Université Paris-Saclay, CEA, CNRS, Molecular Imaging Research Center (MIRCen), Laboratoire des Maladies Neurodégénératives (UMR9199), Fontenay-aux-Roses, France.
Curr Top Microbiol Immunol. 2021;432:57-66. doi: 10.1007/978-3-030-83391-6_6.
Infectious proteins or prions are self-replicating transmissible aggregates responsible for heritable traits in yeasts and amyloid diseases in mammals. Extensive investigations into the many prions discovered in the yeast Saccharomyces cerevisiae, and most importantly the [PSI] prion, shaped our understanding of the cellular mechanisms involved in amyloidosis. [PSI] arises from the assembly of the translation terminator Sup35p into insoluble fibrillar aggregates leading to nonsense suppression phenotypes. We recently found that infectious Sup35p particles traffic via extracellular (EV) and periplasmic (PV) vesicles in a growth phase and glucose-dependent manner. In this chapter, I will summarize these findings and explain how they fit in current models of yeast prions transmission.
传染性蛋白质或朊病毒是自我复制的可传播聚集物，负责酵母中的遗传特征和哺乳动物中的淀粉样疾病。对在酵母酿酒酵母中发现的许多朊病毒的广泛研究，尤其是[PSI]朊病毒，塑造了我们对淀粉样变性涉及的细胞机制的理解。[PSI]是由翻译终止子 Sup35p 组装成不溶性纤维状聚集体引起的无意义抑制表型。我们最近发现，传染性 Sup35p 颗粒通过细胞外（EV）和周质（PV）小泡在生长阶段和葡萄糖依赖性方式进行运输。在本章中，我将总结这些发现，并解释它们如何适应酵母朊病毒传播的当前模型。
