Abstract
The small GTPase Miro is best known for its regulation of mitochondrial movement by engaging with the microtubule-based motor proteins kinesin and dynein. Very recent findings have now showed that Miro also targets peroxisomes and regulates microtubule-dependent peroxisome motility. Moreover, Miro recruits and stabilizes the myosin motor Myo19 at the mitochondria to enable actin-based mitochondria movement, which is important for mitochondrial segregation during mitosis. Miro thus has much broader functions that previously known, and these new findings may have important implications on disease pathology.
Highlights
The small GTPase Mitochondrial Rho (Miro) is best known for its regulation of mitochondrial movement by engaging with the microtubule-based motor proteins kinesin and dynein
Miro1 was shown to be the primary regulator of mitochondrial transport in both axons and dendrites, with its deletion resulted in mitochondria depletion from distal dendrites and compromised neuronal viability [15]
Peroxisome-targeted Miro1 increased movement of peroxisomes in COS-7 cells and induced peroxisome proliferation in human skin fibroblasts. It induced long membrane protrusions in Pex5-deficient fibroblasts that co-localized with microtubules, suggesting that these are formed by the pulling forces generated by Miro1 and the microtubule-associated motors
Summary
The small GTPase Miro is best known for its regulation of mitochondrial movement by engaging with the microtubule-based motor proteins kinesin and dynein. The Miro GTPases are localized to the mitochondrial outer membrane and play critical roles in intracellular mitochondria movement in metazoans, over long distances along microtubule tracts in neurons [2], as well as mediating intercellular transport of mitochondria between cells via tunneling nanotubes [4]. Miro mediates bidirectional mitochondrial movement along microtubule tracts by engaging both kinesin and dynein [5], the former via the cargo adaptors of the Milton/Trak family [6,7,8,9].
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