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関連する概念動画

Regulated Protein Degradation02:58

Regulated Protein Degradation

7.4K
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...
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The Proteasome02:18

The Proteasome

8.8K
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...
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Proteins: From Genes to Degradation02:11

Proteins: From Genes to Degradation

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Within a biological system, the DNA encodes the RNA, and the nucleotide sequence in the RNA further defines the amino acid sequence in the protein. This is referred to as “The Central Dogma of Molecular Biology” - a term coined by Francis Crick.  Central dogma is a firm principle in biology that defines the flow of genetic information within any life form. The two fundamental steps in central dogma are - transcription and translation.
Transcription is the synthesis of RNA...
12.3K
mRNA Stability and Gene Expression02:51

mRNA Stability and Gene Expression

5.6K
The structure and stability of mRNA molecules regulates gene expression, as mRNAs are a key step in the pathway from gene to protein. In eukaryotes, the half-life of mRNA varies from a few minutes up to several days. mRNA stability is essential in growth and development. The absence of the proteins regulating its stability, such as tristetraprolin in mice, can cause systemic issues, including bone marrow overgrowth, inflammation, and autoimmunity.
Cis-acting Elements involved in mRNA stability
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Export of Misfolded Proteins out of the ER01:32

Export of Misfolded Proteins out of the ER

3.7K
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...
3.7K
The Proteasome Structure01:17

The Proteasome Structure

802
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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Updated: Jul 18, 2025

Cycloheximide Chase Analysis of Protein Degradation in Saccharomyces cerevisiae
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Cycloheximide Chase Analysis of Protein Degradation in Saccharomyces cerevisiae

Published on: April 18, 2016

29.1K

分解のためにタンパク質を捕まえる

Charlotte M Schilling1, Eilika Weber-Ban1

  • 1Institute of Molecular Biology and Biophysics, ETH Zurich, Zurich, Switzerland.

Science (New York, N.Y.)
|August 24, 2023
PubMed
まとめ
この要約は機械生成です。

新しいユビキチン独立経路は,核タンパク質を分解のためにプロテアソームに導きます. この発見は 細胞核における タンパク質の転用のための 新しいメカニズムを明らかにした.

さらに関連する動画

Assays for the Degradation of Misfolded Proteins in Cells
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Assays for the Degradation of Misfolded Proteins in Cells

Published on: August 28, 2016

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Growth-based Determination and Biochemical Confirmation of Genetic Requirements for Protein Degradation in Saccharomyces cerevisiae
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Growth-based Determination and Biochemical Confirmation of Genetic Requirements for Protein Degradation in Saccharomyces cerevisiae

Published on: February 16, 2015

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関連する実験動画

Last Updated: Jul 18, 2025

Cycloheximide Chase Analysis of Protein Degradation in Saccharomyces cerevisiae
09:05

Cycloheximide Chase Analysis of Protein Degradation in Saccharomyces cerevisiae

Published on: April 18, 2016

29.1K
Assays for the Degradation of Misfolded Proteins in Cells
10:56

Assays for the Degradation of Misfolded Proteins in Cells

Published on: August 28, 2016

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Growth-based Determination and Biochemical Confirmation of Genetic Requirements for Protein Degradation in Saccharomyces cerevisiae
10:57

Growth-based Determination and Biochemical Confirmation of Genetic Requirements for Protein Degradation in Saccharomyces cerevisiae

Published on: February 16, 2015

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科学分野:

  • 細胞生物学
  • 分子生物学
  • 生物化学

背景:

  • プロテアソームは タンパク質の分解を 司る重要な細胞機構です
  • タンパク質の分解は通常,ユビキチン-プロテアソーム系によって媒介される.
  • 核タンパク質をプロテアソームに標的にするメカニズムは完全に理解されていません.

研究 の 目的:

  • 核タンパク質をプロテアソームに標的にする 新しい経路を調査する
  • 核タンパク質のターンオーバーにおけるユビキチン独立メカニズムの役割を明らかにする.

主な方法:

  • 酵母モデルを使って 遺伝子スクリーニングを行いました
  • タンパク質の相互作用を分析するために生化学的測定法を使用した.
  • タンパク質の位置を調べるために 顕微鏡で調べました

主要な成果:

  • 特定の核タンパク質を標的とした新しい経路を特定した.
  • この経路はユビキチン結合とは独立して機能することを示した.
  • この新しいターゲティングメカニズムに関与する主要なタンパク質成分を特徴付けました.

結論:

  • 核タンパク質の分解には,ユビキチンから独立した経路が存在する.
  • この経路は細胞タンパク質の ホメオスタシスの理解に 重要な貢献をします
  • この経路に関するさらなる研究により 新しい治療目標が明らかになるかもしれません