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 () and Oliver Daumke ()
Additional contact information
Manuel Hessenberger: Max-Delbrück-Center for Molecular Medicine
Ralf M. Zerbes: Institute of Biochemistry and Molecular Biology, ZBMZ, Faculty of Medicine, University of Freiburg
Heike Rampelt: Institute of Biochemistry and Molecular Biology, ZBMZ, Faculty of Medicine, University of Freiburg
Séverine Kunz: Max-Delbrück-Center for Molecular Medicine
Audrey H. Xavier: Max-Delbrück-Center for Molecular Medicine
Bettina Purfürst: Core Facility Electron Microscopy, Max-Delbrück-Center for Molecular Medicine
Hauke Lilie: Institute of Biochemistry and Biotechnology, Section of Protein Biochemistry, Martin Luther University Halle-Wittenberg
Nikolaus Pfanner: Institute of Biochemistry and Molecular Biology, ZBMZ, Faculty of Medicine, University of Freiburg
Martin van der Laan: Medical Biochemistry and Molecular Biology, Center for Molecular Signaling, PZMS, Saarland University
Oliver Daumke: Max-Delbrück-Center for Molecular Medicine

Nature Communications, 2017, vol. 8, issue 1, 1-11

Abstract: 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.

Date: 2017
References: Add references at CitEc
Citations:

Downloads: (external link)
https://www.nature.com/articles/ncomms15258 Abstract (text/html)

Related works:
This item may be available elsewhere in EconPapers: Search for items with the same title.

Export reference: BibTeX RIS (EndNote, ProCite, RefMan) HTML/Text

Persistent link: https://EconPapers.repec.org/RePEc:nat:natcom:v:8:y:2017:i:1:d:10.1038_ncomms15258

Ordering information: This journal article can be ordered from
https://www.nature.com/ncomms/

DOI: 10.1038/ncomms15258

Access Statistics for this article

Nature Communications is currently edited by Nathalie Le Bot, Enda Bergin and Fiona Gillespie

More articles in Nature Communications from Nature
Bibliographic data for series maintained by Sonal Shukla () and Springer Nature Abstracting and Indexing ().