气候变化领域集成服务门户(CCPortal): Structure of V-ATPase from the mammalian brain

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DOI	10.1126/science.aba1120
	Structure of V-ATPase from the mammalian brain
	Abbas Y.M.; Wu D.; Bueler S.A.; Robinson C.V.; Rubinstein J.L.
发表日期	2020
ISSN	0036-8075
起始页码	1240
结束页码	1246
卷号	367 期号:6483
英文摘要	In neurons, the loading of neurotransmitters into synaptic vesicles uses energy from proton-pumping vesicular- or vacuolar-type adenosine triphosphatases (V-ATPases). These membrane protein complexes possess numerous subunit isoforms, which complicates their analysis. We isolated homogeneous rat brain V-ATPase through its interaction with SidK, a Legionella pneumophila effector protein. Cryo- electron microscopy allowed the construction of an atomic model, defining the enzyme's ATP:proton ratio as 3:10 and revealing a homolog of yeast subunit f in the membrane region, which we tentatively identify as RNAseK. The c ring encloses the transmembrane anchors for cleaved ATP6AP1/Ac45 and ATP6AP2/PRR, the latter of which is the (pro)renin receptor that, in other contexts, is involved in both Wnt signaling and the renin-angiotensin system that regulates blood pressure. This structure shows how ATP6AP1/Ac45 and ATP6AP2/PRR enable assembly of the enzyme's catalytic and membrane regions. © 2020 American Association for the Advancement of Science. All rights reserved.
关键词	adenosine triphosphatase neurotransmitter proton renin unclassified drug vacuolar type adenosine triphosphatase Atp6ap1 protein, rat ATP6AP2 protein, rat bacterial protein biological marker cell surface receptor proton transporting adenosine triphosphate synthase blood brain catalysis catalyst enzyme enzyme activity membrane protein Article axon blood pressure regulation brain tissue catalysis chemical structure cryoelectron microscopy electrolyte balance electron microscopy human hydrolysis Legionella pneumophila molecular docking nerve cell neurotransmitter uptake nonhuman priority journal protein structure signal transduction Wnt signaling yeast animal biocatalysis brain cell membrane chemical model chemistry enzymology protein domain rat renin angiotensin aldosterone system Legionella pneumophila Mammalia Rattus Animals Bacterial Proteins Biocatalysis Biomarkers Brain Cell Membrane Cryoelectron Microscopy Models, Chemical Protein Domains Rats Receptors, Cell Surface Renin-Angiotensin System Vacuolar Proton-Translocating ATPases Wnt Signaling Pathway
语种	英语
来源机构	Science
文献类型	期刊论文
条目标识符	http://gcip.llas.ac.cn/handle/2XKMVOVA/133639
推荐引用方式 GB/T 7714	Abbas Y.M.,Wu D.,Bueler S.A.,et al. Structure of V-ATPase from the mammalian brain[J]. Science,2020,367(6483).
APA	Abbas Y.M.,Wu D.,Bueler S.A.,Robinson C.V.,&Rubinstein J.L..(2020).Structure of V-ATPase from the mammalian brain.,367(6483).
MLA	Abbas Y.M.,et al."Structure of V-ATPase from the mammalian brain".367.6483(2020).