Damaged, denatured and aggregated proteins are toxic to the cell (proteotoxicity) through loss of protein function, disruption of membrane structure and trafficking, production of reactive oxygen species, and other mechanisms, often leading to cell death. With its short life cycle, suitability for fluorescent imaging, and availability of genetic tools, Drosophila melanogaster is particularly well suited for this kind of analysis.ĭecreased protein and mitochondrial turnover during agingĬellular proteins are susceptible to numerous types of damage, including hydrolysis, oxidative damage, glycation, cross-linking, denaturation and aggregation. In vivo assays are especially useful for connecting turnover to aging and disease. Both cell culture and live animals have been used for these studies, in systems ranging from yeast to mammals. Several methods exist, including pulse-labelling with radioactive or stable isotopes and strategies making use of fluorescent proteins, each with their own advantages and limitations. To achieve this, reliable assays of turnover must be developed. Changes in protein and mitochondrial turnover are associated with aging and neurodegenerative disease, making it important to understand how these processes occur and are regulated in cells. Damaged mitochondria must also be removed and replaced. Maintaining a balance between these processes, known as protein turnover, is necessary for stress response and cellular adaptation to a changing environment. To maintain homoeostasis, cells must degrade damaged or misfolded proteins and synthesize functional replacements.
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