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Regulatory Role of Ubiquitin Specific Protease-13 (USP13) in Misfolded Protein Clearance in Neurodegenerative Diseases

机译:泛素特异性蛋白酶-13(USP13)在神经变性疾病中错误折叠蛋白质清除的调节作用

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摘要

Specific Protease (USP)-13 is a de-ubiquitinase member of the cysteine-dependent protease superfamily that cleaves ubiquitin off protein substrates to reverse ubiquitin-mediated protein degradation. Several findings implicate USPs in neurodegeneration. Ubiquitin targets proteins to major degradation pathways, including the proteasome and the lysosome. In melanoma cells, USP13 regulates the degradation of several proteins primarily via ubiquitination and de-ubiquitination. However, the significance of USP13 in regulating protein clearance in neurodegeneration is largely unknown. This mini-review summarizes the most recent evidence pertaining to the role of USP13 in protein clearance via autophagy and the proteasome in neurodegenerative diseases. ? 2021 IBRO. Published by Elsevier Ltd. All rights reserved.
机译:特异性蛋白酶(USP)-13是半胱氨酸依赖性蛋白酶超家族中的去泛素酶成员,可将泛素从蛋白质底物上切割下来,以逆转泛素介导的蛋白质降解。一些发现暗示USPs与神经退行性变有关。泛素将蛋白质定位于主要降解途径,包括蛋白酶体和溶酶体。在黑色素瘤细胞中,USP13主要通过泛素化和去泛素化调节几种蛋白质的降解。然而,USP13在神经退行性变中调节蛋白清除的意义尚不清楚。这篇小综述总结了有关USP13通过自噬和蛋白酶体在神经退行性疾病中的蛋白质清除作用的最新证据?2021 IBRO。爱思唯尔有限公司出版。版权所有。

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