関連する実験動画

Updated: Jul 5, 2026

In Situ Monitoring of Transiently Formed Molecular Chaperone Assemblies in Bacteria, Yeast, and Human Cells
08:58

In Situ Monitoring of Transiently Formed Molecular Chaperone Assemblies in Bacteria, Yeast, and Human Cells

Published on: September 2, 2019

DegPの制御されたプロテアゼとシャペロン機能の構造的基礎

Tobias Krojer1, Justyna Sawa, Eva Schäfer

  • 1Research Institute for Molecular Pathology - IMP, Dr Bohrgasse 7, A-1030 Vienna, Austria.

Nature
|May 23, 2008
PubMed
まとめ

細菌の熱ショックタンパク質DegPは品質管理因子として作用し,誤った折りたたまれたタンパク質を排除し,外膜タンパク質の生体生成を支援します. 誤った折りたたまれたタンパク質は,DegPを誘発し,より大きな活性複合体を形成し,その複合体は基質を包装または分解する.

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Export of Misfolded Proteins out of the ER

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Regulated Protein Degradation02:58

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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.
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GTPases and their Regulation02:14

GTPases and their Regulation

Guanine nucleotide-binding proteins (G-proteins), also known as GTPases, are a superfamily of proteins that regulate many cellular processes, such as cell signaling, vesicular transport, and the regulation of cell shape and motility. Mutation or dysfunction of these proteins can lead to disease. There are around 40,000 known G-proteins that can broadly be classified into two groups ‒  small G-proteins consisting of a single domain and large multi-domain G-proteins.
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