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• W11068306 abstract "Autophagy, the evolutionarily conserved lysosome-based degradation system, has been the topic of intensive investigation for the past two decades. The recent explosion of interest can be explained in part by the emerging role of autophagy in pathogenesis and progression of major human diseases, such as neurodegeneration, infection diseases, and cancer. One of the key aspects of autophagy, which is of great importance for the disease-related roles of autophagy and yet remains frequently overlooked, is its remarkable selectivity. Aggregated proteins, damaged mitochondria, superfluous peroxisomes, or invading bacteria are specifically recognized and targeted to the lysosome for destruction by selective autophagy. Research over the past 5 years has identified a number of receptor proteins that bind molecular determinants of the autophagic cargo, leading to nucleation and expansion of the autophagosome around the target structure. Ubiquitin, the small protein modifier, has proven to be one such determinant, which, in addition to protein substrates, earmarks organelles and microbes for selective recognition by the autophagosome. Ubiquitin-like members of the Atg8/LC3/GABARAP protein family are core components of the autophagic machinery that become instrumental in the assembly of target-induced autophagosomes. The understanding of molecular mechanisms of selective clearance of pathogenic structures (protein aggregates, damaged or obsolete organelles and microbes) holds promise for developing new strategies to fight infection, neurodegeneration, and cancer." @default.
• W11068306 created "2016-06-24" @default.
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• W11068306 date "2014-01-01" @default.
• W11068306 modified "2023-09-27" @default.
• W11068306 title "Selective Autophagy" @default.
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• W11068306 doi "https://doi.org/10.1016/b978-0-12-405877-4.00004-4" @default.
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