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Aquaporin protein-protein interactions

Roche, Jennifer Virginia LU and Törnroth-Horsefield, Susanna LU (2017) In International Journal of Molecular Sciences 18(11).
Abstract

Aquaporins are tetrameric membrane-bound channels that facilitate transport of water and other small solutes across cell membranes. In eukaryotes, they are frequently regulated by gating or trafficking, allowing for the cell to control membrane permeability in a specific manner. Protein-protein interactions play crucial roles in both regulatory processes and also mediate alternative functions such as cell adhesion. In this review, we summarize recent knowledge about aquaporin protein-protein interactions; dividing the interactions into three types: (1) interactions between aquaporin tetramers; (2) interactions between aquaporin monomers within a tetramer (hetero-tetramerization); and (3) transient interactions with regulatory proteins.... (More)

Aquaporins are tetrameric membrane-bound channels that facilitate transport of water and other small solutes across cell membranes. In eukaryotes, they are frequently regulated by gating or trafficking, allowing for the cell to control membrane permeability in a specific manner. Protein-protein interactions play crucial roles in both regulatory processes and also mediate alternative functions such as cell adhesion. In this review, we summarize recent knowledge about aquaporin protein-protein interactions; dividing the interactions into three types: (1) interactions between aquaporin tetramers; (2) interactions between aquaporin monomers within a tetramer (hetero-tetramerization); and (3) transient interactions with regulatory proteins. We particularly focus on the structural aspects of the interactions, discussing the small differences within a conserved overall fold that allow for aquaporins to be differentially regulated in an organism-, tissueand trigger-specific manner. A deep knowledge about these differences is needed to fully understand aquaporin function and regulation in many physiological processes, and may enable design of compounds targeting specific aquaporins for treatment of human disease.

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Please use this url to cite or link to this publication:
author
organization
publishing date
type
Contribution to journal
publication status
published
subject
keywords
Aquaporin, Gating, Membrane channel, Membrane protein, Protein-protein interactions, Trafficking
in
International Journal of Molecular Sciences
volume
18
issue
11
publisher
MOLECULAR DIVERSITY PRESERVATION INT
external identifiers
  • scopus:85032570345
  • wos:000416811300029
ISSN
1661-6596
DOI
10.3390/ijms18112255
language
English
LU publication?
yes
id
32ea4187-6370-4e2e-9565-ea621349a699
date added to LUP
2017-11-07 12:37:25
date last changed
2018-02-07 03:00:15
@article{32ea4187-6370-4e2e-9565-ea621349a699,
  abstract     = {<p>Aquaporins are tetrameric membrane-bound channels that facilitate transport of water and other small solutes across cell membranes. In eukaryotes, they are frequently regulated by gating or trafficking, allowing for the cell to control membrane permeability in a specific manner. Protein-protein interactions play crucial roles in both regulatory processes and also mediate alternative functions such as cell adhesion. In this review, we summarize recent knowledge about aquaporin protein-protein interactions; dividing the interactions into three types: (1) interactions between aquaporin tetramers; (2) interactions between aquaporin monomers within a tetramer (hetero-tetramerization); and (3) transient interactions with regulatory proteins. We particularly focus on the structural aspects of the interactions, discussing the small differences within a conserved overall fold that allow for aquaporins to be differentially regulated in an organism-, tissueand trigger-specific manner. A deep knowledge about these differences is needed to fully understand aquaporin function and regulation in many physiological processes, and may enable design of compounds targeting specific aquaporins for treatment of human disease.</p>},
  articleno    = {2255},
  author       = {Roche, Jennifer Virginia and Törnroth-Horsefield, Susanna},
  issn         = {1661-6596},
  keyword      = {Aquaporin,Gating,Membrane channel,Membrane protein,Protein-protein interactions,Trafficking},
  language     = {eng},
  month        = {11},
  number       = {11},
  publisher    = {MOLECULAR DIVERSITY PRESERVATION INT},
  series       = {International Journal of Molecular Sciences},
  title        = {Aquaporin protein-protein interactions},
  url          = {http://dx.doi.org/10.3390/ijms18112255},
  volume       = {18},
  year         = {2017},
}