aggregopathies, neurodegeneration & genetics

protein aggregation is thought to be the pathological driving force responsible for neurodegenerative disorders such as alzheimer’s, parkinson’s, huntington’s, frontotemporal dementia, dementia with lewy bodies and prion diseases, however, it is not yet clear whether, or to what extent, the misfolded proteins are the cause of the diseases rather than the consequences. the aggregated proteins that are characteristic of these diseases have in common the ability to undergo conformational changes and often form fibrillar structures. it is postulated that these proteins may share similar pathways of aggregation. degradation of intracellular proteins via the ubiquitin-proteasome system (ups) is a highly complex, temporally controlled and tightly regulated process that plays major roles in a variety of cellular processes and aberrations in this system have been implicated, either as a primary cause or secondary consequences, in the pathogenesis of neurodegenerative diseases. we will give a brief overview of the possible role of proteasome dysfunction and protein aggregation in neurodegeneration and genetics of synucleinopathies and taupathies and prion protein.