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Mitochondria perform diverse functions within eukaryotic cells that are essential to their survival however, under physiological conditions, they are exposed to pleiotropic stress including reactive oxygen species and misfolded and aggregated proteins that cause mitochondrial dysfunction ( 1, 2). These findings will aid future studies to understand Parkin activation in neuronal subtypes. Last, we have developed an online resource to search for ubiquitin sites and enzymes in mitochondria of neurons, MitoNUb. We also identified a subset of cytoplasmic proteins recruited to mitochondria that undergo PINK1 and Parkin independent ubiquitylation, indicating the presence of alternate ubiquitin E3 ligase pathways that are activated by mitochondrial depolarization in neurons. We use reconstitution assays to demonstrate direct ubiquitylation by Parkin in vitro. Comparative analysis with human iNeuron datasets revealed a subset of 49 PINK1 activationвЂ“dependent diGLY sites in 22 proteins conserved across mouse and human systems. Here, we have undertaken proteomic analysis of mitochondria from mouse neurons to identify ubiquitylated substrates of endogenous Parkin.

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