PERM1 interacts with the MICOS-MIB complex to connect the mitochondria and sarcolemma via ankyrin B.
basic_science · Level V
Where this comes from
- Record sourced from PubMed, PMID 34385433.
- Also identified by DOI 10.1038/s41467-021-25185-3 and PMC identifier 8361071.
- Licence recorded as CC BY.
- The licence permits redistribution, so the abstract is shown in full and the full text is available from the publisher.
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.
Medical subject headings
- Ankyrins
- Mitochondria, Muscle
- Multiprotein Complexes
- Muscle Proteins
- Sarcolemma