Cardiolipin remodeling enables protein crowding in the inner mitochondrial membrane.


Journal

The EMBO journal
ISSN: 1460-2075
Titre abrégé: EMBO J
Pays: England
ID NLM: 8208664

Informations de publication

Date de publication:
01 12 2021
Historique:
revised: 23 09 2021
received: 07 04 2021
accepted: 24 09 2021
pubmed: 19 10 2021
medline: 22 12 2021
entrez: 18 10 2021
Statut: ppublish

Résumé

Mitochondrial cristae are extraordinarily crowded with proteins, which puts stress on the bilayer organization of lipids. We tested the hypothesis that the high concentration of proteins drives the tafazzin-catalyzed remodeling of fatty acids in cardiolipin, thereby reducing bilayer stress in the membrane. Specifically, we tested whether protein crowding induces cardiolipin remodeling and whether the lack of cardiolipin remodeling prevents the membrane from accumulating proteins. In vitro, the incorporation of large amounts of proteins into liposomes altered the outcome of the remodeling reaction. In yeast, the concentration of proteins involved in oxidative phosphorylation (OXPHOS) correlated with the cardiolipin composition. Genetic ablation of either remodeling or biosynthesis of cardiolipin caused a substantial drop in the surface density of OXPHOS proteins in the inner membrane of the mouse heart and Drosophila flight muscle mitochondria. Our data suggest that OXPHOS protein crowding induces cardiolipin remodelling and that remodeled cardiolipin supports the high concentration of these proteins in the inner mitochondrial membrane.

Identifiants

pubmed: 34661298
doi: 10.15252/embj.2021108428
pmc: PMC8634138
doi:

Substances chimiques

Cardiolipins 0
Fatty Acids 0
Liposomes 0
Proteins 0
Acyltransferases EC 2.3.-
tafazzin protein, mouse EC 2.3.-

Types de publication

Journal Article Research Support, N.I.H., Extramural

Langues

eng

Sous-ensembles de citation

IM

Pagination

e108428

Subventions

Organisme : NCI NIH HHS
ID : P30 CA016087
Pays : United States
Organisme : NIGMS NIH HHS
ID : R01 GM115593
Pays : United States
Organisme : NINDS NIH HHS
ID : P30 NS050276
Pays : United States
Organisme : NIH HHS
ID : S10 OD023659
Pays : United States
Organisme : NCRR NIH HHS
ID : S10 RR027990
Pays : United States

Informations de copyright

© 2021 The Authors.

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Auteurs

Yang Xu (Y)

Department of Anesthesiology, New York University Grossman School of Medicine, New York, NY, USA.

Hediye Erdjument-Bromage (H)

Kimmel Center for Biology and Medicine at the Skirball Institute, New York University Grossman School of Medicine, New York, NY, USA.
Department of Cell Biology, New York University Grossman School of Medicine, New York, NY, USA.

Colin K L Phoon (CKL)

Department of Pediatrics, New York University Grossman School of Medicine, New York, NY, USA.

Thomas A Neubert (TA)

Kimmel Center for Biology and Medicine at the Skirball Institute, New York University Grossman School of Medicine, New York, NY, USA.
Department of Cell Biology, New York University Grossman School of Medicine, New York, NY, USA.

Mindong Ren (M)

Department of Anesthesiology, New York University Grossman School of Medicine, New York, NY, USA.
Department of Cell Biology, New York University Grossman School of Medicine, New York, NY, USA.

Michael Schlame (M)

Department of Anesthesiology, New York University Grossman School of Medicine, New York, NY, USA.
Department of Cell Biology, New York University Grossman School of Medicine, New York, NY, USA.

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Classifications MeSH