The yeast Saccharomyces cerevisiae has proven to be a useful model system to investigate the mechanism of prion generation and inheritance, to which studies in Sup35 made a great contribution. Recent studies demonstrated that ‘protein misfolding and aggregation’ (i.e. amyloidogenesis) is a common principle underlying the pathogenesis of neurodegenerative diseases including prion, amyotrophic lateral sclerosis (ALS), Perkinson’s (PD), Alzheimer’s (AD) diseases and polyglutamine (polyQ) diseases such as spinocerebellar ataxia (SCA) and Hantington’s disease (HD). By these findings, the yeast has again been drawing increased attention as a useful system for studying neurodegenerative proteinopathies. So far, it has been reported that proteolytic cleavage of causative amyloidogenic proteins might affect the pathogenesis of the respective neurodegenerative diseases. Although those reports provide a clear phenomenological description, in the majority of cases, it has remained elusive if proteolysis is directly involved in the pathogenesis of the diseases. Recently, we have demonstrated in yeast that proteolysis suppresses prion generation. The yeast-based strategy might make a breakthrough to the unsolved issues.

酿酒酵母已被证明是研究朊病毒产生和遗传机制的有用模型系统，Sup35的研究对此做出了巨大贡献。最近的研究表明，“蛋白质错误折叠和聚集”（即淀粉样变）是神经退行性疾病发病机制的共同原理，包括朊病毒、肌萎缩侧索硬化症（ALS）、帕金森病（PD）、阿尔茨海默病（AD）和多聚谷氨酰胺（polyQ）疾病例如脊髓小脑性共济失调（SCA）和汉廷顿病（HD）。通过这些发现，酵母作为研究神经退行性蛋白质病的有用系统再次受到越来越多的关注。迄今为止，据报道，致病性淀粉样蛋白的蛋白水解切割可能会影响相应神经退行性疾病的发病机制。尽管这些报告提供了清晰的现象学描述，但在大多数情况下，蛋白水解是否直接参与疾病的发病机制仍然难以捉摸。最近，我们在酵母中证明蛋白水解可以抑制朊病毒的产生。基于酵母的策略可能会突破尚未解决的问题。