PERM1 interacts with the MICOS-MIB complex to connect the mitochondria and sarcolemma via ankyrin B
Theresa Bock,
Clara Türk,
Sriram Aravamudhan,
Lena Keufgens,
Wilhelm Bloch,
Dieu Hien Rozsivalova,
Vanina Romanello,
Leonardo Nogara,
Bert Blaauw,
Aleksandra Trifunovic,
Thomas Braun and
Marcus Krüger ()
Additional contact information
Theresa Bock: Cologne Excellence Cluster on Cellular Stress Responses in Aging-Associated Diseases (CECAD)
Clara Türk: BASF SE, Metabolomics and Proteomics
Sriram Aravamudhan: Cell Signaling Technology
Lena Keufgens: Cologne Excellence Cluster on Cellular Stress Responses in Aging-Associated Diseases (CECAD)
Wilhelm Bloch: German Sport University Cologne
Dieu Hien Rozsivalova: Cologne Excellence Cluster on Cellular Stress Responses in Aging-Associated Diseases (CECAD)
Vanina Romanello: University of Padova
Leonardo Nogara: University of Padova
Bert Blaauw: University of Padova
Aleksandra Trifunovic: Cologne Excellence Cluster on Cellular Stress Responses in Aging-Associated Diseases (CECAD)
Thomas Braun: Max Planck Institute for Heart and Lung Research
Marcus Krüger: Cologne Excellence Cluster on Cellular Stress Responses in Aging-Associated Diseases (CECAD)
Nature Communications, 2021, vol. 12, issue 1, 1-15
Abstract:
Abstract Skeletal muscle subsarcolemmal mitochondria (SSM) and intermyofibrillar mitochondria subpopulations have distinct metabolic activity and sensitivity, though the mechanisms that localize SSM to peripheral areas of muscle fibers are poorly understood. A protein interaction study and complexome profiling identifies PERM1 interacts with the MICOS-MIB complex. Ablation of Perm1 in mice reduces muscle force, decreases mitochondrial membrane potential and complex I activity, and reduces the numbers of SSM in skeletal muscle. We demonstrate PERM1 interacts with the intracellular adaptor protein ankyrin B (ANKB) that connects the cytoskeleton to the plasma membrane. Moreover, we identify a C-terminal transmembrane helix that anchors PERM1 into the outer mitochondrial membrane. We conclude PERM1 functions in the MICOS-MIB complex and acts as an adapter to connect the mitochondria with the sarcolemma via ANKB.
Date: 2021
References: Add references at CitEc
Citations:
Downloads: (external link)
https://www.nature.com/articles/s41467-021-25185-3 Abstract (text/html)
Related works:
This item may be available elsewhere in EconPapers: Search for items with the same title.
Export reference: BibTeX
RIS (EndNote, ProCite, RefMan)
HTML/Text
Persistent link: https://EconPapers.repec.org/RePEc:nat:natcom:v:12:y:2021:i:1:d:10.1038_s41467-021-25185-3
Ordering information: This journal article can be ordered from
https://www.nature.com/ncomms/
DOI: 10.1038/s41467-021-25185-3
Access Statistics for this article
Nature Communications is currently edited by Nathalie Le Bot, Enda Bergin and Fiona Gillespie
More articles in Nature Communications from Nature
Bibliographic data for series maintained by Sonal Shukla () and Springer Nature Abstracting and Indexing ().