| Title: |
Plant Aquaporin Gating Is Reversed by Phosphorylation on Intracellular Loop D—Evidence from Molecular Dynamics Simulations |
| Authors: |
Mom, Robin; Réty, Stéphane; Mocquet, Vincent; Auguin, Daniel |
| Contributors: |
Laboratoire de biologie et modélisation de la cellule (LBMC UMR 5239); École normale supérieure de Lyon (ENS de Lyon); Université de Lyon-Université de Lyon-Université Claude Bernard Lyon 1 (UCBL); Université de Lyon-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS); Laboratoire de Biologie des Ligneux et des Grandes Cultures (LBLGC); Université d'Orléans (UO)-Institut National de Recherche pour l’Agriculture, l’Alimentation et l’Environnement (INRAE) |
| Source: |
ISSN: 1661-6596. |
| Publisher Information: |
CCSD; MDPI |
| Publication Year: |
2023 |
| Collection: |
Inserm: HAL (Institut national de la santé et de la recherche médicale) |
| Subject Terms: |
aquaporin PIP gating phosphorylation in silico analysis; aquaporin; PIP; gating; phosphorylation; in silico analysis; [SDV]Life Sciences [q-bio] |
| Description: |
International audience ; Aquaporins (AQPs) constitute a wide and ancient protein family of transmembrane channels dedicated to the regulation of water exchange across biological membranes. In plants, higher numbers of AQP homologues have been conserved compared to other kingdoms of life such as in animals or in bacteria. As an illustration of this plant-specific functional diversity, plasma membrane intrinsic proteins (PIPs, i.e., a subfamily of plant AQPs) possess a long intracellular loop D, which can gate the channel by changing conformation as a function of the cellular environment. However, even though the closure of the AQP by loop D conformational changes is well described, the opening of the channel, on the other hand, is still misunderstood. Several studies have pointed to phosphorylation events as the trigger for the transition from closed- to open-channel states. Nonetheless, no clear answer has been obtained yet. Hence, in order to gain a more complete grasp of plant AQP regulation through this intracellular loop D gating, we investigated the opening of the channel in silico through molecular dynamics simulations of the crystallographic structure of Spinacia oleracea PIP2;1 (SoPIP2;1). Through this technique, we addressed the mechanistic details of these conformational changes, which eventually allowed us to propose a molecular mechanism for PIP functional regulation by loop D phosphorylation. More precisely, our results highlight the phosphorylation of loop D serine 188 as a trigger of SoPIP2;1 water channel opening. Finally, we discuss the significance of this result for the study of plant AQP functional diversity. |
| Document Type: |
article in journal/newspaper |
| Language: |
English |
| Relation: |
info:eu-repo/semantics/altIdentifier/pmid/37762101; PUBMED: 37762101; WOS: 001145205500001 |
| DOI: |
10.3390/ijms241813798 |
| Availability: |
https://hal.science/hal-04218511; https://hal.science/hal-04218511v1/document; https://hal.science/hal-04218511v1/file/ijms-24-13798-v2.pdf; https://doi.org/10.3390/ijms241813798 |
| Rights: |
https://creativecommons.org/licenses/by/4.0/ ; info:eu-repo/semantics/OpenAccess |
| Accession Number: |
edsbas.9350DEC |
| Database: |
BASE |