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Trafficking and degradation pathways in pathogenic conversion of prions and prion-like proteins in neurodegenerative diseases
Ist Teil von
Virus research, 2015-09, Vol.207, p.146-154
Ort / Verlag
Netherlands: Elsevier B.V
Erscheinungsjahr
2015
Quelle
MEDLINE
Beschreibungen/Notizen
•We cover recent work on the trafficking of prions and prion like proteins.•Subcellular localization and trafficking in seeding and conversion.•We discuss a biophysical basis for conversion: metastability.•Degradation pathways that may provide a cellular context favorable for conversion.
Several neurodegenerative diseases such as transmissible spongiform encephalopathies, Alzheimer's and Parkinson's diseases are caused by the conversion of cellular proteins to a pathogenic conformer. Despite differences in the primary structure and subcellular localization of these proteins, which include the prion protein, α-synuclein and amyloid precursor protein (APP), striking similarity has been observed in their ability to seed and convert naïve protein molecules as well as transfer between cells. This review aims to cover what is known about the intracellular trafficking of these proteins as well as their degradation mechanisms and highlight similarities in their movement through the endocytic pathway that could contribute to the pathogenic conversion and seeding of these proteins which underlies the basis of these diseases.