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Regulated Protein Degradation02:58

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...
Regulated Protein Degradation02:58

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...
The Proteasome01:13

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...
The Proteasome02:18

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...
The Proteasome02:18

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...
The Proteasome Structure01:17

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...

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In Vitro Ubiquitination and Deubiquitination Assays of Nucleosomal Histones
11:36

In Vitro Ubiquitination and Deubiquitination Assays of Nucleosomal Histones

Published on: July 25, 2019

ウビキチン:同じ分子,異なる分解経路

Michael J Clague1, Sylvie Urbé

  • 1Institute of Translational Medicine, University of Liverpool, UK. clague@liv.ac.uk

Cell
|November 30, 2010
PubMed
まとめ
この要約は機械生成です。

ウビキチンタギングは,タンパク質をターゲットにして,プロテアソーム,リゾソーム,またはオートファゴソームを通じて分解します. 鎖の長さと結合は,特定の分解経路を決定し,相互作用とデウビキチン酵素の活性に影響を与えます.

さらに関連する動画

Ubiquitin Chain Analysis by Parallel Reaction Monitoring
08:33

Ubiquitin Chain Analysis by Parallel Reaction Monitoring

Published on: June 17, 2020

Measuring Enzymatic Activity of Neurodevelopmental Disorder-Associated Deubiquitylating Enzymes via an In Vitro Ubiquitin Chain Cleavage Assay
07:05

Measuring Enzymatic Activity of Neurodevelopmental Disorder-Associated Deubiquitylating Enzymes via an In Vitro Ubiquitin Chain Cleavage Assay

Published on: September 27, 2024

関連する実験動画

Last Updated: Jun 6, 2026

In Vitro Ubiquitination and Deubiquitination Assays of Nucleosomal Histones
11:36

In Vitro Ubiquitination and Deubiquitination Assays of Nucleosomal Histones

Published on: July 25, 2019

Ubiquitin Chain Analysis by Parallel Reaction Monitoring
08:33

Ubiquitin Chain Analysis by Parallel Reaction Monitoring

Published on: June 17, 2020

Measuring Enzymatic Activity of Neurodevelopmental Disorder-Associated Deubiquitylating Enzymes via an In Vitro Ubiquitin Chain Cleavage Assay
07:05

Measuring Enzymatic Activity of Neurodevelopmental Disorder-Associated Deubiquitylating Enzymes via an In Vitro Ubiquitin Chain Cleavage Assay

Published on: September 27, 2024

科学分野:

  • 細胞生物学 細胞生物学
  • バイオケミストリー バイオケミストリー
  • 分子生物学は分子生物学である.

背景:

  • ウビキチン (Ub) は,重要な翻訳後の修正である.
  • ウビキチン結合は,分解のための基板をターゲットにします.
  • 哺乳類の細胞は,タンパク質分解の3つの主要な経路を活用しています:プロテアソーム,リゾソーム,オートファゴソームです.

研究 の 目的:

  • 異なる分解経路を対象とした基板におけるウビキチンの役割を調査する.
  • ユビキチン鎖の特徴が経路選択にどのように影響するかを探求する.

主な方法:

  • ユビキチン鎖の長さと結合型の分析.
  • 経路特異の受容体との基板相互作用の評価.
  • デウビキチナゼ (DUB) 酵素に対する感受性を評価する.

主要な成果:

  • ウビキチンは,3つの主要な分解経路の共通の信号として機能します.
  • 長さや結合を含むウビキチン鎖の性質は,基質の運命を決定する.
  • これらの性質は,特定の受容体やDUBとの相互作用を調節する.

結論:

  • ウビキチン鎖の特徴は,タンパク質分解経路の選択の決定的な決定因子である.
  • 異なるユビキチネーションパターンは,プロテアソーム,リソソーム,オートファゴソームの基板特異性を保証する.
  • これらのメカニズムを理解することは,細胞タンパク質のホメオスタシスを理解するために不可欠です.