乌比基因特异性酶3:一种新兴的双基因酶,可以调节生理和疾病
Yizhu Wang1, Yanlong Shi1, Kaiyi Niu1
1Hepatopancreatobiliary Center, The Second Affiliated Hospital of Nanjing Medical University, Nanjing, Jiangsu, 210003, China.
Cell death discovery
|May 21, 2024
概括
乌比基特异性酶3 (USP3) 是一种对修复DNA损伤和免疫反应至关重要的二维基基酶. 在癌症中异常USP3表达突出了其作为治疗点的潜力.
科学领域:
- 生物化学 生物化学
- 分子生物学分子生物学
- 遗传学 遗传学 是一个
背景情况:
- 蛋白质对于生命活动至关重要,需要正常化以保持生物体的健康.
- 无素-蛋白酶体系统 (UPS) 通过无素化来调节蛋白质质量和寿命.
- 像USP3一样的deubiquitinases (DUBs) 抵消了无处不在,维持了细胞平衡.
研究的目的:
- 审查目前关于乌比奎丁特异性酶3 (USP3) 的研究.
- 阐明USP3的结构,功能和疾病中的作用.
- 突出USP3作为一个潜在的治疗目标.
主要方法:
- 关于USP3.3现有研究的文献综述.
- 对USP3的结构和功能特征的分析.
- 简要介绍USP3在DNA损伤,免疫力和癌症中的作用.
主要成果:
- USP3是一种二维基因酶和染色质修饰剂,调节DNA损伤反应 (DDR) 和基因组完整性.
- USP3在炎症囊泡和天生的免疫力中起着关键作用.
- 在各种癌症中,USP3经常过度表达,包括胃癌,质母细胞瘤和神经母细胞瘤.
结论:
- USP3对于保持基因组稳定性和免疫功能至关重要.
- 失调USP3与多种癌症和疾病有关.
- USP3代表了新型癌症治疗的有希望的目标.
相关概念视频
Regulated Protein Degradation
7.2K
It is vital to regulate the activity of enzymatic as well as non-enzymatic proteins inside the cell. This can be achieved either through creating a balance between their rate of synthesis and degradation or regulating the intrinsic activity of the protein. Both these regulation mechanisms play an essential role in the normal functioning of cells.
Protein degradation plays two important roles in the cells. It helps to protect cells from misfolded or damaged proteins before they lead to a...
Protein degradation plays two important roles in the cells. It helps to protect cells from misfolded or damaged proteins before they lead to a...
7.2K
The Proteasome
8.6K
Eukaryotic cells can degrade proteins through several pathways. One of the most important amongst these is the ubiquitin-proteasome pathway. It helps the cell eliminate the misfolded, damaged, or unwarranted cytoplasmic proteins in a highly specific manner.
In this pathway, the target proteins are first tagged with small proteins called ubiquitin. A series of enzymes carry out the ubiquitination of the target proteins - E1 (ubiquitin-activating enzyme), E2 (ubiquitin-conjugating enzyme), and E3...
In this pathway, the target proteins are first tagged with small proteins called ubiquitin. A series of enzymes carry out the ubiquitination of the target proteins - E1 (ubiquitin-activating enzyme), E2 (ubiquitin-conjugating enzyme), and E3...
8.6K
Regulation of the Unfolded Protein Response
2.4K
Inositol-requiring kinase one or IRE1 is the most conserved eukaryotic unfolded protein response (UPR) receptor. It is a type I transmembrane protein kinase receptor with a distinctive site-specific RNase activity. As the binding mechanics of the misfolded proteins with the N-terminal domain of IRE-1 are unclear, three binding models — direct, indirect, and allosteric -- are proposed for receptor activation. Nevertheless, it is known that once a misfolded protein associates with IRE1, it...
2.4K
The Unfolded Protein Response
4.5K
The ER is the hub of protein synthesis in a cell. It has robust systems to quality control protein folding and also for degradation of terminally misfolded proteins. Under normal conditions, a small proportion of misfolded proteins that cannot be salvaged need to be transported to the cytoplasm by the ER-associated degradation or ERAD pathways. However, if the ERAD cannot handle the misfolded proteins, the cell activates the unfolded protein response or UPR to adjust the protein folding...
4.5K
Receptor Downregulation in MVBs
2.0K
Multivesicular bodies (MVBs) are mature endosomes that sort ubiquitinated proteins and then fuse with lysosomes to degrade the sorted proteins. Epidermal growth factor (EGF) and its receptor (EGFR) form a complex that can be internalized through endocytosis, sorted into an MVB, and later degraded.
The EGFR can initiate signaling pathways that lead to cell proliferation, migration, and differentiation. Overexpression of EGFR stimulates cells to proliferate. Excessive EGFR...
The EGFR can initiate signaling pathways that lead to cell proliferation, migration, and differentiation. Overexpression of EGFR stimulates cells to proliferate. Excessive EGFR...
2.0K
Covalently Linked Protein Regulators
6.8K
Proteins can undergo many types of post-translational modifications, often in response to changes in their environment. These modifications play an important role in the function and stability of these proteins. Covalently linked molecules include functional groups, such as methyl, acetyl, and phosphate groups, and also small proteins, such as ubiquitin. There are around 200 different types of covalent regulators that have been identified.
These groups modify specific amino acids in a protein....
These groups modify specific amino acids in a protein....
6.8K


