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Regulated membrane remodeling by Mic60 controls formation of mitochondrial crista junctions

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Official URL:https://doi.org/10.1038/ncomms15258
PubMed:View item in PubMed
Creators Name:Hessenberger, M. and Zerbes, R.M. and Rampelt, H. and Kunz, S. and Xavier, A.H. and Purfuerst, B. and Lilie, H. and Pfanner, N. and van der Laan, M. and Daumke, O.
Journal Title:Nature Communications
Journal Abbreviation:Nat Commun
Volume:8
Page Range:15258
Date:31 May 2017
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.
ISSN:2041-1723
Publisher:Nature Publishing Group (U.K.)
Item Type:Article

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