The expanding scope of amyloid signalling.

IF 1.9 3区 生物学 Q4 BIOCHEMISTRY & MOLECULAR BIOLOGY Prion Pub Date : 2021-12-01 DOI:10.1080/19336896.2021.1874791
Asen Daskalov, Sven J Saupe
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引用次数: 3

Abstract

Formation of higher-order supramolecular complexes has emerged as a common principle underlying activity of a number of immune and regulated cell-death signalling pathways in animals, plants and fungi. Some of these signalosomes employ functional amyloid motifs in their assembly process. The description of such systems in fungi finds its origin in earlier studies on a fungal prion termed [Het-s], originally identified as a non-Mendelian cytoplasmic infectious element. Janine Beisson has been a key contributor to such early studies. Recent work on this and related systems offers a more integrated view framing this prion in a broader picture including related signalling systems described in animals. We propose here an auto-commentary centred on three recent studies on amyloid signalling in microbes. Collectively, these studies increase our understanding of fold conservation in functional amyloids and the structural basis of seeding, highlight the relation of fungal amyloid motifs to mammalian RHIM (RIP homotypic interaction motif) and expand the concept of Nod-like receptor-based amyloid signalosomes to the prokaryote reign.

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淀粉样蛋白信号传导范围的扩大。
高阶超分子复合物的形成已成为动物、植物和真菌中许多免疫和受调节的细胞死亡信号通路活动的共同原理。其中一些信号体在其组装过程中使用功能性淀粉样蛋白基序。真菌中这种系统的描述起源于早期对一种称为[Het-s]的真菌朊病毒的研究,最初被确定为一种非孟德尔细胞质感染元素。珍妮·贝松(Janine Beisson)是此类早期研究的关键贡献者。最近对这一系统和相关系统的研究提供了一个更综合的观点,将这种朊病毒纳入更广泛的视野,包括动物中描述的相关信号系统。我们在这里提出一个自动评论集中在三个最近的研究淀粉样蛋白信号在微生物。总的来说,这些研究增加了我们对功能性淀粉样蛋白的折叠保护和播种的结构基础的理解,突出了真菌淀粉样蛋白基序与哺乳动物RHIM (RIP同型相互作用基序)的关系,并将基于nod样受体的淀粉样蛋白信号体的概念扩展到原核生物领域。
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来源期刊
Prion
Prion 生物-生化与分子生物学
CiteScore
5.20
自引率
4.30%
发文量
13
审稿时长
6-12 weeks
期刊介绍: Prion is the first international peer-reviewed open access journal to focus exclusively on protein folding and misfolding, protein assembly disorders, protein-based and structural inheritance. The goal is to foster communication and rapid exchange of information through timely publication of important results using traditional as well as electronic formats. The overriding criteria for publication in Prion are originality, scientific merit and general interest.
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