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High-resolution x-ray structure of human aquaporin 5

Horsefield, Rob; Nordén, Kristina LU ; Agemark, Maria LU ; Backmark, Anna; Tornroth-Horsefield, Susanna; van Scheltinga, Anke C. Terwisscha; Kvassman, Jan; Kjellbom, Per LU ; Johanson, Urban LU and Neutze, Richard (2008) In Proceedings of the National Academy of Sciences 105(36). p.13327-13332
Abstract
Human aquaporin 5 (HsAQP5)facilitates the transport of water across plasma membranes and has been identified within cells of the stomach, duodenum, pancreas, airways, lungs, salivary glands, sweat glands, eyes, lacrimal glands, and the inner ear. AQP5, like AQP2, is subject to posttranslational regulation by phosphorylation, at which point it is trafficked between intracellular storage compartments and the plasma membrane. Details concerning the molecular mechanism of membrane trafficking are unknown. Here we report the x-ray structure of HsAQP5 to 2.0-angstrom resolution and highlight structural similarities and differences relative to other eukaryotic aquaporins. A lipid occludes the putative central pore, preventing the passage of gas... (More)
Human aquaporin 5 (HsAQP5)facilitates the transport of water across plasma membranes and has been identified within cells of the stomach, duodenum, pancreas, airways, lungs, salivary glands, sweat glands, eyes, lacrimal glands, and the inner ear. AQP5, like AQP2, is subject to posttranslational regulation by phosphorylation, at which point it is trafficked between intracellular storage compartments and the plasma membrane. Details concerning the molecular mechanism of membrane trafficking are unknown. Here we report the x-ray structure of HsAQP5 to 2.0-angstrom resolution and highlight structural similarities and differences relative to other eukaryotic aquaporins. A lipid occludes the putative central pore, preventing the passage of gas or ions through the center of the tetramer. Multiple consensus phosphorylation sites are observed in the structure and their potential regulatory role is discussed. We postulate that a change in the conformation of the C terminus may arise from the phosphorylation of AQP5 and thereby signal trafficking. (Less)
Please use this url to cite or link to this publication:
author
organization
publishing date
type
Contribution to journal
publication status
published
subject
keywords
heterologous overexpression, crystallography, water channel protein, trafficking, membrane protein
in
Proceedings of the National Academy of Sciences
volume
105
issue
36
pages
13327 - 13332
publisher
National Acad Sciences
external identifiers
  • wos:000259251700029
  • scopus:51649115305
ISSN
1091-6490
DOI
10.1073/pnas.0801466105
language
English
LU publication?
yes
id
a3999865-0467-4519-ba1f-5f166fa7afc2 (old id 1246817)
alternative location
http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=18768791
date added to LUP
2008-11-20 12:00:41
date last changed
2017-11-12 03:27:57
@article{a3999865-0467-4519-ba1f-5f166fa7afc2,
  abstract     = {Human aquaporin 5 (HsAQP5)facilitates the transport of water across plasma membranes and has been identified within cells of the stomach, duodenum, pancreas, airways, lungs, salivary glands, sweat glands, eyes, lacrimal glands, and the inner ear. AQP5, like AQP2, is subject to posttranslational regulation by phosphorylation, at which point it is trafficked between intracellular storage compartments and the plasma membrane. Details concerning the molecular mechanism of membrane trafficking are unknown. Here we report the x-ray structure of HsAQP5 to 2.0-angstrom resolution and highlight structural similarities and differences relative to other eukaryotic aquaporins. A lipid occludes the putative central pore, preventing the passage of gas or ions through the center of the tetramer. Multiple consensus phosphorylation sites are observed in the structure and their potential regulatory role is discussed. We postulate that a change in the conformation of the C terminus may arise from the phosphorylation of AQP5 and thereby signal trafficking.},
  author       = {Horsefield, Rob and Nordén, Kristina and Agemark, Maria and Backmark, Anna and Tornroth-Horsefield, Susanna and van Scheltinga, Anke C. Terwisscha and Kvassman, Jan and Kjellbom, Per and Johanson, Urban and Neutze, Richard},
  issn         = {1091-6490},
  keyword      = {heterologous overexpression,crystallography,water channel protein,trafficking,membrane protein},
  language     = {eng},
  number       = {36},
  pages        = {13327--13332},
  publisher    = {National Acad Sciences},
  series       = {Proceedings of the National Academy of Sciences},
  title        = {High-resolution x-ray structure of human aquaporin 5},
  url          = {http://dx.doi.org/10.1073/pnas.0801466105},
  volume       = {105},
  year         = {2008},
}