Harrison, MA orcid.org/0000-0002-7826-7472 and Muench, SP orcid.org/0000-0001-6869-4414 (2018) The vacuolar ATPase – a nano-scale motor that drives cell biology. In: Harris, JR and Boekema, EJ, (eds.) Membrane Protein Complexes: Structure and Function. Subcellular Biochemistry, 87 . Springer Nature , Singapore , pp. 409-459. ISBN 978-981-10-7756-2
Abstract
The vacuolar H+-ATPase (V-ATPase) is a ~1 MDa membrane protein complex that couples the hydrolysis of cytosolic ATP to the transmembrane movement of protons. In essentially all eukaryotic cells, this acid pumping function plays critical roles in the acidification of endosomal/lysosomal compartments and hence in transport, recycling and degradative pathways. It is also important in acid extrusion across the plasma membrane of some cells, contributing to homeostatic control of cytoplasmic pH and maintenance of appropriate extracellular acidity. The complex, assembled from up to 30 individual polypeptides, operates as a molecular motor with rotary mechanics. Historically, structural inferences about the eukaryotic V-ATPase and its subunits have been made by comparison to the structures of bacterial homologues. However, more recently, we have developed a much better understanding of the complete structure of the eukaryotic complex, in particular through advances in cryo-electron microscopy. This chapter explores these recent developments, and examines what they now reveal about the catalytic mechanism of this essential proton pump and how its activity might be regulated in response to cellular signals.
Metadata
Item Type: | Book Section |
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Authors/Creators: |
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Editors: |
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Keywords: | Vacuolar H+-ATPase (V-ATPase); Acidification; Proton pump; Cryo-electron microscopy; Endosomal compartment; Lysosomal compartment; Molecular motor |
Dates: |
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Institution: | The University of Leeds |
Academic Units: | The University of Leeds > Faculty of Biological Sciences (Leeds) > School of Biomedical Sciences (Leeds) |
Funding Information: | Funder Grant number BBSRC BB/D016142/1 Wellcome Trust 109158/B/15/A BBSRC BB/P026397/1 |
Depositing User: | Symplectic Publications |
Date Deposited: | 01 Mar 2018 10:33 |
Last Modified: | 01 Mar 2018 10:33 |
Published Version: | https://link.springer.com/book/10.1007/978-981-10-... |
Status: | Published |
Publisher: | Springer Nature |
Series Name: | Subcellular Biochemistry |
Identification Number: | 10.1007/978-981-10-7757-9_14 |
Open Archives Initiative ID (OAI ID): | oai:eprints.whiterose.ac.uk:127801 |