Mitochondrial dynamics in Parkinson's disease: a role for α-synuclein?

The distinctive pathological hallmarks of Parkinson's disease are the progressive death of dopaminergic neurons and the intracellular accumulation of Lewy bodies enriched in α-synuclein protein. Several lines of evidence from the study of sporadic, familial and pharmacologically induced forms of human Parkinson's disease also suggest that mitochondrial dysfunction plays an important role in disease progression. Although many functions have been proposed for α-synuclein, emerging data from human and animal models of Parkinson's disease highlight a role for α-synuclein in the control of neuronal mitochondrial dynamics. Here, we review the α-synuclein structural, biophysical and biochemical properties that influence relevant mitochondrial dynamic processes such as fusion-fission, transport and clearance. Drawing on current evidence, we propose that α-synuclein contributes to the mitochondrial defects that are associated with the pathology of this common and progressive neurodegenerative disease

Additional file 1 of Unraveling axonal mechanisms of traumatic brain injury

Additional file 1: Fig. S1. Characterization of injury system, Related to Fig. 1

Additional file 12 of Unraveling axonal mechanisms of traumatic brain injury

Additional file 12: Table S3. Kinase analysis results

Additional file 7 of Unraveling axonal mechanisms of traumatic brain injury

Additional file 7: Fig. S2. Membrane permeability and Ca2+ blockers dose response assessment, Related to Fig. 3

Additional file 20 of Unraveling axonal mechanisms of traumatic brain injury

Additional file 20. Key Resources Table: Table including antibodies, resources, kits, cells, and software with catalog numbers

Additional file 10 of Unraveling axonal mechanisms of traumatic brain injury

Additional file 10: Table S1. Proteomics original and processed data for both discovery and confirmatory experiments

Additional file 9 of Unraveling axonal mechanisms of traumatic brain injury

Additional file 9: Fig. S3. Axonal proteomic profiling before and immediately after injury, Related to Fig. 4

Additional file 13 of Unraveling axonal mechanisms of traumatic brain injury

Additional file 13: Fig. S4. Structural reorganization of the axonal cytoskeleton following injury, Related to Fig. 6

Additional file 11 of Unraveling axonal mechanisms of traumatic brain injury

Additional file 11: Table S2. Phosphoproteomics original data and detailed phosphorylation information