Structural insights into crista junction formation by the Mic60-Mic19 complex-Reference-Cited by-同舟云学术

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

Published:2022-09-02 Issue:35 Volume:8 Page:
ISSN:2375-2548
Container-title:Science Advances
language:en
Short-container-title:Sci. Adv.

Author:

Bock-Bierbaum Tobias¹^ORCID,Funck Kathrin¹²^ORCID,Wollweber Florian³^ORCID,Lisicki Elisa¹²^ORCID,von der Malsburg Karina³,von der Malsburg Alexander³,Laborenz Janina³,Noel Jeffrey K.¹^ORCID,Hessenberger Manuel¹^ORCID,Jungbluth Sibylle³,Bernert Carola¹,Kunz Séverine⁴^ORCID,Riedel Dietmar⁵^ORCID,Lilie Hauke⁶,Jakobs Stefan⁷⁸⁹^ORCID,van der Laan Martin³^ORCID,Daumke Oliver¹²^ORCID

Affiliation:

1. Structural Biology, Max Delbrück Center for Molecular Medicine in the Helmholtz Association (MDC), Berlin, Germany.

2. Institute of Chemistry and Biochemistry, Freie Universität Berlin, Berlin, Germany.

3. Medical Biochemistry and Molecular Biology, Center for Molecular Signaling (PZMS), Saarland University Medical School, Homburg, Saarland, Germany.

4. Technology Platform for Electron Microscopy, Max Delbrück Center for Molecular Medicine in the Helmholtz Association (MDC), Berlin, Germany.

5. Laboratory of Electron Microscopy, Max Planck Institute for Biophysical Chemistry, Göttingen, Germany.

6. Institute of Biochemistry and Biotechnology, Section of Protein Biochemistry, Martin Luther University Halle-Wittenberg, Halle/Saale, Germany.

7. Research Group Mitochondrial Structure and Dynamics, Max Planck Institute for Multidisciplinary Sciences, Göttingen, Germany.

8. Clinic for Neurology, University Medical Center Göttingen, Göttingen, Germany.

9. Translational Neuroinflammation and Automated Microscopy, Fraunhofer Institute for Translational Medicine and Pharmacology ITMP, Göttingen, Germany.

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.

Publisher

American Association for the Advancement of Science (AAAS)

Subject

Multidisciplinary

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