関連する実験動画
Updated: Mar 11, 2026

05:52
Reconstitution of Msp1 Extraction Activity with Fully Purified Components
Published on: August 10, 2021
3.0K
SNDタンパク質は,エンドプラズマの網膜への代替標的となる
Naama Aviram1, Tslil Ast1, Elizabeth A Costa2
1Department of Molecular Genetics, Weizmann Institute of Science, Rehovot 7610001, Israel.
Nature
|December 2, 2016
まとめ
3つのタンパク質であるSnd1,Snd2,Snd3を含む新しいバックアップ経路は,酵母体内膜のタンパク質を標的とするのに役立ちます. このSRPとGETから独立したシステムは,既知の経路の欠陥を補償する堅固なタンパク質リレーを保証します.
科学分野:
- 細胞生物学
- 分子生物学
- タンパク質の密輸
背景:
- ユカリオット細胞は,折りたたみと処理のために,内プラズマの網膜 (ER) にタンパク質を標的とする.
- タンパク質のターゲティングは,信号認識粒子 (SRP) またはテールアンカーされたタンパク質 (GET) の誘導入り経路を通じて発生します.
- いくつかのタンパク質は,SRPとGETとは独立して標的にされ,未定の経路を示唆する.
研究 の 目的:
- エンドプラズマ網膜 (ER) ターゲティングに関与する新しいタンパク質を特定する.
- ERへのタンパク質リレーの潜在的な新しい経路を特徴付ける.
- セルラー・ターゲティング装置の 頑丈さと柔軟性を理解するために
主な方法:
- 酵母菌Saccharomyces cerevisiaeの偏らない高濃度視覚検診
- 特徴のない標的タンパク質を特定するための系統的な遺伝子スクリーニング
- 既知のSRPとGET経路と並行して識別されたタンパク質の機能分析.
主要な成果:
- Snd1,Snd2,Snd3という特徴化されていない3つのタンパク質は,タンパク質ターゲティングに不可欠であると特定されました.
- これらのタンパク質はSRPとGET経路とは独立して機能する.
- Snd1,Snd2とSnd3は,SRPとGETの損失を補う平行経路を形成しています.
結論:
- エンドプラズマ網膜のタンパク質を標的にする新しいSRPとGET独立した経路が発見されました.
- Sndタンパク質はバックアップシステムとして機能し,堅固なタンパク質リレーを保証します.
- この発見は,真核タンパク質の標的装置の相互接続性と柔軟性を明らかにしています.
関連する概念動画
Directing Proteins to the Rough Endoplasmic Reticulum
18.2K
The organelle-specific signaling sequences direct proteins synthesized in the cytosol to their final destination like ER, mitochondria, peroxisomes, etc. Some of the proteins directed to ER are then trafficked via vesicles to other organelles within the cell or the extracellular environment through the Golgi complex. For example, the rough ER synthesizes soluble proteins for transportation to the lysosomes or secretion out of the cell. It can also synthesize transmembrane proteins that can...
18.2K
Post-translational Translocation of Proteins to the RER
8.0K
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...
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...
8.0K
Tail-anchoring of Proteins in the ER Membrane
4.0K
Tail-anchored, or TA, proteins are estimated to make up to 3-5% of membrane proteins found in the eukaryotic cell. Such proteins have a single transmembrane domain located approximately 30 amino acid residues upstream from the C-terminal end. As a result, the signal recognition particle (SRP) cannot guide a TA protein to the ER membrane for cotranslational insertion. Hence, they are integrated into the ER membrane post-translationally using their C-terminal end as the anchor. TA proteins...
4.0K
Cotranslational Protein Translocation
10.8K
Translocation of proteins across membranes is an ancient process that occurs even in bacteria and archaebacteria. In fact, the components of the translocation machinery are still conserved between prokaryotes and eukaryotes.
Sec61 channel partners for cotranslational translocation
During cotranslational translocation, the Sec61 channel partners with the signal recognition particle (SRP), the signal recognition particle receptor (SR), and the ribosomes to transport the nascent polypeptide chain...
Sec61 channel partners for cotranslational translocation
During cotranslational translocation, the Sec61 channel partners with the signal recognition particle (SRP), the signal recognition particle receptor (SR), and the ribosomes to transport the nascent polypeptide chain...
10.8K
Insertion of Single-pass Transmembrane Proteins in the RER
18.6K
Integral membrane proteins are proteins adhered to the lipid bilayer of a cell organelle or membrane. They can be of two types: transmembrane integral proteins that span the lipid bilayer and monotopic proteins that are attached to either side of the membrane but do not pass through it.
Integral transmembrane proteins possess transmembrane and extra membrane domains. The transmembrane domains are primarily made of 20-25 hydrophobic amino acids arranged in a helical secondary confirmation. These...
Integral transmembrane proteins possess transmembrane and extra membrane domains. The transmembrane domains are primarily made of 20-25 hydrophobic amino acids arranged in a helical secondary confirmation. These...
18.6K
GPI Anchoring of Proteins in the ER Membrane
5.7K
GPI-anchoring is a post-translational, reversible protein modification that is ubiquitous in eukaryotes. Such proteins are primarily present on the exoplasmic leaflet of the plasma membrane.
GPI-anchor structure
A sequence of 11 enzymatic reactions results in the synthesis of the complete GPI anchor consisting of a hydrophobic and a hydrophilic portion. The hydrophobic portion comprises phosphatidylinositol, while the hydrophilic part comprises polar groups like phosphoethanolamine,...
GPI-anchor structure
A sequence of 11 enzymatic reactions results in the synthesis of the complete GPI anchor consisting of a hydrophobic and a hydrophilic portion. The hydrophobic portion comprises phosphatidylinositol, while the hydrophilic part comprises polar groups like phosphoethanolamine,...
5.7K

