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High-resolution structure of a fish aquaporin reveals a novel extracellular fold

Zeng, Jiao ; Schmitz, Florian ; Isaksson, Simon ; Glas, Jessica ; Arbab, Olivia ; Andersson, Martin ; Sundell, Kristina ; Eriksson, Leif A. ; Swaminathan, Kunchithapadam and Törnroth-Horsefield, Susanna LU , et al. (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.

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organization
publishing date
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
2025-05-03 03:58:31
@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}},
}