Elisa Lisicki

Max Delbrück Center

Author Statistics

Papers

Citation

H-Index

i-10 index

Research Trends

Author Order

Document Type

Co-Authors

Stefan Jakobs

Max Planck Institute for Biophysical Chemistry

Oliver Daumke

Freie Universität Berlin

Manuel Hessenberger

Karl Landsteiner University of Health Sciences

Karina von der Malsburg

Saarland University

Jeffrey K. Noel

Max Delbrück Center

Florian Wollweber

ETH Zurich

Dietmar Riedel

Max Planck Institute for Multidisciplinary Sciences

Janina Laborenz

Saarland University

Alexander von der Malsburg

Saarland University

Hauke Lilie

Martin Luther University Halle-Wittenberg

Cooperative Institutions

Max Delbrück Center

Saarland University

University of Freiburg

Freie Universität Berlin

MRC Laboratory of Molecular Biology

Max Planck Institute for Biophysical Chemistry

Max Planck Institute for Multidisciplinary Sciences

Universitätsmedizin Göttingen

Max Planck Institute for Dynamics and Self-Organization

Charité - Universitätsmedizin Berlin

Author Statistics

Papers

Citation

H-Index

i-10 index

Research Field

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

Science Advances (2022)

Tobias Bock-Bierbaum Kathrin Funck Florian Wollweber Elisa Lisicki Karina von der Malsburg

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.

Crista

Helix (gastropod)

Coiled coil

10.1126/sciadv.abo4946

Cite

Citations (23)

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

bioRxiv (Cold Spring Harbor Laboratory) (2022)

Tobias Bock-Bierbaum Kathrin Funck Florian Wollweber Elisa Lisicki Janina Laborenz

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 domain of the mitochondrial contact and cristae organizing system (MICOS) 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 domains. Dimerization of mitofilin domains exposes a crescent-shaped membrane-binding site with convex curvature tailored to interact with curved CJ necks. Our study suggests that the Mic60-Mic19 subcomplex transverses CJs as a molecular strut, thereby controlling CJ architecture and function.

Crista

10.1101/2022.03.30.486340

Cite

Citations (1)