信号媒介によるグリコシルトランスフェラーゼのダイナミックリテンションは,ゴルギの Golgi に存在します
Linna Tu1, William C S Tai, Lu Chen
1Department of Biology, Hong Kong University of Science and Technology, Clear Water Bay, Kowloon, Hong Kong, Special Administrative Region (SAR) of the People's Republic of China.
まとめ
Vps74pはゴルギ・グリコシルトランスフェラーゼとCOPIに結合し,ゴルギ装置内の酵素の局所化を促進する. このタンパク質は,膀輸送経由で酵素の位置づけを維持するための重要なリンクとして機能します.
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.
- タンパク質の密輸 タンパク質の密輸
背景:
- ゴルギ系レジデントのグリコシルトランスフェラーゼは,グリコタンパク質の改変に不可欠な酵素である.
- これらの酵素は,局所化に不可欠なサイトプラズマ尾を持つII型統合膜タンパク質です.
- コートタンパク質複合体I (COPI) 膀経由の逆行輸送はゴルギの局所化に関与しているが,直接結合モチーフは不明であった.
研究 の 目的:
- ゴルギ・レジデントのグリコシルトランスフェラーゼがゴルギ内部に局所するメカニズムを調査する.
- グリコシルトランスフェラーゼとCOPI輸送機構の相互作用を媒介する潜在的な結合パートナーを特定する.
主な方法:
- 酵母遺伝学とタンパク質生化学のテクニックが採用されました.
- Vps74p,グリコシルトランスファーゼ,COPIとの結合を評価するために相互作用研究が行われました.
主要な成果:
- Vps74pは,ほとんどの酵母ゴルギ局所化されたグリコシルトランスフェラーゼの細胞質尾の結合パートナーとして特定されました.
- また,Vps74pは,逆行移動に関与するコート複合体であるCOPIにも結合する.
- 酵素尾の保存されたペンタメリクモチーフはVps74p結合を媒介する.
結論:
- Vps74pはアダプタータンパク質として作用し,ゴルギ・グリコシルトランスファーゼをCOPI輸送システムと結びつけます.
- この相互作用は,これらの酵素がゴルギ内での動的,安定状態の局所化に不可欠です.
- Vps74pは,適切な取引のために,COPIでコーティングされた膀にグリコシルトランスファーゼの組み込みを促進します.
関連する概念動画
Oligosaccharide Assembly
Protein glycosylation starts in the ER lumen and continues in the Golgi apparatus. Glycosyltransferases catalyze the addition of sugar molecules or glycosylation of proteins. Usually, these enzymes add sugars to the hydroxyl groups of selected serine or threonine residues to form O-linked glycans or the amino groups of asparagine residues to form N-linked glycans. Different positions on the same polypeptide chain can contain differently linked glycans.
Multiple sugar molecules that may or may...
Multiple sugar molecules that may or may...
Golgi Matrix Proteins
Golgi matrix proteins are a group of highly dynamic proteins that maintain the stacked structure of Golgi. These proteins adapt to rapid morphological changes of the Golgi during the cell cycle. During cell division, mild proteolysis removes these connections resulting in Golgi unstacking. In The daughter cells, these proteins help reassemble the unstacked Golgi.
One of the first identified Golgi matrix proteins was GM130, a rod-like protein located in the cis-Golgi. Subsequently, many Golgi...
One of the first identified Golgi matrix proteins was GM130, a rod-like protein located in the cis-Golgi. Subsequently, many Golgi...
Protein Glycosylation
Glycosylation, the most common post-translational modification for proteins, serves diverse functions. Adding sugars to proteins makes the proteins more resistant to proteolytic digestion. Glycosylated proteins can act as markers and receptors to promote cell-cell adhesion. Additionally, they have many essential quality control functions in the cell, such as correct protein folding and facilitating transport of misfolded proteins to the cytosol, which can be degraded.
Glycosylation occurs in...
Glycosylation occurs in...
Transport Across the Golgi
While it is unclear how molecules move between adjacent Golgi cisternae, it is apparent that the molecules move from cis- cisterna, the entry face, to the trans- cisterna, the exit face. Experiments initially suggested vesicles that bud from one cisterna and fuse with the next cisterna to transport proteins between the cisternae. This vesicular transport model describes the Golgi apparatus as a relatively static structure with a unique enzyme composition in each cisterna. Molecules are...
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,...
Golgi Apparatus
As they leave the Endoplasmic Reticulum (ER), properly folded and assembled proteins are selectively packaged into vesicles. These vesicles are transported by microtubule-based motor proteins and fuse together to form vesicular tubular clusters, subsequently arriving at the Golgi apparatus, a eukaryotic endomembrane organelle that often has a distinctive ribbon-like appearance.The Golgi apparatus is a major sorting and dispatch station for the products of the ER. Newly arriving vesicles enter...

