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-Structure paper
タイトル | High-resolution electron cryomicroscopy of V-ATPase in native synaptic vesicles. |
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ジャーナル・号・ページ | Science, Vol. 385, Issue 6705, Page 168-174, Year 2024 |
掲載日 | 2024年7月12日 |
著者 | Claire E Coupland / Ryan Karimi / Stephanie A Bueler / Yingke Liang / Gautier M Courbon / Justin M Di Trani / Cassandra J Wong / Rayan Saghian / Ji-Young Youn / Lu-Yang Wang / John L Rubinstein / |
PubMed 要旨 | Intercellular communication in the nervous system occurs through the release of neurotransmitters into the synaptic cleft between neurons. In the presynaptic neuron, the proton pumping vesicular- or ...Intercellular communication in the nervous system occurs through the release of neurotransmitters into the synaptic cleft between neurons. In the presynaptic neuron, the proton pumping vesicular- or vacuolar-type ATPase (V-ATPase) powers neurotransmitter loading into synaptic vesicles (SVs), with the V complex dissociating from the membrane region of the enzyme before exocytosis. We isolated SVs from rat brain using SidK, a V-ATPase-binding bacterial effector protein. Single-particle electron cryomicroscopy allowed high-resolution structure determination of V-ATPase within the native SV membrane. In the structure, regularly spaced cholesterol molecules decorate the enzyme's rotor and the abundant SV protein synaptophysin binds the complex stoichiometrically. ATP hydrolysis during vesicle loading results in a loss of the V region of V-ATPase from the SV membrane, suggesting that loading is sufficient to induce dissociation of the enzyme. |
リンク | Science / PubMed:38900912 |
手法 | EM (単粒子) |
解像度 | 3.2 - 3.9 Å |
構造データ | EMDB-44350, PDB-9b8o: EMDB-44351, PDB-9b8p: EMDB-44352, PDB-9b8q: EMDB-44353, PDB-9brd: EMDB-44354, PDB-9brc: EMDB-44355, PDB-9brb: |
化合物 | ChemComp-PC1: ChemComp-WJP: ChemComp-NAG: ChemComp-LP3: ChemComp-PTY: ChemComp-CLR: ChemComp-ADP: |
由来 |
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キーワード | PROTON TRANSPORT / Membrane / Synaptic / Complex / Mmebrane / Native / Vesicle |