期刊
SCIENCE
卷 367, 期 6483, 页码 1240-+出版社
AMER ASSOC ADVANCEMENT SCIENCE
DOI: 10.1126/science.aaz2924
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资金
- Canadian Institutes of Health Research [PJT166152]
- European Research Council [69551-ENABLE]
- Wellcome Trust [104633/Z/14/Z]
- Restracomp fellowship
- Canada Research Chairs program
- Canada Foundation for Innovation
- Ontario Research Fund
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. Cryoelectron 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.
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