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Aquaporin Protein-Protein Interactions
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 inte...
Autores principales: | , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2017
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5713225/ https://www.ncbi.nlm.nih.gov/pubmed/29077056 http://dx.doi.org/10.3390/ijms18112255 |
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author | Roche, Jennifer Virginia Törnroth-Horsefield, Susanna |
author_facet | Roche, Jennifer Virginia Törnroth-Horsefield, Susanna |
author_sort | Roche, Jennifer Virginia |
collection | PubMed |
description | 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-, tissue- and 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. |
format | Online Article Text |
id | pubmed-5713225 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2017 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
spelling | pubmed-57132252017-12-07 Aquaporin Protein-Protein Interactions Roche, Jennifer Virginia Törnroth-Horsefield, Susanna Int J Mol Sci Review 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-, tissue- and 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. MDPI 2017-10-27 /pmc/articles/PMC5713225/ /pubmed/29077056 http://dx.doi.org/10.3390/ijms18112255 Text en © 2017 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (http://creativecommons.org/licenses/by/4.0/). |
spellingShingle | Review Roche, Jennifer Virginia Törnroth-Horsefield, Susanna Aquaporin Protein-Protein Interactions |
title | Aquaporin Protein-Protein Interactions |
title_full | Aquaporin Protein-Protein Interactions |
title_fullStr | Aquaporin Protein-Protein Interactions |
title_full_unstemmed | Aquaporin Protein-Protein Interactions |
title_short | Aquaporin Protein-Protein Interactions |
title_sort | aquaporin protein-protein interactions |
topic | Review |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5713225/ https://www.ncbi.nlm.nih.gov/pubmed/29077056 http://dx.doi.org/10.3390/ijms18112255 |
work_keys_str_mv | AT rochejennifervirginia aquaporinproteinproteininteractions AT tornrothhorsefieldsusanna aquaporinproteinproteininteractions |