Arghavani Payam, Pirhaghi Mitra, Moosavi-Movahedi Faezeh, Mamashli Fatemeh, Hosseini Elnaz, Moosavi-Movahedi Ali Akbar
Institute of Biochemistry and Biophysics, University of Tehran, Tehran, 1417466191, Iran.
Curr Res Struct Biol. 2022 Dec 7;4:356-364. doi: 10.1016/j.crstbi.2022.11.002. eCollection 2022.
Protein oligomerization has two notable aspects: it is crucial for the performing cellular and molecular processes accurately, and it produces amyloid fibril precursors. Although a clear explanation for amyloidosis as a whole is lacking, most studies have emphasized the importance of protein misfolding followed by formation of cytotoxic oligomer structures, which are responsible for disorders as diverse as neurodegenerative diseases, such as Alzheimer's and Parkinson's diseases, and metabolic disorders, such as type 2 diabetes. Constant surveillance by oligomeric protein structures known as molecular chaperones enables cells to overcome the challenge of misfolded proteins and their harmful assemblies. These molecular chaperones encounter proteins in cells, and benefit cell survival as long as they perform correctly. Thus, this review highlights the roles of structural aspects of chaperone protein oligomers in determining cell fate-either succumbing to amyloid oligomers or survival-as well as experimental approaches used to investigate these entities.
它对于准确执行细胞和分子过程至关重要，并且会产生淀粉样纤维前体。尽管目前尚缺乏对整个淀粉样变性的清晰解释，但大多数研究都强调了蛋白质错误折叠继而形成细胞毒性寡聚体结构的重要性，这些结构与多种疾病有关，如神经退行性疾病（如阿尔茨海默病和帕金森病）以及代谢紊乱（如2型糖尿病）。被称为分子伴侣的寡聚蛋白质结构持续进行监测，使细胞能够克服错误折叠蛋白质及其有害聚集体带来的挑战。这些分子伴侣在细胞中与蛋白质相遇，只要它们正常发挥作用，就能促进细胞存活。因此，本综述强调了伴侣蛋白寡聚体的结构方面在决定细胞命运（要么屈服于淀粉样寡聚体，要么存活）中的作用，以及用于研究这些实体的实验方法。
