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

Tobias Bock-Bierbaum; Kathrin Funck; Florian Wollweber; Elisa Lisicki; Karina von der Malsburg; Alexander von der Malsburg; Janina Laborenz; Jeffrey K Noel; Manuel Hessenberger; Sibylle Jungbluth; Carola Bernert; Séverine Kunz; Dietmar Riedel; Hauke Lilie; Stefan Jakobs; Martin van der Laan; Oliver Daumke

doi:10.1126/sciadv.abo4946

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

Tobias Bock-Bierbaum, Kathrin Funck, Florian Wollweber, Elisa Lisicki, Karina von der Malsburg, Alexander von der Malsburg, Janina Laborenz, Jeffrey K Noel, Manuel Hessenberger, Sibylle Jungbluth, Carola Bernert, Séverine Kunz, Dietmar Riedel, Hauke Lilie, Stefan Jakobs, Martin van der Laan, Oliver Daumke

Research output: Journal article (peer-reviewed) › Journal article

15 Citations (Scopus)

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.

Original language	English
Article number	eabo4946
Pages (from-to)	eabo4946
Journal	Science advances
Volume	8
Issue number	35
DOIs	https://doi.org/10.1126/sciadv.abo4946
Publication status	Published - 02 Sept 2022
Externally published	Yes

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Bock-Bierbaum, T., Funck, K., Wollweber, F., Lisicki, E., von der Malsburg, K., von der Malsburg, A., Laborenz, J., Noel, J. K., Hessenberger, M., Jungbluth, S., Bernert, C., Kunz, S., Riedel, D., Lilie, H., Jakobs, S., van der Laan, M., & Daumke, O. (2022). Structural insights into crista junction formation by the Mic60-Mic19 complex. Science advances, 8(35), eabo4946. Article eabo4946. https://doi.org/10.1126/sciadv.abo4946

@article{bc47b7e18d6d4fd7b0ef84da57b24abb,

title = "Structural insights into crista junction formation by the Mic60-Mic19 complex",

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.",

author = "Tobias Bock-Bierbaum and Kathrin Funck and Florian Wollweber and Elisa Lisicki and {von der Malsburg}, Karina and {von der Malsburg}, Alexander and Janina Laborenz and Noel, {Jeffrey K} and Manuel Hessenberger and Sibylle Jungbluth and Carola Bernert and S{\'e}verine Kunz and Dietmar Riedel and Hauke Lilie and Stefan Jakobs and {van der Laan}, Martin and Oliver Daumke",

note = "Publisher Copyright: {\textcopyright} 2022 The Authors.",

year = "2022",

month = sep,

day = "2",

doi = "10.1126/sciadv.abo4946",

language = "English",

volume = "8",

pages = "eabo4946",

journal = "Science advances",

issn = "2375-2548",

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Bock-Bierbaum, T, Funck, K, Wollweber, F, Lisicki, E, von der Malsburg, K, von der Malsburg, A, Laborenz, J, Noel, JK, Hessenberger, M, Jungbluth, S, Bernert, C, Kunz, S, Riedel, D, Lilie, H, Jakobs, S, van der Laan, M & Daumke, O 2022, 'Structural insights into crista junction formation by the Mic60-Mic19 complex', Science advances, vol. 8, no. 35, eabo4946, pp. eabo4946. https://doi.org/10.1126/sciadv.abo4946

TY - JOUR

T1 - Structural insights into crista junction formation by the Mic60-Mic19 complex

AU - Bock-Bierbaum, Tobias

AU - Funck, Kathrin

AU - Wollweber, Florian

AU - Lisicki, Elisa

AU - von der Malsburg, Karina

AU - von der Malsburg, Alexander

AU - Laborenz, Janina

AU - Noel, Jeffrey K

AU - Hessenberger, Manuel

AU - Jungbluth, Sibylle

AU - Bernert, Carola

AU - Kunz, Séverine

AU - Riedel, Dietmar

AU - Lilie, Hauke

AU - Jakobs, Stefan

AU - van der Laan, Martin

AU - Daumke, Oliver

PY - 2022/9/2

Y1 - 2022/9/2

N2 - 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.

AB - 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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U2 - 10.1126/sciadv.abo4946

DO - 10.1126/sciadv.abo4946

M3 - Journal article

C2 - 36044574

SN - 2375-2548

VL - 8

SP - eabo4946

JO - Science advances

JF - Science advances

IS - 35

M1 - eabo4946

ER -

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

Abstract

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