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関連する概念動画

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...
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...
Anaphase Promoting Complex00:50

Anaphase Promoting Complex

The stepwise destruction of specific proteins is necessary for the progression and completion of the cell cycle. Such proteins are ubiquitinated by ubiquitin ligases and then subsequently destroyed by the proteasome. The SCF (Skp1/Cullin/F-box) and the anaphase-promoting complex (APC) are two important ubiquitin ligases involved in cell cycle progression. While SCF is active throughout the cell cycle, APC gets activated during metaphase to anaphase transition. Cdc20 or Cdh1 binds to APC and...
Post-translational Translocation of Proteins to the RER01:27

Post-translational Translocation of Proteins to the RER

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...
Anaphase Promoting Complex00:50

Anaphase Promoting Complex

The stepwise destruction of specific proteins is necessary for the progression and completion of the cell cycle. Such proteins are ubiquitinated by ubiquitin ligases and then subsequently destroyed by the proteasome. The SCF (Skp1/Cullin/F-box) and the anaphase-promoting complex (APC) are two important ubiquitin ligases involved in cell cycle progression. While SCF is active throughout the cell cycle, APC gets activated during metaphase to anaphase transition. Cdc20 or Cdh1 binds to APC and...
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...

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関連する実験動画

Updated: May 20, 2026

In Vitro Analysis of E3 Ubiquitin Ligase Function
06:06

In Vitro Analysis of E3 Ubiquitin Ligase Function

Published on: May 14, 2021

連続的なE2sは,APCのターゲットに対するポリユビキチンチェーンアセンブリを駆動します.

Monica C Rodrigo-Brenni1, David O Morgan

  • 1Department of Physiology, University of California, San Francisco, CA 94158, USA.

Cell
|July 17, 2007
PubMed
まとめ

アナフェーズ促進複合体 (APC) は,ユビキチン鎖の組み立てのために,連続的なE2酵素,Ubc4とUbc1を使用します. このメカニズムは,細胞サイクル進行と標的タンパク質のタンパク質破壊に不可欠です.

科学分野:

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

背景:

  • アナフェーズ促進複合体 (APC/C) は,重要なE3ユビキチンリガゼであり,分解のための重要なタンパク質をターゲットにすることで,細胞サイクル進行を調節します.
  • APC/Cおよび他のE3リガゼが,ポリユビキチン連鎖組成のための明確なユビキチネーション反応を触媒化する正確なメカニズムは,まだ完全に理解されていません.

研究 の 目的:

  • APC/C媒介型ポリユビキチン鎖形成における異なるE2ユビキチン結合酵素の役割を解明する.
  • APC/Cと連携する特定のE2酵素を特定し,それらの独特の酵素活性性を特徴づける.

主な方法:

  • APC/C共酵素としてのすべての芽生える酵母E2酵素のインビトロスクリーニング.
  • APC/C-E2相互作用と酵素活性に関する分析.
  • 特定のE2酵素に欠けている酵母菌株の機能評価.

主要な成果:

  • 芽生えた酵母 APC/C.の重要なE2パートナーとしてUbc4とUbc1を特定しました.
  • Ubc4がAPC/C標的の急速なモノウビキチン化を触媒し,Ubc1がK48結合ポリウビキチン鎖の拡張を媒介することを示した.
  • Ubc1とUbc4の両方が欠けている酵母におけるミトティックAPC/C機能の喪失が観察されました.

さらに関連する動画

Evaluation of Substrate Ubiquitylation by E3 Ubiquitin-ligase in Mammalian Cell Lysates
09:47

Evaluation of Substrate Ubiquitylation by E3 Ubiquitin-ligase in Mammalian Cell Lysates

Published on: May 10, 2022

In-vitro Reconstitution of Bacterial Ubiquitination and VCP/p97-mediated Elimination
07:58

In-vitro Reconstitution of Bacterial Ubiquitination and VCP/p97-mediated Elimination

Published on: January 2, 2026

関連する実験動画

Last Updated: May 20, 2026

In Vitro Analysis of E3 Ubiquitin Ligase Function
06:06

In Vitro Analysis of E3 Ubiquitin Ligase Function

Published on: May 14, 2021

Evaluation of Substrate Ubiquitylation by E3 Ubiquitin-ligase in Mammalian Cell Lysates
09:47

Evaluation of Substrate Ubiquitylation by E3 Ubiquitin-ligase in Mammalian Cell Lysates

Published on: May 10, 2022

In-vitro Reconstitution of Bacterial Ubiquitination and VCP/p97-mediated Elimination
07:58

In-vitro Reconstitution of Bacterial Ubiquitination and VCP/p97-mediated Elimination

Published on: January 2, 2026

  • Ubc1の同型であるヒトのE2-25Kも,APC/C依存鎖の拡張を促進することを示した.

    • 結論:

    • 異なるE2酵素 (Ubc4とUbc1) の連続的な作用が,APC/C標的のK48結合型ポリユビキチネーションを誘発するモデルを提案した.
    • この連続的なE2メカニズムは,APC/C基板の適時なタンパク質分解を促進し,適切な細胞サイクル進行を保証します.