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Aquaporin Gating: A New Twist to Unravel Permeation through Water Channels

Aquaporins (AQPs) are small transmembrane tetrameric proteins that facilitate water, solute and gas exchange. Their presence has been extensively reported in the biological membranes of almost all living organisms. Although their discovery is much more recent than ion transport systems, different bi...

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Autores principales: Ozu, Marcelo, Alvear-Arias, Juan José, Fernandez, Miguel, Caviglia, Agustín, Peña-Pichicoi, Antonio, Carrillo, Christian, Carmona, Emerson, Otero-Gonzalez, Anselmo, Garate, José Antonio, Amodeo, Gabriela, Gonzalez, Carlos
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2022
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9604103/
https://www.ncbi.nlm.nih.gov/pubmed/36293170
http://dx.doi.org/10.3390/ijms232012317
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author Ozu, Marcelo
Alvear-Arias, Juan José
Fernandez, Miguel
Caviglia, Agustín
Peña-Pichicoi, Antonio
Carrillo, Christian
Carmona, Emerson
Otero-Gonzalez, Anselmo
Garate, José Antonio
Amodeo, Gabriela
Gonzalez, Carlos
author_facet Ozu, Marcelo
Alvear-Arias, Juan José
Fernandez, Miguel
Caviglia, Agustín
Peña-Pichicoi, Antonio
Carrillo, Christian
Carmona, Emerson
Otero-Gonzalez, Anselmo
Garate, José Antonio
Amodeo, Gabriela
Gonzalez, Carlos
author_sort Ozu, Marcelo
collection PubMed
description Aquaporins (AQPs) are small transmembrane tetrameric proteins that facilitate water, solute and gas exchange. Their presence has been extensively reported in the biological membranes of almost all living organisms. Although their discovery is much more recent than ion transport systems, different biophysical approaches have contributed to confirm that permeation through each monomer is consistent with closed and open states, introducing the term gating mechanism into the field. The study of AQPs in their native membrane or overexpressed in heterologous systems have experimentally demonstrated that water membrane permeability can be reversibly modified in response to specific modulators. For some regulation mechanisms, such as pH changes, evidence for gating is also supported by high-resolution structures of the water channel in different configurations as well as molecular dynamics simulation. Both experimental and simulation approaches sustain that the rearrangement of conserved residues contributes to occlude the cavity of the channel restricting water permeation. Interestingly, specific charged and conserved residues are present in the environment of the pore and, thus, the tetrameric structure can be subjected to alter the positions of these charges to sustain gating. Thus, is it possible to explore whether the displacement of these charges (gating current) leads to conformational changes? To our knowledge, this question has not yet been addressed at all. In this review, we intend to analyze the suitability of this proposal for the first time.
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spelling pubmed-96041032022-10-27 Aquaporin Gating: A New Twist to Unravel Permeation through Water Channels Ozu, Marcelo Alvear-Arias, Juan José Fernandez, Miguel Caviglia, Agustín Peña-Pichicoi, Antonio Carrillo, Christian Carmona, Emerson Otero-Gonzalez, Anselmo Garate, José Antonio Amodeo, Gabriela Gonzalez, Carlos Int J Mol Sci Review Aquaporins (AQPs) are small transmembrane tetrameric proteins that facilitate water, solute and gas exchange. Their presence has been extensively reported in the biological membranes of almost all living organisms. Although their discovery is much more recent than ion transport systems, different biophysical approaches have contributed to confirm that permeation through each monomer is consistent with closed and open states, introducing the term gating mechanism into the field. The study of AQPs in their native membrane or overexpressed in heterologous systems have experimentally demonstrated that water membrane permeability can be reversibly modified in response to specific modulators. For some regulation mechanisms, such as pH changes, evidence for gating is also supported by high-resolution structures of the water channel in different configurations as well as molecular dynamics simulation. Both experimental and simulation approaches sustain that the rearrangement of conserved residues contributes to occlude the cavity of the channel restricting water permeation. Interestingly, specific charged and conserved residues are present in the environment of the pore and, thus, the tetrameric structure can be subjected to alter the positions of these charges to sustain gating. Thus, is it possible to explore whether the displacement of these charges (gating current) leads to conformational changes? To our knowledge, this question has not yet been addressed at all. In this review, we intend to analyze the suitability of this proposal for the first time. MDPI 2022-10-14 /pmc/articles/PMC9604103/ /pubmed/36293170 http://dx.doi.org/10.3390/ijms232012317 Text en © 2022 by the authors. https://creativecommons.org/licenses/by/4.0/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 (https://creativecommons.org/licenses/by/4.0/).
spellingShingle Review
Ozu, Marcelo
Alvear-Arias, Juan José
Fernandez, Miguel
Caviglia, Agustín
Peña-Pichicoi, Antonio
Carrillo, Christian
Carmona, Emerson
Otero-Gonzalez, Anselmo
Garate, José Antonio
Amodeo, Gabriela
Gonzalez, Carlos
Aquaporin Gating: A New Twist to Unravel Permeation through Water Channels
title Aquaporin Gating: A New Twist to Unravel Permeation through Water Channels
title_full Aquaporin Gating: A New Twist to Unravel Permeation through Water Channels
title_fullStr Aquaporin Gating: A New Twist to Unravel Permeation through Water Channels
title_full_unstemmed Aquaporin Gating: A New Twist to Unravel Permeation through Water Channels
title_short Aquaporin Gating: A New Twist to Unravel Permeation through Water Channels
title_sort aquaporin gating: a new twist to unravel permeation through water channels
topic Review
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9604103/
https://www.ncbi.nlm.nih.gov/pubmed/36293170
http://dx.doi.org/10.3390/ijms232012317
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