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Cryo-EM structures of intact V-ATPase from bovine brain

The vacuolar-type H(+)-ATPases (V-ATPase) hydrolyze ATP to pump protons across the plasma or intracellular membrane, secreting acids to the lumen or acidifying intracellular compartments. It has been implicated in tumor metastasis, renal tubular acidosis, and osteoporosis. Here, we report two cryo-E...

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Autores principales: Wang, Rong, Long, Tao, Hassan, Abdirahman, Wang, Jin, Sun, Yingyuan, Xie, Xiao-Song, Li, Xiaochun
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Nature Publishing Group UK 2020
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7414150/
https://www.ncbi.nlm.nih.gov/pubmed/32764564
http://dx.doi.org/10.1038/s41467-020-17762-9
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author Wang, Rong
Long, Tao
Hassan, Abdirahman
Wang, Jin
Sun, Yingyuan
Xie, Xiao-Song
Li, Xiaochun
author_facet Wang, Rong
Long, Tao
Hassan, Abdirahman
Wang, Jin
Sun, Yingyuan
Xie, Xiao-Song
Li, Xiaochun
author_sort Wang, Rong
collection PubMed
description The vacuolar-type H(+)-ATPases (V-ATPase) hydrolyze ATP to pump protons across the plasma or intracellular membrane, secreting acids to the lumen or acidifying intracellular compartments. It has been implicated in tumor metastasis, renal tubular acidosis, and osteoporosis. Here, we report two cryo-EM structures of the intact V-ATPase from bovine brain with all the subunits including the subunit H, which is essential for ATPase activity. Two type-I transmembrane proteins, Ac45 and (pro)renin receptor, along with subunit c”, constitute the core of the c-ring. Three different conformations of A/B heterodimers suggest a mechanism for ATP hydrolysis that triggers a rotation of subunits DF, inducing spinning of subunit d with respect to the entire c-ring. Moreover, many lipid molecules have been observed in the Vo domain to mediate the interactions between subunit c, c”, (pro)renin receptor, and Ac45. These two structures reveal unique features of mammalian V-ATPase and suggest a mechanism of V1-Vo torque transmission.
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spelling pubmed-74141502020-08-17 Cryo-EM structures of intact V-ATPase from bovine brain Wang, Rong Long, Tao Hassan, Abdirahman Wang, Jin Sun, Yingyuan Xie, Xiao-Song Li, Xiaochun Nat Commun Article The vacuolar-type H(+)-ATPases (V-ATPase) hydrolyze ATP to pump protons across the plasma or intracellular membrane, secreting acids to the lumen or acidifying intracellular compartments. It has been implicated in tumor metastasis, renal tubular acidosis, and osteoporosis. Here, we report two cryo-EM structures of the intact V-ATPase from bovine brain with all the subunits including the subunit H, which is essential for ATPase activity. Two type-I transmembrane proteins, Ac45 and (pro)renin receptor, along with subunit c”, constitute the core of the c-ring. Three different conformations of A/B heterodimers suggest a mechanism for ATP hydrolysis that triggers a rotation of subunits DF, inducing spinning of subunit d with respect to the entire c-ring. Moreover, many lipid molecules have been observed in the Vo domain to mediate the interactions between subunit c, c”, (pro)renin receptor, and Ac45. These two structures reveal unique features of mammalian V-ATPase and suggest a mechanism of V1-Vo torque transmission. Nature Publishing Group UK 2020-08-06 /pmc/articles/PMC7414150/ /pubmed/32764564 http://dx.doi.org/10.1038/s41467-020-17762-9 Text en © The Author(s) 2020 Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/.
spellingShingle Article
Wang, Rong
Long, Tao
Hassan, Abdirahman
Wang, Jin
Sun, Yingyuan
Xie, Xiao-Song
Li, Xiaochun
Cryo-EM structures of intact V-ATPase from bovine brain
title Cryo-EM structures of intact V-ATPase from bovine brain
title_full Cryo-EM structures of intact V-ATPase from bovine brain
title_fullStr Cryo-EM structures of intact V-ATPase from bovine brain
title_full_unstemmed Cryo-EM structures of intact V-ATPase from bovine brain
title_short Cryo-EM structures of intact V-ATPase from bovine brain
title_sort cryo-em structures of intact v-atpase from bovine brain
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7414150/
https://www.ncbi.nlm.nih.gov/pubmed/32764564
http://dx.doi.org/10.1038/s41467-020-17762-9
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