関連する実験動画
Updated: Feb 22, 2026

10:56
Assays for the Degradation of Misfolded Proteins in Cells
Published on: August 28, 2016
12.6K
Slp1-Emp65: 折りたたみポリペプチドを乱暴な劣化から保護する保護因子
Shan Zhang1, Chengchao Xu1, Katherine E Larrimore2
1Temasek Life Sciences Laboratory, National University of Singapore, Singapore 117604, Singapore; Department of Biological Sciences, National University of Singapore, Singapore 117604, Singapore.
Cell
|September 19, 2017
まとめ
新しく発見されたタンパク質複合体Slp1-Emp65は,エンドプラズマ網膜の"守護者"として働き,折りたたみ中の新合成タンパク質の分解を防ぐ. 細胞の重要なタンパク質を 早期に分解しないようにします
科学分野:
- 細胞生物学
- 分子生物学
- プロテオスタシス
背景:
- 新しく合成されたタンパク質は 適切な折りたたみのために 分子チャペロンに依存しています
- 細胞の品質管理システムは 誤った折りたたみのタンパク質を 破壊対象にします
- チャペロンは逆説的に分解のために展開されたタンパク質を標的とし,新生ポリペプチドにリスクをもたらす.
研究 の 目的:
- 積極的に折りたたむポリペプチドの分解を防ぐメカニズムを特定する.
- エンドプラズマ網膜における Slp1-Emp65複合体の機能を特徴づける.
主な方法:
- タンパク質の折りたたみと分解における Slp1-Emp65複合体の役割を調査した.
- Slp1-Emp65複合体の欠如が新合成タンパク質に与える影響を評価した.
主要な成果:
- 展開されたタンパク質に結合する保存された内プラズマ網膜 (ER) 膜タンパク質複合体 (Slp1-Emp65) を特定した.
- Slp1-Emp65複合体は,折りたたむ過程で溶解性タンパク質を分解から保護することを実証した.
- Slp1-Emp65複合体がない場合,折りたたみ可能なタンパク質の20%から30%が分解される.
結論:
- Slp1-Emp65複合体は,新たに合成され,活発に折りたたむタンパク質の重要な保護者として機能する.
- "保護者"タンパク質と呼ばれる 新種のプロテオスタシス因子を発見した.
- 新生ポリペプチドの脆弱性と,専用の保護メカニズムの重要性を強調した.
関連する概念動画
Protein Folding
11.8K
Proteins are chains of amino acids linked together by peptide bonds. Upon synthesis, a protein folds into a three-dimensional conformation, critical to its biological function. Interactions between its constituent amino acids guide protein folding, and hence the protein structure is primarily dependent on its amino acid sequence.
Protein Structure Is Critical to Its Biological Function
Proteins perform a wide range of biological functions such as catalyzing chemical reactions, providing...
Protein Structure Is Critical to Its Biological Function
Proteins perform a wide range of biological functions such as catalyzing chemical reactions, providing...
11.8K
Protein Folding
128.7K
Overview
128.7K
Molecular Chaperones and Protein Folding
20.0K
The native conformation of a protein is formed by interactions between the side chains of its constituent amino acids. When the amino acids cannot form these interactions, the protein cannot fold by itself and needs chaperones. Notably, chaperones do not relay any additional information required for the folding of polypeptides; the native conformation of a protein is determined solely by its amino acid sequence. Chaperones catalyze protein folding without being a part of the folded protein.
The...
The...
20.0K
Molecular Chaperones and Protein Folding
15.2K
15.2K
Protein Folding Quality Check in the RER
5.3K
ER is the primary site for the maturation and folding of soluble and transmembrane secretory proteins. The calnexin cycle is a specific chaperone system that folds and assesses the confirmation of N-glycosylated proteins before they can exit the ER lumen. The primary players of this quality check pipeline are the lectins, ER-resident chaperones, and a glucosyl transferase enzyme. In case the calnexin system in the lumen fails to salvage a misfolded protein, it is transported to the cytoplasm...
5.3K
Bacterial Protein Maturation
608
Bacterial protein maturation is a tightly regulated process that ensures newly synthesized polypeptides achieve correct functional conformations. This maturation involves a series of modifications, folding events, and quality control steps, often assisted by specialized chaperone proteins.N-Terminal ModificationsThe maturation of bacterial polypeptides begins cotranslationally as the polypeptide exits the ribosome. The first amino acid, N-formylmethionine (fMet), is typically modified at the...
608

