Localized Proteasomal Degradation: From the Nucleus to Cell Periphery.

Localized Proteasomal Degradation: From the Nucleus to Cell Periphery.
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局部蛋白酶体降解:从细胞核到细胞外周

DOI:
10.3390/biom12020229
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发表时间:
2022-01-29
期刊:
影响因子:
5.5
通讯作者:
Guo X
Guo X
中科院分区:
生物学2区
文献类型:
--
作者:
Guo X

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蛋白酶体负责大多数细胞蛋白的选择性降解。蛋白酶体大量存在于细胞中,不仅在细胞质和细胞核中扩散,而且还与染色质、细胞骨架、各种膜和无膜细胞器/凝聚物结合。蛋白酶体如何以及为什么到达这些特定的亚细胞区室仍然知之甚少,尽管越来越多的证据支持细胞内定位可能对蛋白酶体的活性,底物可及性和稳定性/完整性产生深远影响的假设。在这篇简短的综述中,我总结了蛋白酶体的功能,调节和靶向机制的最新进展,特别是那些定位于细胞的核凝聚物和膜结构,我讨论了其在介导区室化蛋白质降解的生物学意义。
The proteasome is responsible for selective degradation of most cellular proteins. Abundantly present in the cell, proteasomes not only diffuse in the cytoplasm and the nucleus but also associate with the chromatin, cytoskeleton, various membranes and membraneless organelles/condensates. How and why the proteasome gets to these specific subcellular compartments remains poorly understood, although increasing evidence supports the hypothesis that intracellular localization may have profound impacts on the activity, substrate accessibility and stability/integrity of the proteasome. In this short review, I summarize recent advances on the functions, regulations and targeting mechanisms of proteasomes, especially those localized to the nuclear condensates and membrane structures of the cell, and I discuss the biological significance thereof in mediating compartmentalized protein degradation.
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