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Structures Of A Complete Human V-Atpase Reveal Mechanisms Of Its

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Wang, L., Wu, D., Robinson, C. V., Wu, H., & Fu, T.-M. (2020). Structures of a Complete Human V-ATPase Reveal Mechanisms of Its Assembly. Molecular Cell. doi:10.1016

人源V-ATPase高分辨率结构

6WM4 Human V-ATPase in state 3 with SidK and ADP Summary for 6WM4 Structure validation Download full validation report

Vacuolar ATPase (V-ATPase) Proton Pump and Its Significance in Human ...

Wang et al. (2020a) present near-atomic resolution cryo-EM structures of endoge-nous human V-ATPase, providing the mostdetailedpictureofanintactV-ATPase from any source. V-ATPase is a large, multisubunit enzyme complex composed of membrane extrinsic V1-ATPase and membrane inte-gral Vo proton channel subcomplexes (Figure 1).

In V 0, the c ring rotates relative to the membrane-embedded C-terminal structural domain of subunit a, driving proton translocation across the membrane. Structural research on the human V-ATPase The researchers report cryo-electron microscopy structures of human V-ATPase in three rotational states with a resolution of up to 2.9 Å. More recent studies on mammalian V-ATPases have provide mechanistic insights into the assembly and regulation of mammalian V-ATPases. In particular, high-resolution cryo-EM structures of human V-ATPases represent the first complete structure of mammalian V-ATPases.

Structures of a Complete Human V-ATPase Reveal Mechanisms of Its Assembly Vesicular- or vacuolar-type adenosine triphosphatases (V-ATPases) are ATP-driven proton pumps comprised of a cytoplasmic V 1 complex for ATP hydrolysis and a

Vesicular- or vacuolar-type adenosine triphosphatases (V-ATPases) are ATP-driven proton pumps comprised of a cytoplasmic V1 complex for ATP hydrolysis and a membrane-embedded Vo complex for proton transfer. They play important roles in acidification of intracellular vesicles, organelles, and the extracellular milieu in eukaryotes. Here, we report cryoelectron microscopy 其中，他们对阳离子通道 TRPM2 的研究发表于2018年的 Science 杂志上 【3】。 2020年10月15日， 傅天民 博士、 王隆飞 博士和 吴皓 院士在 Molecular Cell

Our structure shows that mEAK-7 interacts with subunits A, B, D, and E of V-ATPases in state 2. Thus, we propose that mEAK-7 may regulate V-ATPase function through binding to V-ATPases in state 2 as well as mediate mTOR signaling. EMPIAR-11132 Cryo-EM structures of human V-ATPase Publication: Structures of a Complete Human V-ATPase Reveal Mechanisms of Its Assembly Wang L , Wu D, Robinson CV, Wu H , Fu TM Mol Cell 80 501 -511000.0 (2020) PMID: 33065002 Structural basis of V-ATPase regulation by endogenous proteins is unclear. Here, the authors find mEAK7 as an endogenous V-ATPase modulator and determine its structure with V-ATPase, suggesting

  • 北京大学生命科学学院
  • 人源V-ATPase高分辨率结构
  • Cryo-EM structures of intact V-ATPase from bovine brain
  • EMPIAR-11132 Cryo-EM structures of human V-ATPase

Article „Structures of a Complete Human V-ATPase Reveal Mechanisms of Its Assembly“ Detailed information of the J-GLOBAL is an information service managed by the Japan Science and Technology Agency (hereinafter referred to as „JST“). It provides free access to secondary information on researchers, articles, patents, etc., in science and technology, medicine and

Structures of a complete human V-ATPase reveal mechanisms of its assembly Molecular Cell 2020, 80 (3), 501-511. Vora SM*, Fontana P*, Mao T, Leger V, 其中，他们对阳离子通道TRPM2的研究发表于2018年的Science杂志上【3】。 2020年10月15日，傅天民博士、王隆飞博士和吴皓院士在Molecular Cell上发表了文章Structures of a Complete Human V-ATPase Reveal Mechanisms of Its Assembly，解析了人源V-ATPase高分辨率结构 Abstract Wang et al. report the mechanisms of human V-ATPase assembly. Cryo-EM structures of human V-ATPase combined with mass spectrometry analysis reveal that the protein subunits, glycans, glycolipids, and phospholipids are essential components of V-ATPase. The subunit ATP6AP1, glycans, and lipids have important roles in V-ATPase assembly and biogenesis.

Long-standing challenges in purifying mammalian V-ATPases have limited the biochemical and structural study of mammalian V-ATPase. Here, we provide a protocol for purifying milligrams of human V-ATPase and detail procedures for the reconstruction of its structure by cryo-EM. Wang et al. report the mechanisms of human V-ATPase assembly. Cryo-EM structures of human V-ATPase combined with mass spectrometry analysis reveal that the protein subunits, glycans, glycolipids, and phospholipids are essential components of V-ATPase. The subunit ATP6AP1, glycans, and lipids have important roles in V-ATPase assembly and biogenesis. Wang et al. report the mechanisms of human V-ATPase assembly. Cryo-EM structures of human V-ATPase combined with mass spectrometry analysis reveal that the protein subunits, glycans, glycolipids, and phospholipids are essential components of V-ATPase. The subunit ATP6AP1, glycans, and lipids have important roles in V-ATPase assembly and biogenesis.

Structure of V-ATPase from citrus fruit: Structure

Vesicular- or vacuolar-type adenosine triphosphatases (V-ATPases) are ATP-driven proton pumps comprised of a cytoplasmic V1 complex for ATP hydrolysis and a membrane-embedded Vo complex for proton transfer. They play important roles in acidification of intracellular vesicles, organelles, and the extracellular milieu in eukaryotes. Here, we report cryoelectron microscopy Wang et al. report the mechanisms of human V-ATPase assembly. Cryo-EM structures of human V-ATPase combined with mass spectrometry analysis reveal that the protein subunits, glycans, glycolipids, and phospholipids are essential components of V-ATPase. The subunit ATP6AP1, glycans, and lipids have important roles in V-ATPase assembly and biogenesis.

EMD-21849 – Human V-ATPase in state 3 with SidK and ADP 此外，Synaptophysin还可以与Synaptobrevin寡聚形成更大的复合物，进一步增加V-ATPase相关复合体的尺寸。 这些由Synaptophysin介导的相互作用会增加突触小泡表面分子的拥挤程度，从而限制V-ATPase的随机插入，实现对突触小泡上V-ATPase拷贝数的调控。

2020年10月15日， 傅天民 博士、 王隆飞 博士和 吴皓 院士在 Molecular Cell 上发表了文章 Structures of a Complete Human V-ATPase Reveal Mechanisms of Its Assembly，解析了人源V-ATPase高分辨率结构 【4】。 We determine cryo-EM structure of human mEAK7 in complex with human V-ATPase in native lipid-containing nanodiscs. Isoforms of subunit a are involved in regulation both via the control of coupling and via selective targeting. This review will begin with a brief introduction to the function, structure, and mechanism of the V-ATPases followed by a discussion of the role of V-ATPase subunit isoforms and the mechanisms involved in regulation of V

The rotary ATPases use a rotary catalytic mechanism to drive transmembrane proton movement powered by ATP hydrolysis. Here, the authors report a collection of V/A-ATPase V1 domain structures 北京大学生命科学学院研究者采用了冷冻电子断层扫描（cryo-ET）和单颗粒三维重构技术，对小鼠大脑中分离的谷氨酸能突触小泡进行了表征。结果表明，在突触小泡上 V-ATPase 能够与 Synaptophysin 形成 1： 1 化学计量比的稳定复合物，而该复合物在此前分离纯化的样品中未被观察到 1-4。为了进一步区分 Cryo-EM structures of ASC and NLRC4 CARD filaments reveal a unified mechanism of nucleation and activation of caspase-1 Li Y*, Fu TM*†, Lu A, Witt K, Ruan J, Shen C, Wu H†.

Here, we report cryoelectron microscopy structures of human V-ATPase in three rotational states at up to 2.9-Å resolution. Aided by mass spectrometry, we build all known protein subunits with associated N-linked glycans and identify RELION: Implementation of a Bayesian approach to cryo-EM structure determination Journal of Structural Biology, 2012 Definition of Membrane Topology and Identification of Residues Important for Transport in Subunit a of the Vacuolar ATPase Journal of Biological Chemistry, 2011 Regulation and Isoform Function of the V-ATPases Biochemistry, 2010 PHENIX: a

Structures of a Complete Human V-ATPase Reveal Mechanisms of Its Assembly Longfei Wang, Di Wu, Carol V. Robinson, Hao Wu, Tian-Min Fu Molecular Cell Volume 80 Issue 3 Pages 501-511.e3 (November 2020)

Cryo-EM structures of human V-ATPase combined with mass spectrometry analysis reveal that the protein subunits, glycans, glycolipids, and phospholipids are essential components of V-ATPase.