Regulated membrane remodeling by Mic60 controls formation of mitochondrial crista junctions

Manuel Hessenberger, Ralf M Zerbes, Heike Rampelt, Séverine Kunz, Audrey H Xavier, Bettina Purfürst, Hauke Lilie, Nikolaus Pfanner, Martin van der Laan, Oliver Daumke

Publikation: Beitrag in Fachzeitschrift (peer-reviewed)Artikel in Fachzeitschrift

72 Zitate (Scopus)

Abstract

The mitochondrial contact site and cristae organizing system (MICOS) is crucial for the formation of crista junctions and mitochondrial inner membrane architecture. MICOS contains two core components. Mic10 shows membrane-bending activity, whereas Mic60 (mitofilin) forms contact sites between inner and outer membranes. Here we report that Mic60 deforms liposomes into thin membrane tubules and thus displays membrane-shaping activity. We identify a membrane-binding site in the soluble intermembrane space-exposed part of Mic60. This membrane-binding site is formed by a predicted amphipathic helix between the conserved coiled-coil and mitofilin domains. The mitofilin domain negatively regulates the membrane-shaping activity of Mic60. Binding of Mic19 to the mitofilin domain modulates this activity. Membrane binding and shaping by the conserved Mic60-Mic19 complex is crucial for crista junction formation, mitochondrial membrane architecture and efficient respiratory activity. Mic60 thus plays a dual role by shaping inner membrane crista junctions and forming contact sites with the outer membrane.

OriginalspracheEnglisch
Aufsatznummer15258
Seiten (von - bis)15258
FachzeitschriftNature Communications
Jahrgang8
DOIs
PublikationsstatusVeröffentlicht - 31 Mai 2017
Extern publiziertJa

Fingerprint

Untersuchen Sie die Forschungsthemen von „Regulated membrane remodeling by Mic60 controls formation of mitochondrial crista junctions“. Zusammen bilden sie einen einzigartigen Fingerprint.

Dieses zitieren