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作 者:吴佳莲 WU Jialian(South China Agricultural University,Guangzhou 510000,China)
机构地区:[1]华南农业大学,广东广州510000
出 处:《工业微生物》2025年第1期237-239,共3页Industrial Microbiology
摘 要:蛋白质二硫键异构酶(Protein disulfide isomerase,PDI)作为一类多功能氧化还原酶,参与蛋白质合成、折叠和修饰等多个过程。最新研究表明,酵母和哺乳动物体内的PDI与内质网甘露糖苷酶协同作用,参与一种特殊的内质网相关降解(Endoplasmic reticulum associated degradation,ERAD)途径,该途径通过修剪N-糖链上的甘露糖可以实现对错误折叠糖蛋白的处理。尽管研究人员已经从拟南芥(Arabidopsis thaliana)中鉴定出14种PDI,但它们是否参与植物ERAD过程及其作用机制尚不明晰。文章旨在探讨酵母、哺乳动物和植物中PDI家族的结构与功能,并着重讨论其氧化还原活性在与其他蛋白质相互作用过程中的重要性,以及PDIs与EDEMs复合体在植物中的保守性。当前的研究不断深入对PDI家族的认知,旨在逐渐揭示其多样性与复杂性,为理解蛋白质质量控制和错误折叠蛋白降解提供新的视角。Protein disulfide isomerase(PDI)is a kind of multifunctional oxidoreductase involved in several processes such as protein synthesis,folding,and modification.Recent studies have revealed the synergistic effect of PDI with endoplasmic reticulum mannosidase in yeast and mammals,which participates in a special endoplasmic reticulum associated degradation(ERAD)pathway.The pathway processes misfolded glycoproteins by trimming mannose on N-glycan chains.Although 14 PDIs have been identified in Arabidopsis thaliana,whether they participate in the plant ERAD process and their mechanism of action are still unclear.The purpose of this article is to investigate the structure and function of the PDIs in yeast,mammals and plants,with a focus on the importance of redox activity of PDIs in interactions with other proteins,and the conservation of PDIs and EDEMs complexes in plants.With the deepening of the understanding of the PDIs,it has gradually revealed their diversity and complexity,and provided a new perspective for understanding protein quality control and misfolded protein-related degradation.
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