Miro phosphorylation sites regulate Parkin recruitment and mitochondrial motility

In mitophagy, damaged mitochondria stabilize PTEN-induced putative kinase 1 (PINK1) and recruit Parkin, an E3-ligase that ubiquitinates proteins on the outer membrane and targets mitochondria for degradation. The crucial roles of PINK1 phosphorylation of Parkin and ubiquitin in mitophagy are well-established. Other substrates of PINK1, however, have also been reported but the significance of those phosphorylations is less clear. We now show that Miro phosphorylations can regulate Parkin recruitment to Miro and trigger Miro degradation. The consequence of this branch of the PINK1/Parkin pathway is the disruption of mitochondrial motility, an event that may spatially restrict the deleterious effects of mitochondrial damage prior to the mitophagic removal of the organelle.