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淀粉样蛋白信号转导的扩展范围。

The expanding scope of amyloid signalling.

机构信息

Institut de Biochimie et de Génétique Cellulaire (CNRS UMR 5095, Université de Bordeaux) , France.

出版信息

Prion. 2021 Dec;15(1):21-28. doi: 10.1080/19336896.2021.1874791.

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.

摘要

高等细胞外基质复合物的形成已成为动物、植物和真菌中许多免疫和调控细胞死亡信号通路活性的共同原则。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。这些系统在真菌中的描述源于对一种真菌朊病毒的早期研究,该朊病毒最初被称为非孟德尔细胞质传染性元件[Het-s]。Janine Beisson 是这些早期研究的主要贡献者。最近对该系统及相关系统的研究提供了一个更综合的视角,将朊病毒置于更广泛的图景中,包括在动物中描述的相关信号系统。我们在这里提出了一个以三篇关于微生物中淀粉样蛋白信号的最新研究为中心的自动评论。这些研究共同提高了我们对功能淀粉样蛋白折叠保守性和种子结构基础的理解,强调了真菌淀粉样蛋白基序与哺乳动物 RHIM(RIP 同源相互作用基序)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了原核领域。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/b8a4/7889193/3644a0cbebd1/KPRN_A_1874791_F0001_B.jpg

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