Why size matters – balancing mitochondrial dynamics in Alzheimer's disease
| Autor: | Brian DuBoff, Mel B. Feany, Jürgen Götz |
|---|---|
| Rok vydání: | 2013 |
| Předmět: |
Dynamins
Models Neurological Nerve Tissue Proteins tau Proteins GTPase Mitochondrion Biology Receptors Metabotropic Glutamate Axonal Transport Membrane Fusion Mitochondrial Membrane Transport Proteins GTP Phosphohydrolases Mitochondrial Proteins Synapse Pathogenesis Mice Adenosine Triphosphate Alzheimer Disease Charcot-Marie-Tooth Disease Organelle medicine Animals Humans Actin Neurons Amyloid beta-Peptides General Neuroscience Membrane Proteins Neurodegenerative Diseases medicine.disease Mitochondria Synapses Energy Metabolism Microtubule-Associated Proteins Neuroscience Function (biology) Frontotemporal dementia |
| Zdroj: | Trends in Neurosciences. 36:325-335 |
| ISSN: | 0166-2236 |
| Popis: | Once perceived as solitary structures, mitochondria are now recognized as highly dynamic, interconnected organelles. The tight control of their fusion and fission, a process termed 'mitochondrial dynamics', is crucial for neurons, given their unique architecture and special energy and calcium-buffering requirements at the synapse. Interestingly, in Alzheimer's disease (AD), a condition initiated at the synapse, mitochondrial dynamics are severely impaired. Of the two proteins implicated in AD pathogenesis, amyloid-β (Aβ) and TAU, only the impact of Aβ on mitochondrial dynamics has been studied in detail. We highlight recent findings that TAU exerts a determinative effect in the regulation of mitochondrial dynamics, and therefore neuronal function. In this process, the GTPase DRP1 has emerged as a key target of both Aβ and TAU. |
| Databáze: | OpenAIRE |
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