関連する実験動画
Updated: Jan 2, 2026

10:34
A High-content Assay for Monitoring AMPA Receptor Trafficking
Published on: January 28, 2019
8.0K
AMPA受容体の構造は,その補助サブユニットであるコーンチーンと複合している
1Department of Molecular Physiology and Biophysics, Center for Structural Biology, and Vanderbilt Brain Institute, Vanderbilt University School of Medicine, Nashville, TN 37232, USA.
まとめ
構造は,コニホログ (CNIH) がAMPA型グルタミン酸受容体 (AMPAR) とどのように相互作用するかを明らかにする. CNIH3に関する分子学的洞察が得られます.
科学分野:
- 神経科学
- 分子生物学
- 構造生物学
背景:
- AMPA型グルタミン酸受容体 (AMPARs) は脳内の迅速な興奮神経伝達に不可欠です.
- AMPARは補助サブユニットと複合して機能し,シナプス可塑性,学習,記憶を調節する.
- トランスメンブレーンAMPAR調節タンパク質 (TARP) とコニホモログ (CNIH) は,異なる役割を持つ主要なAMPAR補助サブユニットカテゴリーである.
研究 の 目的:
- CNIH3との複合でAMPARの高解像度構造を決定する.
- CNIH3媒介のAMPAR調節と複合組成の背後にある分子メカニズムを解明する.
主な方法:
- 高解像度冷凍電子顕微鏡 (冷凍EM)
主要な成果:
- AMPAR/CNIH3複合体の冷凍-EM構造を決定した.
- CNIH3の膜トポロジを明らかにし,四つのトランスメブランヘリクスを特徴とし,細胞外ドメインがない.
- 経路調節に不可欠なタンパク質とタンパク質の相互作用界面を特定した.
- AMPAR/CNIH3複合体を囲む脂質環境を特徴づけた.
結論:
- CNIH3の構造と相互作用は,AMPAR補助サブユニットの機能に関する新しい洞察を提供します.
- CNIHタンパク質によるイオンチャネル調節の分子基礎を明らかにした.
- これらの構造は,神経伝達におけるAMPAR複合体の構成と機能の理解を進める.
関連する概念動画
Structure of Cadherins
4.6K
The cadherins were one of the first cell adhesion molecules discovered; the term “cadherins” is based on their calcium-dependent adhering properties. The first cadherins discovered on the epithelial, neuronal, and placental cells were named E-cadherin, P-cadherin, and N-cadherin, respectively. These classical cadherins share sequence and structural similarities. Other cadherins, including those involved in cell signaling, are grouped into non-classical cadherins. This...
4.6K
Assembly of Signaling Complexes
6.4K
Multiprotein signaling complexes are formed in a dynamic process involving protein-protein interactions at the cytoplasmic domain of transmembrane receptors or enzymatic and non-enzymatic proteins associated with the receptor. These complexes ensure the activation and propagation of intracellular signals that regulate cell functions.
Interaction domains in cell signaling
Interaction domains recognize exposed features of their binding partners containing post-translationally modified sequences,...
Interaction domains in cell signaling
Interaction domains recognize exposed features of their binding partners containing post-translationally modified sequences,...
6.4K
G-protein Coupled Receptors
131.2K
G-protein coupled receptors are ligand binding receptors that indirectly affect changes in the cell. The actual receptor is a single polypeptide that transverses the cell membrane seven times creating intracellular and extracellular loops. The extracellular loops create a ligand specific pocket which binds to neurotransmitters or hormones. The intracellular loops holds onto the G-protein.
131.2K
Calmodulin-dependent Signaling
5.9K
Calmodulin (CaM) is a calcium-binding protein in eukaryotes that controls various calcium-regulated cellular processes. It has four calcium-binding sites that bind calcium to form the calcium-calmodulin ( Ca2+-CaM) complex. GPCR stimulation increases the calcium levels in the cells that bind to CaM and induces a conformational change.
The Ca2+-CaM complex does not have enzymatic activity by itself. Instead, the complex binds downstream target proteins, including membrane proteins or enzymes,...
The Ca2+-CaM complex does not have enzymatic activity by itself. Instead, the complex binds downstream target proteins, including membrane proteins or enzymes,...
5.9K
Adrenergic Receptors: ɑ Subtype
2.6K
Adrenoceptors are classified into α and ꞵ classes based on their potencies to catecholamine agonists. α-adrenoceptors show the following order of catecholamine potency:
Adrenaline ≥ Noradrenaline >> Isoprenaline
α-adrenoceptors are further divided into α1 and α2-adrenoceptors.
α1-Adrenoceptors: These receptors are located postsynaptically on the effector organs and cause constriction of smooth muscle mediated by activation of phospholipase...
Adrenaline ≥ Noradrenaline >> Isoprenaline
α-adrenoceptors are further divided into α1 and α2-adrenoceptors.
α1-Adrenoceptors: These receptors are located postsynaptically on the effector organs and cause constriction of smooth muscle mediated by activation of phospholipase...
2.6K
Tension Response at Adherens Junctions
3.4K
The adherens junctions that anchor cells together are multi-protein complexes that dynamically adapt to mechanical stimuli such as tensile forces and shear stress. Mechanosensory proteins in these junctions can sense such mechanical stimuli and undergo a shift in their conformation, resulting in an altered function — a process called mechanotransduction.
α-Catenin as a Mechanosensory Protein
The α-catenin of adherens junctions is an allosteric protein with three VH (vinculin...
α-Catenin as a Mechanosensory Protein
The α-catenin of adherens junctions is an allosteric protein with three VH (vinculin...
3.4K

