Role of Lipids and Divalent Cations in Membrane Fusion Mediated by the Heptad Repeat Domain 1 of Mitofusin.
Mitofusin
amphipathic helix
divalent cations
fusion
lipid packing defects
membrane
mitochondria
Journal
Biomolecules
ISSN: 2218-273X
Titre abrégé: Biomolecules
Pays: Switzerland
ID NLM: 101596414
Informations de publication
Date de publication:
02 09 2023
02 09 2023
Historique:
received:
26
07
2023
revised:
21
08
2023
accepted:
30
08
2023
medline:
4
10
2023
pubmed:
28
9
2023
entrez:
28
9
2023
Statut:
epublish
Résumé
Mitochondria are highly dynamic organelles that constantly undergo fusion and fission events to maintain their shape, distribution and cellular function. Mitofusin 1 and 2 proteins are two dynamin-like GTPases involved in the fusion of outer mitochondrial membranes (OMM). Mitofusins are anchored to the OMM through their transmembrane domain and possess two heptad repeat domains (HR1 and HR2) in addition to their N-terminal GTPase domain. The HR1 domain was found to induce fusion via its amphipathic helix, which interacts with the lipid bilayer structure. The lipid composition of mitochondrial membranes can also impact fusion. However, the precise mode of action of lipids in mitochondrial fusion is not fully understood. In this study, we examined the role of the mitochondrial lipids phosphatidylethanolamine (PE), cardiolipin (CL) and phosphatidic acid (PA) in membrane fusion induced by the HR1 domain, both in the presence and absence of divalent cations (Ca
Identifiants
pubmed: 37759741
pii: biom13091341
doi: 10.3390/biom13091341
pmc: PMC10527301
pii:
doi:
Substances chimiques
Cations, Divalent
0
GTP Phosphohydrolases
EC 3.6.1.-
Lipids
0
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
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