Aquaporins: More Than Functional Monomers in a Tetrameric Arrangement
Aquaporins (AQPs) function as tetrameric structures in which each monomer has its own permeable pathway. The combination of structural biology, molecular dynamics simulations, and experimental approaches has contributed to improve our knowledge of how protein conformational changes can challenge its...
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| Format: | Article |
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MDPI AG
2018-11-01
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| Series: | Cells |
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| Online Access: | https://www.mdpi.com/2073-4409/7/11/209 |
| _version_ | 1797721100009865216 |
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| author | Marcelo Ozu Luciano Galizia Cynthia Acuña Gabriela Amodeo |
| author_facet | Marcelo Ozu Luciano Galizia Cynthia Acuña Gabriela Amodeo |
| author_sort | Marcelo Ozu |
| collection | DOAJ |
| description | Aquaporins (AQPs) function as tetrameric structures in which each monomer has its own permeable pathway. The combination of structural biology, molecular dynamics simulations, and experimental approaches has contributed to improve our knowledge of how protein conformational changes can challenge its transport capacity, rapidly altering the membrane permeability. This review is focused on evidence that highlights the functional relationship between the monomers and the tetramer. In this sense, we address AQP permeation capacity as well as regulatory mechanisms that affect the monomer, the tetramer, or tetramers combined in complex structures. We therefore explore: (i) water permeation and recent evidence on ion permeation, including the permeation pathway controversy—each monomer versus the central pore of the tetramer—and (ii) regulatory mechanisms that cannot be attributed to independent monomers. In particular, we discuss channel gating and AQPs that sense membrane tension. For the latter we propose a possible mechanism that includes the monomer (slight changes of pore shape, the number of possible H-bonds between water molecules and pore-lining residues) and the tetramer (interactions among monomers and a positive cooperative effect). |
| first_indexed | 2024-03-12T09:28:47Z |
| format | Article |
| id | doaj.art-f564c1187f3c4d26a345c0487453cdb4 |
| institution | Directory Open Access Journal |
| issn | 2073-4409 |
| language | English |
| last_indexed | 2024-03-12T09:28:47Z |
| publishDate | 2018-11-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | Cells |
| spelling | doaj.art-f564c1187f3c4d26a345c0487453cdb42023-09-02T14:02:24ZengMDPI AGCells2073-44092018-11-0171120910.3390/cells7110209cells7110209Aquaporins: More Than Functional Monomers in a Tetrameric ArrangementMarcelo Ozu0Luciano Galizia1Cynthia Acuña2Gabriela Amodeo3Departamento de Biodiversidad y Biología Experimental, Facultad de Ciencias Exactas y Naturales, Universidad de Buenos Aires, Buenos Aires C1428EGA, ArgentinaInstituto de investigaciones Médicas A. Lanari, Facultad de Medicina, Universidad de Buenos Aires, Buenos Aires C1427ARO, ArgentinaDepartamento de Biodiversidad y Biología Experimental, Facultad de Ciencias Exactas y Naturales, Universidad de Buenos Aires, Buenos Aires C1428EGA, ArgentinaDepartamento de Biodiversidad y Biología Experimental, Facultad de Ciencias Exactas y Naturales, Universidad de Buenos Aires, Buenos Aires C1428EGA, ArgentinaAquaporins (AQPs) function as tetrameric structures in which each monomer has its own permeable pathway. The combination of structural biology, molecular dynamics simulations, and experimental approaches has contributed to improve our knowledge of how protein conformational changes can challenge its transport capacity, rapidly altering the membrane permeability. This review is focused on evidence that highlights the functional relationship between the monomers and the tetramer. In this sense, we address AQP permeation capacity as well as regulatory mechanisms that affect the monomer, the tetramer, or tetramers combined in complex structures. We therefore explore: (i) water permeation and recent evidence on ion permeation, including the permeation pathway controversy—each monomer versus the central pore of the tetramer—and (ii) regulatory mechanisms that cannot be attributed to independent monomers. In particular, we discuss channel gating and AQPs that sense membrane tension. For the latter we propose a possible mechanism that includes the monomer (slight changes of pore shape, the number of possible H-bonds between water molecules and pore-lining residues) and the tetramer (interactions among monomers and a positive cooperative effect).https://www.mdpi.com/2073-4409/7/11/209water channelosmotic permeabilitygatingcooperative mechanism |
| spellingShingle | Marcelo Ozu Luciano Galizia Cynthia Acuña Gabriela Amodeo Aquaporins: More Than Functional Monomers in a Tetrameric Arrangement Cells water channel osmotic permeability gating cooperative mechanism |
| title | Aquaporins: More Than Functional Monomers in a Tetrameric Arrangement |
| title_full | Aquaporins: More Than Functional Monomers in a Tetrameric Arrangement |
| title_fullStr | Aquaporins: More Than Functional Monomers in a Tetrameric Arrangement |
| title_full_unstemmed | Aquaporins: More Than Functional Monomers in a Tetrameric Arrangement |
| title_short | Aquaporins: More Than Functional Monomers in a Tetrameric Arrangement |
| title_sort | aquaporins more than functional monomers in a tetrameric arrangement |
| topic | water channel osmotic permeability gating cooperative mechanism |
| url | https://www.mdpi.com/2073-4409/7/11/209 |
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