Sugiyama Shinju, Tanaka Motomasa
Laboratory for Protein Conformation Diseases, RIKEN Brain Science Institute, Wako 351-0198, Japan and Department of Biological Information, Graduate School of Bioscience and Biotechnology, Tokyo Institute of Technology, Yokohama 226-8501, JapanLaboratory for Protein Conformation Diseases, RIKEN Brain Science Institute, Wako 351-0198, Japan and Department of Biological Information, Graduate School of Bioscience and Biotechnology, Tokyo Institute of Technology, Yokohama 226-8501, Japan.
Laboratory for Protein Conformation Diseases, RIKEN Brain Science Institute, Wako 351-0198, Japan and Department of Biological Information, Graduate School of Bioscience and Biotechnology, Tokyo Institute of Technology, Yokohama 226-8501, JapanLaboratory for Protein Conformation Diseases, RIKEN Brain Science Institute, Wako 351-0198, Japan and Department of Biological Information, Graduate School of Bioscience and Biotechnology, Tokyo Institute of Technology, Yokohama 226-8501, Japan
J Biochem. 2014 Jun;155(6):345-51. doi: 10.1093/jb/mvu026. Epub 2014 Apr 7.
Amyloids are β-sheet-rich fibrillar protein aggregates characterized by structural properties of self-propagation and strong resistance to detergent and proteinase. Although a number of causative proteins for neurodegenerative disorders are known to undergo amyloid formation, recent studies have revealed that amyloids may also play beneficial roles in cells. Cellular processes that could be regulated by amyloids are diverse and include translational regulation, programmed cell death and protein storage. Yeast prions of Mod5 and Mot3, non-Mendelian extra-chromosomal factors, also show amyloid-like biophysical properties and have recently been shown to confer host cells resistant to environmental stressors. Furthermore, yeast cells actively respond to environmental stress for fitness adaptation to environmental changes by converting soluble yeast prion proteins into their amyloid forms, allowing cells to survive under stress conditions. Therefore, amyloids are not simply the terminal end-products of protein misfolding but a growing body of evidence suggests that they may possess physiological roles by using their self-propagating properties. Here, we present an overview on recent progress of the research on such functional amyloids.
淀粉样蛋白是富含β-折叠的纤维状蛋白质聚集体，其特征在于具有自我传播的结构特性以及对去污剂和蛋白酶的强抗性。尽管已知许多神经退行性疾病的致病蛋白会形成淀粉样蛋白，但最近的研究表明，淀粉样蛋白在细胞中也可能发挥有益作用。可能受淀粉样蛋白调节的细胞过程多种多样，包括翻译调控、程序性细胞死亡和蛋白质储存。酵母中的Mod5和Mot3朊病毒，即非孟德尔染色体外因子，也表现出类似淀粉样蛋白的生物物理特性，并且最近已证明它们能使宿主细胞抵抗环境应激源。此外，酵母细胞通过将可溶性酵母朊病毒蛋白转化为淀粉样蛋白形式，积极响应环境应激，以适应环境变化，从而使细胞能够在应激条件下存活。因此，淀粉样蛋白不仅仅是蛋白质错误折叠的终产物，越来越多的证据表明，它们可能通过利用自身的自我传播特性而具有生理作用。在此，我们概述了此类功能性淀粉样蛋白的最新研究进展。
