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  Structural insights into crista junction formation by the Mic60-Mic19 complex

Bock-Bierbaum, T., Funck, K., Wollweber, F., Lisicki, E., von der Malsburg, K., von der Malsburg, A., et al. (2022). Structural insights into crista junction formation by the Mic60-Mic19 complex. Science Advances, 8(35): eabo4946. doi:10.1126/sciadv.abo494.

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Item Permalink: https://hdl.handle.net/21.11116/0000-000B-781B-1 Version Permalink: https://hdl.handle.net/21.11116/0000-000C-3B18-8
Genre: Journal Article

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 Creators:
Bock-Bierbaum, Tobias, Author
Funck, Kathrin, Author
Wollweber, Florian, Author
Lisicki, Elisa, Author
von der Malsburg, Karina, Author
von der Malsburg, Alexander, Author
Laborenz, Janina, Author
Noel, Jeffrey K., Author
Hessenberger, Manuel, Author
Jungbluth, Sibylle, Author
Bernert, Carola, Author
Kunz, Séverine, Author
Riedel, D.1, Author           
Lilie, Hauke, Author
Jakobs, Stefan2, Author                 
van der Laan, Martin, Author
Daumke, Oliver, Author
Affiliations:
1Department of Structural Dynamics, Max Planck Institute for Multidisciplinary Sciences, Max Planck Society, ou_3350272              
2Research Group of Mitochondrial Structure and Dynamics, Max Planck Institute for Multidisciplinary Sciences, Max Planck Society, ou_3350049              

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 Abstract: Mitochondrial cristae membranes are the oxidative phosphorylation sites in cells. Crista junctions (CJs) form the highly curved neck regions of cristae and are thought to function as selective entry gates into the cristae space. Little is known about how CJs are generated and maintained. We show that the central coiled-coil (CC) domain of the mitochondrial contact site and cristae organizing system subunit Mic60 forms an elongated, bow tie–shaped tetrameric assembly. Mic19 promotes Mic60 tetramerization via a conserved interface between the Mic60 mitofilin and Mic19 CHCH (CC-helix-CC-helix) domains. Dimerization of mitofilin domains exposes a crescent-shaped membrane-binding site with convex curvature tailored to interact with the curved CJ neck. Our study suggests that the Mic60-Mic19 subcomplex traverses CJs as a molecular strut, thereby controlling CJ architecture and function.

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Language(s): eng - English
 Dates: 2022-08-31
 Publication Status: Published online
 Pages: -
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 Table of Contents: -
 Rev. Type: Peer
 Identifiers: DOI: 10.1126/sciadv.abo494
 Degree: -

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Project name : This project was supported by grants from the Deutsche Forschungsgemeinschaft (FOR 2848/P06 to O.D., FOR 2848/Z1 to S.Ja. and D.R., and SFB 894/P20 and IRTG 1830 to M.v.d.L.), the ERC grant MitoShape (ERC-2013-CoG-616024 to O.D.), the ERC grant MitoCristae (ERCAdG no. 835102 to S.Ja.), a Humboldt fellowship to J.K.N., a Boehringer Ingelheim Fonds fellowship to F.W., and a DOC Fellowship of the Austrian Academy of Sciences to M.H.
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Funding organization : -
Project name : MitoShape
Grant ID : ERC-2013-CoG-616024
Funding program : -
Funding organization : European Research Council
Project name : MitoCristae ERCAdG
Grant ID : 835102
Funding program : -
Funding organization : European Research Council

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Title: Science Advances
  Other : Sci. Adv.
Source Genre: Journal
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Publ. Info: Washington : AAAS
Pages: - Volume / Issue: 8 (35) Sequence Number: eabo4946 Start / End Page: - Identifier: ISSN: 2375-2548
CoNE: https://pure.mpg.de/cone/journals/resource/2375-2548