We find that the assembly/abundance control of a complex containing the mitochondrial trafficking adaptor MIRO depends on the spatial partitioning of the ARMC1 protein between the cytosol and distinct mitochondrial complexes.
ARMC1 assembles into a complex with MIRO that antagonizes retrograde mitochondrial movement. In another complex, ARMC1 associates with DNAJC11, which promotes ARMC1 removal from the mitochondrial surface. This balanced partitioning is important for steady-state mitochondrial distribution.
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