関連する実験動画
Updated: Jul 11, 2026

06:45
Transmembrane Domain Oligomerization Propensity determined by ToxR Assay
Published on: May 26, 2011
まとめ
膀性口炎ウイルスにおけるトランスメブランドメインの大きさは,その適切な細胞表面輸送のために,グリコプロテイン (G) が不可欠である. このドメインの縮小は,膜の固定と細胞内の正常なタンパク質の輸送に影響します.
科学分野:
- ウイルス学 ウイルス学 ウイルス学
- 分子生物学は分子生物学である.
- 細胞生物学 細胞生物学
背景:
- 膀性口腔炎ウイルスのグリコプロテイン (G) は,ウイルスの侵入に不可欠です.
- その膜を横断するドメインは,タンパク質を細胞膜内に固定します.
研究 の 目的:
- Gタンパク質機能におけるトランスメブランドメインの大きさの役割を調査する.
- 超膜領域の変化がGタンパク質の輸送と細胞表面の局所化にどのように影響するかを決定する.
主な方法:
- オリゴヌクレオチド誘導変異は,短縮されたトランスメブラン領域を持つGタンパク質を作成するために使用されました.
- これらの変異Gタンパク質の細胞内の発現は,それらの構成と輸送を評価するために分析されました.
主要な成果:
- 18,16,または14のトランスメブランアミノ酸を持つGタンパク質は,細胞表面に正しく固定され,輸送されました.
- 12または8つの膜外アミノ酸を備えたGタンパク質は細胞内膜を横断しているが,ゴルジのような領域でブロックされている.
- 超膜ドメインが欠けているGタンパク質が,エンドプラズマ網膜に蓄積され,ゆっくり分泌された.
結論:
- 超膜領域の長さは,Gタンパク質膜のアンカリングに極めて重要です.
- 膜外ドメインの大きさは,Gタンパク質の細胞表面への正常な輸送に直接影響を及ぼします.
関連する概念動画
Lipids as Anchors
In the plasma membrane, the lipids forming the bilayer can also act as an anchor to tether proteins to the membrane. The three main types of lipid anchors found in eukaryotes are – prenyl groups, fatty acyl groups, and glycosylphosphatidylinositol or GPI groups. Prenyl and fatty acyl groups act as anchors on the cytosolic surface of the membrane, whereas GPI anchors proteins on the extracellular side.
The carboxy-terminal of most of the prenylated proteins, such as Ras proteins, contains the...
The carboxy-terminal of most of the prenylated proteins, such as Ras proteins, contains the...
Single-pass Transmembrane Proteins
Integral membrane proteins are tightly associated with the cell membrane and play a crucial role in cell communication, signaling, adhesion, and transport of the molecules. Some integral membrane proteins are present only in the membrane monolayer. For example, the enzyme fatty acid amide hydrolase is present in the cytoplasmic side of the membrane monolayer. In contrast, another type of integral membrane protein, also known as a transmembrane protein, spans across the membrane. Transmembrane...
Membrane Domains
The membrane domains concentrate specific lipids and proteins at one place within the membrane, which helps in cell signaling, adhesion, and other critical cellular processes. These domains can differ in size, composition, function, and lifespan.
Protein Domains
The membrane comprises a group of distinct proteins responsible for carrying out a cell's specific function. For example, the plasma membrane of the human sperm, or a single germ cell, contains a unique set of proteins in the anterior...
Protein Domains
The membrane comprises a group of distinct proteins responsible for carrying out a cell's specific function. For example, the plasma membrane of the human sperm, or a single germ cell, contains a unique set of proteins in the anterior...
GPI Anchoring of Proteins in the ER Membrane
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,...
Multi-pass Transmembrane Proteins and β-barrels
In multi-pass transmembrane proteins, the polypeptide chain crosses the membrane more than once. The transmembrane polypeptide chain either forms an α-helix or β-strand structure. α-Helix containing multi-pass transmembrane proteins are ubiquitous, whereas β-strand containing ones are mainly found in gram-negative bacteria, mitochondria, and chloroplasts.
α-Helix containing multi-pass transmembrane proteins
Multi-pass transmembrane proteins such as G-protein-linked receptors (GPCRs) and...
α-Helix containing multi-pass transmembrane proteins
Multi-pass transmembrane proteins such as G-protein-linked receptors (GPCRs) and...
Mechanisms of Membrane Domain Formation
Different physical properties of lipids and proteins allow them to localize and form distinct islands or domains in the membrane. Some membrane domains are formed due to protein-protein interactions, whereas others are formed due to the presence of specific lipids such as sphingolipids and sterols—for example, large proteins, such as bacteriorhodopsin, aggregate and create distinct domains.
Another mechanism for membrane domain formation involves membrane proteins interacting with cytoskeletal...
Another mechanism for membrane domain formation involves membrane proteins interacting with cytoskeletal...

