相关实验视频
Updated: Jan 12, 2026

10:55
Purification of Ubiquitinated p53 Proteins from Mammalian Cells
Published on: March 21, 2022
2.7K
使用带有信号的ubiquitin提高了蛋白质聚合物去除效率
1Department of Life Science, University of Seoul, Seoul 02504, Korea.
BMB reports
|October 31, 2025
概括
利波卡林-2 (LCN2) 的信号 (SP) 可以引导无素 (Ub) 进行蛋白质聚合物的分泌和自清除. 这种改性无素 (UbE) 有助于清除有毒蛋白质的积累,而不会改变其核心功能.
科学领域:
- 细胞生物学 细胞生物学
- 贩卖蛋白质 贩卖蛋白质 是一个问题.
- 自自是一种自的过程.
背景情况:
- 利波卡林-2 (LCN2) 由星球细胞分泌,其信号 (SP) 对于分泌和自至关重要.
- SP将蛋白质引导到内 плазма网膜 (ER),并影响它们的后ER通路.
- 由ER产生的蛋白质可以分泌或进入自通路.
研究的目的:
- 在一个新的背景下研究LCN2的SP的功能作用.
- 确定LCN2 SP是否可以改变细胞内蛋白质的运输和降解.
- 为了检查SP-fused ubiquitin (UbE) 对蛋白质聚合物的清除的影响.
主要方法:
- LCN2 SP的融合到乌比奎丁 (Ub) 的N端.
- 分析Ub分泌和向自道的分析.
- 评估细胞内UB合物水平和降解.
- 在蛋白质毒性压力下对UBE在多比基因化和侵略性形成中的作用的研究.
主要成果:
- SP促进了自由Ub的分泌,并准了Ub对自的结合物.
- SP通过自途径调节了细胞内UB结合体的降解.
- 由ER生成的Ub (UbE) 增强了蛋白质聚合物的多基化,促进了侵袭体的形成和自体的招募.
- 在自细胞招募之前,UBE似乎与蛋白质聚合物共享一个贩运路线.
结论:
- LCN2 SP可以改变到无处不在的贩运途径.
- 通过改变其贩运,Ube通过自促进蛋白质聚合物的清除.
- 这种机制有助于清除有毒的蛋白质聚合物,而不会影响乌比奎的内在生化活性.
相关概念视频
The Proteasome
1.6K
Eukaryotic cells can degrade proteins through several pathways. One of the most important among 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. This involves participation of a series of enzymes including— E1 (ubiquitin-activating enzyme), E2 (ubiquitin-conjugating enzyme), and E3...
In this pathway, the target proteins are first tagged with small proteins called ubiquitin. This involves participation of a series of enzymes including— E1 (ubiquitin-activating enzyme), E2 (ubiquitin-conjugating enzyme), and E3...
1.6K
The Proteasome
10.0K
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...
10.0K
Regulated Protein Degradation
8.7K
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...
8.7K
Tagging and Fusion Proteins
8.3K
Proteins are involved in several cellular processes and biochemical reactions. Analyzing a specific protein of interest requires it to be isolated from the other proteins in the cell. This is achieved by overexpressing the specific gene in a suitable host to produce large quantities of the target protein. A tag or label is recombined with the gene to produce a fusion protein containing the target protein and the tag. The tags on these fusion proteins can then be used for easy detection and...
8.3K
The Proteasome Structure
1.6K
The ubiquitin-proteasome pathway is a well-known mechanism utilized by eukaryotic cells to remove cytoplasmic proteins that are misfolded, damaged, or no longer needed. In this pathway, the protein that needs to be eliminated undergoes a process called ubiquitination, where a chain of ubiquitin molecules is attached to the 48th lysine residue of the target protein. This ubiquitin modification helps the proteasome distinguish between a target protein and a healthy protein.
The proteasome is an...
The proteasome is an...
1.6K
Export of Misfolded Proteins out of the ER
5.0K
After folding, the ER assesses the quality of secretory and membrane proteins. The correctly folded proteins are cleared by the calnexin cycle for transport to their final destination, while misfolded proteins are held back in the ER lumen. The ER chaperones attempt to unfold and refold the misfolded proteins but sometimes fail to achieve the correct native conformation. Such terminally misfolded proteins are then exported to the cytosol by ER-associated degradation or ERAD pathway for...
5.0K

