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関連する概念動画

Covalently Linked Protein Regulators02:04

Covalently Linked Protein Regulators

9.9K
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....
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Protein Complexes with Interchangeable Parts01:57

Protein Complexes with Interchangeable Parts

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Groups of proteins may form a complex where each protein in this complex has a different role in the overall execution of the complex’s function. Often some of the proteins in the complex can be replaced by a closely related variant to give a complex that contains many of the same components yet is functionally distinct.
The SCF ubiquitin ligase is a protein complex of five individual proteins. This complex attaches ubiquitin to other target proteins to mark them for degradation. In order...
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The Proteasome02:18

The Proteasome

10.7K
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...
10.7K
Regulated Protein Degradation02:58

Regulated Protein Degradation

9.3K
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...
9.3K
Export of Misfolded Proteins out of the ER01:32

Export of Misfolded Proteins out of the ER

5.7K
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...
5.7K
The Proteasome01:13

The Proteasome

2.0K
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...
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Method for Measuring the Activity of Deubiquitinating Enzymes in Cell Lines and Tissue Samples
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Method for Measuring the Activity of Deubiquitinating Enzymes in Cell Lines and Tissue Samples

Published on: May 10, 2015

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人間のデウビキチン化酵素相互作用の景観を定義する.

Mathew E Sowa1, Eric J Bennett, Steven P Gygi

  • 1Department of Pathology, Harvard Medical School, Boston, MA 02115, USA.

Cell
|July 21, 2009
PubMed
まとめ

研究者は,デウビキチン化酵素 (Dubs) のタンパク質相互作用をマッピングし,重要な細胞プロセスにおけるそれらの役割を明らかにしました. この研究は,Dubインタラクトームの基礎的な理解と,ユビキチン-プロテアゾーム経路への関与を提供します.

科学分野:

  • 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.
  • プロテオミクス プロテオミクスは,プロテオミクスの

背景:

  • 脱ユビキチン化酵素 (Dubs) は,ユビキチンを取り除き,タンパク質の活性と豊富さを調節する.
  • ほとんどのDubsの機能,目標,規制は,ほとんど特徴づけられていないままです.
  • Dubsを理解することは,ユビキチン-プロテアゾーム経路の解読に不可欠です.

研究 の 目的:

  • グローバル・プロテオミック・アナリストを通じて,Dubsの機能を体系的に調査する.
  • Dubs.に関連するタンパク質複合体を特定するために.
  • ダブの相互作用の地図を作成し,研究されていないダブを生物学的経路に配置します.

主な方法:

  • 公平な相互作用の信頼度測定のためのCompPASSソフトウェアプラットフォームの開発.
  • パラレルな非互換性プロテオミックデータ分析.
  • ゲン・オントロジー,インタラクトーム・トポロジー,サブセルラー・ローカライゼーション,機能研究を統合する.

主要な成果:

  • 75のDubs.に関連した774の候補相互作用タンパク質の識別.
  • リンクダブは,タンパク質のターンオーバー,転写,RNAの処理,DNAの損傷,およびERに関連した分解を含む多様な細胞プロセスにリンクしています.

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Measuring Enzymatic Activity of Neurodevelopmental Disorder-Associated Deubiquitylating Enzymes via an In Vitro Ubiquitin Chain Cleavage Assay
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Method for Measuring the Activity of Deubiquitinating Enzymes in Cell Lines and Tissue Samples

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

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  • Dubインタラクトーム内の新しい相互作用とタンパク質複合体の発見.

    • 結論:

    • この研究は,Dubのインタラクション・ランドスケープの最初の包括的な見方を提供しています.
    • 特徴づけられていないDubsは,推定される生物学的経路内に配置されます.
    • Ubiquitin-proteasome経路におけるDubsの役割に関する新しい洞察が確立されています.