Aquaporin protein-protein interactions
(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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- author
- Roche, Jennifer Virginia LU and Törnroth-Horsefield, Susanna LU
- organization
- publishing date
- 2017-11-01
- 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
- article number
- 2255
- publisher
- MDPI AG
- external identifiers
-
- pmid:29077056
- wos:000416811300029
- scopus:85032570345
- 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
- 2024-03-31 20:03:26
@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>}},
author = {{Roche, Jennifer Virginia and Törnroth-Horsefield, Susanna}},
issn = {{1661-6596}},
keywords = {{Aquaporin; Gating; Membrane channel; Membrane protein; Protein-protein interactions; Trafficking}},
language = {{eng}},
month = {{11}},
number = {{11}},
publisher = {{MDPI AG}},
series = {{International Journal of Molecular Sciences}},
title = {{Aquaporin protein-protein interactions}},
url = {{http://dx.doi.org/10.3390/ijms18112255}},
doi = {{10.3390/ijms18112255}},
volume = {{18}},
year = {{2017}},
}