蛋白质酶子单元Rpn13是一种新型的无素受体
Koraljka Husnjak1, Suzanne Elsasser, Naixia Zhang
1Institute of Biochemistry II and Cluster of Excellence Macromolecular Complexes, Goethe University, Theodor-Stern-Kai 7, D-60590 Frankfurt (Main), Germany.
Nature
|May 24, 2008
概括
研究人员确定了Rpn13,一种新型的蛋白质体受体,它结合了无素链. 这一发现揭示了在选择性蛋白质降解过程中,乌比奎受体和二维奎化酶之间的功能联系.
科学领域:
- 分子生物学分子生物学
- 细胞生物学 细胞生物学
- 生物化学 生物化学
背景情况:
- 保护体受体对于真核生物中选择性蛋白质降解至关重要.
- 这些受体在基质蛋白上识别了无素链.
- Rpn13/ARM1是一种新发现的泛素受体,也是已知的蛋白酶组分.
研究的目的:
- 为了识别和描述参与蛋白质体降解的新型泛素受体.
- 阐明Rpn13.的功能和结合特性.
- 为了研究乌比奎受体和脱乌比奎化酶之间的相互作用.
主要方法:
- 蛋白质的识别和表征.
- 生物化学试验以确定乌比奎的结合亲和力 (K48相关的duibiquitin).
- 酵母遗传学评估Rpn10和Rpn13之间的功能联系.
主要成果:
- Rpn13拥有一个类似于pleckstrin的受体,用于结合K48结合的duibiquitin的ubiquitin (Pru) 域,这种受体具有很高的亲和力 (约90nM).
- 与Rpn10/S5a相似的Rpn13与UBL-ubiquitin关联蛋白 (UBA) 的泛类 (UBL) 域结合.
- 在酵母中Rpn10和Rpn13结合部位的组合突变导致合成表型,表明功能链接.
结论:
- Rpn13是一种新型的泛素受体,在选择性蛋白质降解中发挥作用.
- 在Rpn10和Rpn13泛素受体之间存在功能联系.
- 作为Rpn13受体的Rpn13作为受体的 deubiquitinating酶Uch37表明,在蛋白质酶的ubiquitin链识别和拆卸的合.
相关概念视频
The Proteasome
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 (ubiquitin...
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 (ubiquitin...
The Proteasome
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...
The Proteasome
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...
The Proteasome Structure
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...
Regulated Protein Degradation
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...
Regulation of the Unfolded Protein Response
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...


