High-resolution structure of a fish aquaporin reveals a novel extracellular fold
(2022) In Life Science Alliance 5(12).- Abstract
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 (Anabas testudineus), 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... (More)
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 (Anabas testudineus), 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.
(Less)
- author
- organization
- publishing date
- 2022
- type
- Contribution to journal
- publication status
- published
- subject
- in
- Life Science Alliance
- volume
- 5
- issue
- 12
- article number
- e202201491
- publisher
- Rockefeller University Press
- external identifiers
-
- scopus:85139812432
- pmid:36229063
- ISSN
- 2575-1077
- DOI
- 10.26508/lsa.202201491
- language
- English
- LU publication?
- yes
- id
- c1553adb-11f5-4d5e-86ef-6f5bf3dfbfe1
- date added to LUP
- 2022-12-13 11:03:24
- date last changed
- 2024-09-20 06:43:35
@article{c1553adb-11f5-4d5e-86ef-6f5bf3dfbfe1,
abstract = {{<p>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 (Anabas testudineus), 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.</p>}},
author = {{Zeng, Jiao and Schmitz, Florian and Isaksson, Simon and Glas, Jessica and Arbab, Olivia and Andersson, Martin and Sundell, Kristina and Eriksson, Leif A. and Swaminathan, Kunchithapadam and Törnroth-Horsefield, Susanna and Hedfalk, Kristina}},
issn = {{2575-1077}},
language = {{eng}},
number = {{12}},
publisher = {{Rockefeller University Press}},
series = {{Life Science Alliance}},
title = {{High-resolution structure of a fish aquaporin reveals a novel extracellular fold}},
url = {{http://dx.doi.org/10.26508/lsa.202201491}},
doi = {{10.26508/lsa.202201491}},
volume = {{5}},
year = {{2022}},
}