Current progress in plant V-ATPase : From biochemical properties to physiological functions
Copyright © 2021 Elsevier GmbH. All rights reserved.
| Publié dans: | Journal of plant physiology. - 1979. - 266(2021) vom: 15. Nov., Seite 153525 |
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| Auteur principal: | |
| Autres auteurs: | , |
| Format: | Article en ligne |
| Langue: | English |
| Publié: |
2021
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| Accès à la collection: | Journal of plant physiology |
| Sujets: | Journal Article Review Stress response Structure TGN/EE V-ATPase Vacuole pH homeostasis Adenosine Triphosphate 8L70Q75FXE plus... |
| Résumé: | Copyright © 2021 Elsevier GmbH. All rights reserved. Vacuolar-type adenosine triphosphatase (V-ATPase, VHA) is a highly conserved, ATP-driven multisubunit proton pump that is widely distributed in all eukaryotic cells. V-ATPase consists of two domains formed by at least 13 different subunits, the membrane peripheral V1 domain responsible for ATP hydrolysis, and the membrane-integral V0 domain responsible for proton translocation. V-ATPase plays an essential role in energizing secondary active transport and is indispensable to plants. In addition to multiple stress responses, plant V-ATPase is also implicated in physiological processes such as growth, development, and morphogenesis. Based on the identification of distinct V-ATPase mutants and advances in luminal pH measurements in vivo, it has been revealed that this holoenzyme complex plays a pivotal role in pH homeostasis of the plant endomembrane system and endocytic and secretory trafficking. Here, we review recent progress in comprehending the biochemical properties and physiological functions of plant V-ATPase and explore the topics that require further elucidation |
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| Description: | Date Completed 13.01.2022 Date Revised 13.01.2022 published: Print-Electronic Citation Status MEDLINE |
| ISSN: | 1618-1328 |
| DOI: | 10.1016/j.jplph.2021.153525 |