Plant and animal aquaporins crosstalk: what can be revealed from distinct perspectives
Aquaporins (AQPs) can be revisited from a distinct and complementary perspective: the outcome from analyzing them from both plant and animal studies. (1) The approach in the study. Diversity found in both kingdoms contrasts with the limited number of crystal structures determined within each group....
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2017
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| Acceso en línea: | https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_18672450_v9_n5_p545_Sutka http://hdl.handle.net/20.500.12110/paper_18672450_v9_n5_p545_Sutka |
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paper:paper_18672450_v9_n5_p545_Sutka2023-06-08T16:29:52Z Plant and animal aquaporins crosstalk: what can be revealed from distinct perspectives Aquaporins Diversity Gases Osmosensor Solutes aquaglyceroporin aquaporin aquaporin 1 aquaporin 10 aquaporin 11 aquaporin 12 aquaporin 2 aquaporin 3 aquaporin 4 aquaporin 5 aquaporin 6 aquaporin 7 aquaporin 8 aquaporin 9 arginine carbon dioxide epidermal growth factor GlpF like intrinsic protein glycerol transporter hybrid intrinsic protein hydrogen peroxide hydroxyl radical nodulin 26 like intrinsic protein plasma membrane intrinsic protein small basic intrinsic protein superoxide tonoplast intrinsic protein uncategorized intrinsic protein unclassified drug unindexed drug vasopressin crystal structure development drug screening gas transport growth homeostasis and regulation human hydraulic conductivity nonhuman pH priority journal protein expression protein localization regulatory mechanism Review stress water transport Aquaporins (AQPs) can be revisited from a distinct and complementary perspective: the outcome from analyzing them from both plant and animal studies. (1) The approach in the study. Diversity found in both kingdoms contrasts with the limited number of crystal structures determined within each group. While the structure of almost half of mammal AQPs was resolved, only a few were resolved in plants. Strikingly, the animal structures resolved are mainly derived from the AQP2-lineage, due to their important roles in water homeostasis regulation in humans. The difference could be attributed to the approach: relevance in animal research is emphasized on pathology and in consequence drug screening that can lead to potential inhibitors, enhancers and/or regulators. By contrast, studies on plants have been mainly focused on the physiological role that AQPs play in growth, development and stress tolerance. (2) The transport capacity. Besides the well-described AQPs with high water transport capacity, large amount of evidence confirms that certain plant AQPs can carry a large list of small solutes. So far, animal AQP list is more restricted. In both kingdoms, there is a great amount of evidence on gas transport, although there is still an unsolved controversy around gas translocation as well as the role of the central pore of the tetramer. (3) More roles than expected. We found it remarkable that the view of AQPs as specific channels has evolved first toward simple transporters to molecules that can experience conformational changes triggered by biochemical and/or mechanical signals, turning them also into signaling components and/or behave as osmosensor molecules. © 2017, International Union for Pure and Applied Biophysics (IUPAB) and Springer-Verlag GmbH Germany. 2017 https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_18672450_v9_n5_p545_Sutka http://hdl.handle.net/20.500.12110/paper_18672450_v9_n5_p545_Sutka |
| institution |
Universidad de Buenos Aires |
| institution_str |
I-28 |
| repository_str |
R-134 |
| collection |
Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) |
| topic |
Aquaporins Diversity Gases Osmosensor Solutes aquaglyceroporin aquaporin aquaporin 1 aquaporin 10 aquaporin 11 aquaporin 12 aquaporin 2 aquaporin 3 aquaporin 4 aquaporin 5 aquaporin 6 aquaporin 7 aquaporin 8 aquaporin 9 arginine carbon dioxide epidermal growth factor GlpF like intrinsic protein glycerol transporter hybrid intrinsic protein hydrogen peroxide hydroxyl radical nodulin 26 like intrinsic protein plasma membrane intrinsic protein small basic intrinsic protein superoxide tonoplast intrinsic protein uncategorized intrinsic protein unclassified drug unindexed drug vasopressin crystal structure development drug screening gas transport growth homeostasis and regulation human hydraulic conductivity nonhuman pH priority journal protein expression protein localization regulatory mechanism Review stress water transport |
| spellingShingle |
Aquaporins Diversity Gases Osmosensor Solutes aquaglyceroporin aquaporin aquaporin 1 aquaporin 10 aquaporin 11 aquaporin 12 aquaporin 2 aquaporin 3 aquaporin 4 aquaporin 5 aquaporin 6 aquaporin 7 aquaporin 8 aquaporin 9 arginine carbon dioxide epidermal growth factor GlpF like intrinsic protein glycerol transporter hybrid intrinsic protein hydrogen peroxide hydroxyl radical nodulin 26 like intrinsic protein plasma membrane intrinsic protein small basic intrinsic protein superoxide tonoplast intrinsic protein uncategorized intrinsic protein unclassified drug unindexed drug vasopressin crystal structure development drug screening gas transport growth homeostasis and regulation human hydraulic conductivity nonhuman pH priority journal protein expression protein localization regulatory mechanism Review stress water transport Plant and animal aquaporins crosstalk: what can be revealed from distinct perspectives |
| topic_facet |
Aquaporins Diversity Gases Osmosensor Solutes aquaglyceroporin aquaporin aquaporin 1 aquaporin 10 aquaporin 11 aquaporin 12 aquaporin 2 aquaporin 3 aquaporin 4 aquaporin 5 aquaporin 6 aquaporin 7 aquaporin 8 aquaporin 9 arginine carbon dioxide epidermal growth factor GlpF like intrinsic protein glycerol transporter hybrid intrinsic protein hydrogen peroxide hydroxyl radical nodulin 26 like intrinsic protein plasma membrane intrinsic protein small basic intrinsic protein superoxide tonoplast intrinsic protein uncategorized intrinsic protein unclassified drug unindexed drug vasopressin crystal structure development drug screening gas transport growth homeostasis and regulation human hydraulic conductivity nonhuman pH priority journal protein expression protein localization regulatory mechanism Review stress water transport |
| description |
Aquaporins (AQPs) can be revisited from a distinct and complementary perspective: the outcome from analyzing them from both plant and animal studies. (1) The approach in the study. Diversity found in both kingdoms contrasts with the limited number of crystal structures determined within each group. While the structure of almost half of mammal AQPs was resolved, only a few were resolved in plants. Strikingly, the animal structures resolved are mainly derived from the AQP2-lineage, due to their important roles in water homeostasis regulation in humans. The difference could be attributed to the approach: relevance in animal research is emphasized on pathology and in consequence drug screening that can lead to potential inhibitors, enhancers and/or regulators. By contrast, studies on plants have been mainly focused on the physiological role that AQPs play in growth, development and stress tolerance. (2) The transport capacity. Besides the well-described AQPs with high water transport capacity, large amount of evidence confirms that certain plant AQPs can carry a large list of small solutes. So far, animal AQP list is more restricted. In both kingdoms, there is a great amount of evidence on gas transport, although there is still an unsolved controversy around gas translocation as well as the role of the central pore of the tetramer. (3) More roles than expected. We found it remarkable that the view of AQPs as specific channels has evolved first toward simple transporters to molecules that can experience conformational changes triggered by biochemical and/or mechanical signals, turning them also into signaling components and/or behave as osmosensor molecules. © 2017, International Union for Pure and Applied Biophysics (IUPAB) and Springer-Verlag GmbH Germany. |
| title |
Plant and animal aquaporins crosstalk: what can be revealed from distinct perspectives |
| title_short |
Plant and animal aquaporins crosstalk: what can be revealed from distinct perspectives |
| title_full |
Plant and animal aquaporins crosstalk: what can be revealed from distinct perspectives |
| title_fullStr |
Plant and animal aquaporins crosstalk: what can be revealed from distinct perspectives |
| title_full_unstemmed |
Plant and animal aquaporins crosstalk: what can be revealed from distinct perspectives |
| title_sort |
plant and animal aquaporins crosstalk: what can be revealed from distinct perspectives |
| publishDate |
2017 |
| url |
https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_18672450_v9_n5_p545_Sutka http://hdl.handle.net/20.500.12110/paper_18672450_v9_n5_p545_Sutka |
| _version_ |
1768546743275749376 |