LonP1 Links Mitochondria-ER Interaction to Regulate Heart Function.
Journal
Research (Washington, D.C.)
ISSN: 2639-5274
Titre abrégé: Research (Wash D C)
Pays: United States
ID NLM: 101747148
Informations de publication
Date de publication:
2023
2023
Historique:
received:
17
03
2023
accepted:
29
05
2023
medline:
19
6
2023
pubmed:
19
6
2023
entrez:
19
6
2023
Statut:
epublish
Résumé
Interorganelle contacts and communications are increasingly recognized to play a vital role in cellular function and homeostasis. In particular, the mitochondria-endoplasmic reticulum (ER) membrane contact site (MAM) is known to regulate ion and lipid transfer, as well as signaling and organelle dynamics. However, the regulatory mechanisms of MAM formation and their function are still elusive. Here, we identify mitochondrial Lon protease (LonP1), a highly conserved mitochondrial matrix protease, as a new MAM tethering protein. The removal of LonP1 substantially reduces MAM formation and causes mitochondrial fragmentation. Furthermore, deletion of LonP1 in the cardiomyocytes of mouse heart impairs MAM integrity and mitochondrial fusion and activates the unfolded protein response within the ER (UPR
Identifiants
pubmed: 37333972
doi: 10.34133/research.0175
pii: 0175
pmc: PMC10275618
doi:
Types de publication
Journal Article
Langues
eng
Pagination
0175Informations de copyright
Copyright © 2023 Yujie Li et al.
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