Parkinson's disease (PD) is one of the most common neurodegenerative disorders. The causes of PD remain elusive, but mitochondrial malfunction is likely to be an important component. PD-related proteins PINK1 and Parkin affect mitochondrial function and morphology and participate in mitochondrial quality control. In Volume 147 Issue 4 of Cell (2011 Nov), Wang et al. published a paper entitled “PINK1 and Parkin target Miro for phosphorylation and degradation to arrest mitochondrial motility”. They identify the mitochondrial outer-membrane protein Miro as a phosphorylation substrate of PINK1 and show that Miro is degraded through a Parkin-denpendent mechanism after phosphorylation. Destruction of Miro unhooks damaged mitochondria from the microtubule network and prevents mitochondrial movement. The PINK1/Parkin pathway may quarantine damaged mitochondria prior to their clearance. This study not only reveals a glimpse into how PINK1 and Parkin cooperate, but also shows that mitochondrial quality control system can directly alter mitochondrial transport and raises the possibility that one cause of PD is the inappropriate transport of damaged mitochondria.