High-resolution structure of a fish aquaporin reveals a novel extracellular fold.
Journal
Life science alliance
ISSN: 2575-1077
Titre abrégé: Life Sci Alliance
Pays: United States
ID NLM: 101728869
Informations de publication
Date de publication:
13 10 2022
13 10 2022
Historique:
received:
20
04
2022
revised:
21
09
2022
accepted:
22
09
2022
entrez:
13
10
2022
pubmed:
14
10
2022
medline:
18
10
2022
Statut:
epublish
Résumé
Aquaporins are protein channels embedded in the lipid bilayer in cells from all organisms on earth that are crucial for water homeostasis. In fish, aquaporins are believed to be important for osmoregulation; however, the molecular mechanism behind this is poorly understood. Here, we present the first structural and functional characterization of a fish aquaporin; cpAQP1aa from the fresh water fish climbing perch (<i>Anabas testudineus</i>), a species that is of high osmoregulatory interest because of its ability to spend time in seawater and on land. These studies show that cpAQP1aa is a water-specific aquaporin with a unique fold on the extracellular side that results in a constriction region. Functional analysis combined with molecular dynamic simulations suggests that phosphorylation at two sites causes structural perturbations in this region that may have implications for channel gating from the extracellular side.
Identifiants
pubmed: 36229063
pii: 5/12/e202201491
doi: 10.26508/lsa.202201491
pmc: PMC9559756
pii:
doi:
Substances chimiques
Aquaporins
0
Lipid Bilayers
0
Water
059QF0KO0R
Banques de données
PDB
['3GD8', '6QZI', '5I32', '1J4N', '3C02', '2B6O', '1YMG', '1Z98', '2B5F', '7W7S', '7W7R']
GENBANK
['JX645188.1']
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Informations de copyright
© 2022 Zeng et al.
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