コアトーマーとディライシン・エンドプラズマ網膜保持モチーフの相互作用
1Basel Institute for Immunology, Switzerland.
まとめ
コアトーマー複合体は,膜タンパク質のER保持モチーフに結合し,酵母と哺乳類の内 плазма網膜 (ER) にこれらのタンパク質を回収する役割を示唆します.
科学分野:
- 細胞生物学 細胞生物学
- 分子生物学は分子生物学である.
- プロテインの密輸,人身売買
背景:
- エンドプラズマ網膜 (ER) 居住型I型トランスメブランタンパク質は,細胞プラズマ保持信号を有する.
- ER保持を制御する正確なメカニズムは,ほとんど不明のままです.
研究 の 目的:
- I型トランスメブランタンパク質のER保持の基礎となる分子メカニズムを調査する.
- ER保持モチーフと相互作用するタンパク質を特定する.
主な方法:
- イーストと哺乳類の細胞溶解物におけるER保持モチーフの分析.
- コイムノプレシピテーションは,タンパク質の相互作用を検出するための測定法です.
- サイト・ディレクテッド・ミュータジェネシス (Site-directed mutagenesis) により,ER保持とコアトーマー結合に対する突然変異の機能的影響を評価する.
主要な成果:
- ER保持モチーフは,細胞溶解体内のコアトーマー複合体と特異的に相互作用した.
- ER保持能力を破壊する突然変異は,コアトーマー結合も廃止した.
- この相互作用は,酵母と哺乳類のシステム間で保存された.
結論:
- コアトーマー複合体は,トランスメブランタンパク質をエンドプラズマ網膜に回収する上で重要な役割を果たします.
- ER保持モチーフとのコアトーマー相互作用は,ER内のタンパク質局所化を維持するための重要なメカニズムです.
関連する概念動画
Translocation of Proteins into the Mitochondria
Mitochondrial precursors are translocated to the internal subcompartments via independent mechanisms involving distinct protein machineries called translocases.
Sorting of outer membrane proteins:
Mitochondrial outer membrane proteins are of two types: the transmembrane, beta-barrel porins, and the membrane-anchored, alpha-helical proteins. Beta-barrel porin precursors are translocated by the TOM complex and inserted into the outer mitochondrial membrane by the SAM complex. In contrast,...
Sorting of outer membrane proteins:
Mitochondrial outer membrane proteins are of two types: the transmembrane, beta-barrel porins, and the membrane-anchored, alpha-helical proteins. Beta-barrel porin precursors are translocated by the TOM complex and inserted into the outer mitochondrial membrane by the SAM complex. In contrast,...
Coat Assembly and GTPases
Vesicles incorporate different coat protein subunits in different cell locations, which changes the properties of the coat, such as the shape and geometry of the transport vesicles. Thus, vesicle coat proteins also play a significant role in cargo selection.
Coat assembly depends on the local availability of phosphatidylinositol phosphates or PIPs and GTP-binding proteins. Adaptor proteins, which link the coat proteins to the membrane, bind to these PIPs and play a crucial role in controlling...
Coat assembly depends on the local availability of phosphatidylinositol phosphates or PIPs and GTP-binding proteins. Adaptor proteins, which link the coat proteins to the membrane, bind to these PIPs and play a crucial role in controlling...
Rab Proteins
Rab proteins constitute the largest family of monomeric GTPases, of which 70 members are present in humans. Rab proteins and their effectors regulate consecutive stages of vesicle transport such as vesicle transport, docking, and fusion to the correct recipient membrane.
Rab proteins switch between a cytosolic, GDP-bound inactive state and a membrane-anchored, GTP-bound active state. By themselves, Rabs show slow rates of GDP/GTP exchange and GTP hydrolysis. Thus, Rab proteins are considered...
Rab proteins switch between a cytosolic, GDP-bound inactive state and a membrane-anchored, GTP-bound active state. By themselves, Rabs show slow rates of GDP/GTP exchange and GTP hydrolysis. Thus, Rab proteins are considered...
ER Retrieval Pathway
In the secretory pathway, vesicles transport proteins from one cellular compartment to another in forward transport to deliver the protein to its correct location. Occasionally, misfolded proteins and incorrect proteins escape their original compartments, and a retrieval pathway is used to return the escaped proteins to their original compartment.
The ER uses many checkpoints to prevent the entry of incorrectly folded or a resident protein as cargo onto a transport vesicle. These mechanisms...
The ER uses many checkpoints to prevent the entry of incorrectly folded or a resident protein as cargo onto a transport vesicle. These mechanisms...
Directing Proteins to the Rough Endoplasmic Reticulum
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...
Tail-anchoring of Proteins in the ER Membrane
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...


