関連する実験動画
Updated: May 19, 2026

11:31
Image-Based Methods to Study Membrane Trafficking Events in Stomatal Lineage Cells
Published on: May 12, 2023
エチレンガスに対するER-テッダー付きEIN2制御応答の処理とサブセルラー取引
Hong Qiao1, Zhouxin Shen, Shao-shan Carol Huang
1Plant Biology Laboratory, Salk Institute for Biological Studies, La Jolla, CA 92037, USA.
まとめ
植物におけるエチレンシグナリングは,ETHYLENE INSENSITIVE2 (EIN2) に依存しています. エチレンはEIN2分裂と核転移を誘発し,植物反応を活性化します.
科学分野:
- 植物生物学 植物生物学
- 分子生物学は分子生物学である.
- バイオケミストリー バイオケミストリー
背景:
- エチレンガスは,発達とストレス反応を調節する重要な植物ホルモンです.
- EIN2 (ETHYLENE INSENSITIVE2) は,エチレンシグナル伝達における重要な統合膜タンパク質ですが,その正確な機能は不明です.
研究 の 目的:
- エチレン信号伝達においてEIN2が機能する分子メカニズムを解明する.
- EIN2.2の翻訳後の改変と細胞下局所化の役割を調査する.
主な方法:
- EIN2のリン酸化とタンパク質分解処理の分析.
- 遺伝子変異と生化学的測定を用いて,EIN2断片のERから核への転移を追跡する.
- 構成三重反応1 (CTR1) キナーゼ活性における役割を調査する.
主要な成果:
- EIN2のリン酸化調節によるタンパク質分解分裂は,その輸送をエンドプラズマ網膜 (ER) から核へと開始する.
- エチレンシグナリングは,EIN2の脱リン酸化と特定の割れ目を伴い,EIN2-C'断片の核インポートにつながります.
- 構成要素のEIN2-C'核の局所化とEIN3/EIN3-LIKE1の活性化は,デフォスフォリレーションやCTR1の無活性化を模倣する変異で起こる.
結論:
- エチレンシグナリングは,EIN2-C'ペプチドの制御された分裂と核転位によって媒介されます.
- このメカニズムは,ER局所化ホルモン知覚を核転写調節と結びつけ,植物反応を制御する.
- EIN2処理は,エチレン信号伝導経路における重要なチェックポイントです.
関連する概念動画
The Unfolded Protein Response
The ER is the hub of protein synthesis in a cell. It has robust systems to quality control protein folding and also for degradation of terminally misfolded proteins. Under normal conditions, a small proportion of misfolded proteins that cannot be salvaged need to be transported to the cytoplasm by the ER-associated degradation or ERAD pathways. However, if the ERAD cannot handle the misfolded proteins, the cell activates the unfolded protein response or UPR to adjust the protein folding...
Regulation of the Unfolded Protein Response
Inositol-requiring kinase one or IRE1 is the most conserved eukaryotic unfolded protein response (UPR) receptor. It is a type I transmembrane protein kinase receptor with a distinctive site-specific RNase activity. As the binding mechanics of the misfolded proteins with the N-terminal domain of IRE-1 are unclear, three binding models — direct, indirect, and allosteric -- are proposed for receptor activation. Nevertheless, it is known that once a misfolded protein associates with IRE1, it...
Protein Translocation Machinery on the ER Membrane
The translocon complex situated on the ER membrane is the main gateway for the protein secretory pathway. It facilitates the transport of nascent peptides into the ER lumen and their insertion into the ER membrane.
Sec61 protein conducting channel
In eukaryotes, the translocon complex comprises a core heterotrimeric translocator channel called the Sec61 complex. This channel includes three transmembrane proteins, Sec61α, Sec61β, and Sec61γ, and is the largest subunit of the translocon complex.
Sec61 protein conducting channel
In eukaryotes, the translocon complex comprises a core heterotrimeric translocator channel called the Sec61 complex. This channel includes three transmembrane proteins, Sec61α, Sec61β, and Sec61γ, and is the largest subunit of the translocon complex.
Cell Signaling in Plants
Plant cells communicate to coordinate their cycle of growth, flowering and fruiting, and activities in roots, shoots, and leaves in response to the changing environmental conditions. Plant signaling is distinct from animal signaling. Plants primarily utilize enzyme-linked receptors, whereas the largest class of cell-surface receptors in animals are G-protein coupled receptors (GPCRs). Unlike animals, receptor tyrosine kinases are rare in plants. Instead, plants have a diverse class of...
Export of Misfolded Proteins out of the ER
After folding, the ER assesses the quality of secretory and membrane proteins. The correctly folded proteins are cleared by the calnexin cycle for transport to their final destination, while misfolded proteins are held back in the ER lumen. The ER chaperones attempt to unfold and refold the misfolded proteins but sometimes fail to achieve the correct native conformation. Such terminally misfolded proteins are then exported to the cytosol by ER-associated degradation or ERAD pathway for...
The Endoplasmic Reticulum
The endoplasmic reticulum or ER makes up for more than half of the membranes in a cell and accounts for 10% of total cell volume. It is also the primary protein and lipid synthesis factory for most cell organelles, such as the Golgi apparatus, lysosomes, secretory vesicles, and the plasma membrane. Despite being the most extensive and functionally complex subcellular organelle, ER was the last to be discovered. After years of deliberation, Keith Porter and George Palade in the year 1954,...

