相关实验视频
Updated: May 25, 2025

08:33
Ubiquitin Chain Analysis by Parallel Reaction Monitoring
Published on: June 17, 2020
3.5K
乌比奎丁通过一种直接与蛋白质结合的单-ADP-ribose结合
Daniel S Bejan1, Rachel E Lacoursiere2, Jonathan N Pruneda3,4,5
1Department of Chemical Physiology and Biochemistry, Oregon Health & Science University, Portland, OR, 97239, USA.
The EMBO journal
|February 25, 2025
概括
这项研究揭示了一种新的双重翻译后修饰 (PTM),称为单-ADP-ribosyl无处不在 (MARUbylation),发生在PARP蛋白质上. 这一发现扩大了我们对细胞过程中ADP-ribosylation的理解.
科学领域:
- 生物化学 生物化学
- 分子生物学分子生物学
- 细胞生物学 细胞生物学
背景情况:
- 翻译后修改 (PTMs) 传统上涉及每种氨基酸的单个修改.
- 已经观察到PTM之间的交叉,如ADP-ribosylation和ubiquitylation.
- 之前的体外研究表明ADP-ribose的无处不在.
研究的目的:
- 为了证明细胞中出现双 PTM 的情况.
- 描述一种涉及ADP-ribosylation和ubiquitylation的新型双PTM.
- 为了研究这种新修饰的细胞功能和调节.
主要方法:
- 细胞测定检测双 PTMs.
- 化学和酶处理以分析修饰.
- 一种具有雌激酶活性的新型细菌二维基因酶的表征.
- 对外表达和内生修饰的PARP的分析.
主要成果:
- 在细胞中首次证明了双PTM:在PARP10上进行单-ADP-ribosyl无处不在化 (MARUbylation).
- 在Glu/Asp残留物上形成一个独特的MAR无素链.
- 在多个PARP上识别MARUbylation,通过K11连接的多比基链扩展.
- 在I型干扰素刺激后对PARP点观察到的内源性MARUbylation.
结论:
- MARUbylation 是一种在细胞中发生的新型双 PTM.
- 这种修改扩大了已知的PARP介导ADP-ribosylation的范围.
- MARUbylation 在细胞反应中发挥作用,例如对干扰素刺激.
相关概念视频
The Proteasome
796
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...
796
Regulated Protein Degradation
7.1K
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...
7.1K
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
Protein Modifications in the RER
5.0K
Modification of secretory and transmembrane proteins entering the rough ER begins in the ER lumen. These modifications aid in protein folding and stabilize the acquired tertiary structure. Protein modifications in the rough ER co-occur at different stages of protein folding.
Broadly, these modifications can be categorized into four main categories — glycosylation, formation of disulfide bonds, assembly of protein subunits, and specific proteolytic cleavages like removal of signal...
Broadly, these modifications can be categorized into four main categories — glycosylation, formation of disulfide bonds, assembly of protein subunits, and specific proteolytic cleavages like removal of signal...
5.0K
Post-translational Translocation of Proteins to the RER
5.5K
A sizable fraction of proteins destined for ER are first synthesized in the cell cytosol and then transported across the ER membrane–a process called post-translational translocation. Similar to cotranslationally translocated proteins, these proteins also use the Sec translocon complex to enter the ER lumen.
Targeting proteins to the ER
Hsp40 and Hsp70 chaperone molecules bind the translated proteins in the cytosol to prevent their folding. The chaperone binding helps to keep the signal...
Targeting proteins to the ER
Hsp40 and Hsp70 chaperone molecules bind the translated proteins in the cytosol to prevent their folding. The chaperone binding helps to keep the signal...
5.5K
Export of Misfolded Proteins out of the ER
3.4K
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...
3.4K

