Miro clusters regulate ER-mitochondria contact sites and link cristae organization to the mitochondrial transport machinery

Souvik Modi (), Guillermo López-Doménech (), Elise F. Halff, Christian Covill-Cooke, Davor Ivankovic, Daniela Melandri, I. Lorena Arancibia-Cárcamo, Jemima J. Burden, Alan R. Lowe and Josef T. Kittler ()
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Souvik Modi: University College London
Guillermo López-Doménech: University College London
Elise F. Halff: University College London
Christian Covill-Cooke: University College London
Davor Ivankovic: University College London
Daniela Melandri: University College London
I. Lorena Arancibia-Cárcamo: University College London
Jemima J. Burden: University College London
Alan R. Lowe: University College London
Josef T. Kittler: University College London

Nature Communications, 2019, vol. 10, issue 1, 1-15

Abstract: Abstract Mitochondrial Rho (Miro) GTPases localize to the outer mitochondrial membrane and are essential machinery for the regulated trafficking of mitochondria to defined subcellular locations. However, their sub-mitochondrial localization and relationship with other critical mitochondrial complexes remains poorly understood. Here, using super-resolution fluorescence microscopy, we report that Miro proteins form nanometer-sized clusters along the mitochondrial outer membrane in association with the Mitochondrial Contact Site and Cristae Organizing System (MICOS). Using knockout mouse embryonic fibroblasts we show that Miro1 and Miro2 are required for normal mitochondrial cristae architecture and Endoplasmic Reticulum-Mitochondria Contacts Sites (ERMCS). Further, we show that Miro couples MICOS to TRAK motor protein adaptors to ensure the concerted transport of the two mitochondrial membranes and the correct distribution of cristae on the mitochondrial membrane. The Miro nanoscale organization, association with MICOS complex and regulation of ERMCS reveal new levels of control of the Miro GTPases on mitochondrial functionality.

Date: 2019
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DOI: 10.1038/s41467-019-12382-4

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