The MICOS component Mic60 displays a conserved membrane-bending activity that is necessary for normal cristae morphology

2017 | journal article; research paper. A publication with affiliation to the University of Göttingen.

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​The MICOS component Mic60 displays a conserved membrane-bending activity that is necessary for normal cristae morphology​
Tarasenko, D. ; Barbot, M. ; Jans, D. C. ; Kroppen, B. ; Sadowski, B. ; Heim, G.   & Möbius, W.  et al.​ (2017) 
The Journal of Cell Biology216(4) pp. 889​-899​.​ DOI: 

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Tarasenko, Daryna ; Barbot, Mariam ; Jans, Daniel C. ; Kroppen, Benjamin ; Sadowski, Boguslawa ; Heim, Gudrun ; Möbius, Wiebke ; Jakobs, Stefan ; Meinecke, Michael 
The inner membrane (IM) of mitochondria displays an intricate, highly folded architecture and can be divided into two domains: the inner boundary membrane adjacent to the outer membrane and invaginations toward the matrix, called cristae. Both domains are connected by narrow, tubular membrane segments called cristae junctions (CJs). The formation and maintenance of CJs is of vital importance for the organization of the mitochondrial IM and for mitochondrial and cellular physiology. The multisubunit mitochondrial contact site and cristae organizing system (MICOS) was found to be a major factor in CJ formation. In this study, we show that the MICOS core component Mic60 actively bends membranes and, when inserted into prokaryotic membranes, induces the formation of cristae-like plasma membrane invaginations. The intermembrane space domain of Mic60 has a lipid-binding capacity and induces membrane curvature even in the absence of the transmembrane helix. Mic60 homologues from α-proteobacteria display the same membrane deforming activity and are able to partially overcome the deletion of Mic60 in eukaryotic cells. Our results show that membrane bending by Mic60 is an ancient mechanism, important for cristae formation, and had already evolved before α-proteobacteria developed into mitochondria.
Issue Date
The Journal of Cell Biology 
SFB 1190: Transportmaschinen und Kontaktstellen zellulärer Kompartimente 
SFB 1190 | P01: Untersuchung der Unterschiede in der Zusammensetzung, Funktion und Position von individuellen MICOS Komplexen in einzelnen Säugerzellen 
SFB 1190 | P12: Funktionelle Regulation der mitochondrialen Präsequenz-Translokase 
Institut für Zellbiochemie 
Working Group
RG Jakobs (Structure and Dynamics of Mitochondria) 
RG Meinecke (Molecular Membrane Biology) 



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