compromised in Sidt2 knockout skeletal muscle cells. In summary, the deletion of the Sidt2 gene not only interfered with the quality control of mitochondria, but also inhibited the clearance of mitochondria and caused the accumulation of a large number of damaged mitochondria, ultimately leading to the abnormal structure and function of skeletal muscle.
Identifiants
pubmed: 33715196
doi: 10.1096/fj.202000424R
doi:
Substances chimiques
Nucleotide Transport Proteins
0
Sidt2 protein, mouse
0
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
e21223Informations de copyright
© 2020 Federation of American Societies for Experimental Biology.
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