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Regulated membrane remodeling by Mic60 controls formation of mitochondrial crista junctions

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Item Type:Article
Title:Regulated membrane remodeling by Mic60 controls formation of mitochondrial crista junctions
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.
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.
Source:Nature Communications
ISSN:2041-1723
Publisher:Nature Publishing Group (U.K.)
Volume:8
Page Range:15258
Date:31 May 2017
Official Publication:https://doi.org/10.1038/ncomms15258
PubMed:View item in PubMed

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