Heteromerization of PIP aquaporins affects their intrinsic permeability
The plant aquaporin plasma membrane intrinsic proteins (PIP) subfamily represents one of the main gateways for water exchange at the plasma membrane (PM). A fraction of this subfamily, known as PIP1, does not reach the PM unless they are coexpressed with a PIP2 aquaporin. Although ubiquitous and abu...
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paper:paper_00278424_v111_n1_p231_Yaneff2023-06-08T14:54:30Z Heteromerization of PIP aquaporins affects their intrinsic permeability Sigaut, Lorena aquaporin membrane protein plasma membrane intrinsic protein 1 plasma membrane intrinsic protein 2 unclassified drug acidification article cell membrane channel gating mathematical model membrane permeability molecular dynamics permeability pH priority journal protein expression protein function protein interaction protein transport regulatory mechanism strawberry water flow water permeability Animals Aquaporins Bacterial Proteins Cell Membrane Cytosol Fragaria Gene Expression Regulation, Plant Hydrogen-Ion Concentration Lipid Bilayers Luminescent Proteins Microscopy, Confocal Models, Theoretical Mutagenesis, Site-Directed Oocytes Permeability Plant Proteins Protein Multimerization RNA, Complementary Water Xenopus laevis The plant aquaporin plasma membrane intrinsic proteins (PIP) subfamily represents one of the main gateways for water exchange at the plasma membrane (PM). A fraction of this subfamily, known as PIP1, does not reach the PM unless they are coexpressed with a PIP2 aquaporin. Although ubiquitous and abundantly expressed, the role and properties of PIP1 aquaporins have therefore remained masked. Here, we unravel how FaPIP1;1, a fruit-specific PIP1 aquaporin from Fragaria x ananassa, contributes to the modulation of membrane water permeability (Pf) and pH aquaporin regulation. Our approach was to combine an experimental and mathematical model design to test its activity without affecting its trafficking dynamics. We demonstrate that FaPIP1;1 has a high water channel activity when coexpressed as well as how PIP1-PIP2 affects gating sensitivity in terms of cytosolic acidification. PIP1-PIP2 random heterotetramerization not only allows FaPIP1;1 to arrive at the PMbut also produces an enhancement of FaPIP2;1 activity. In this context, we propose that FaPIP1;1 is a key participant in the regulation of water movement across the membranes of cells expressing both aquaporins. Fil:Sigaut, L. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. 2014 https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00278424_v111_n1_p231_Yaneff http://hdl.handle.net/20.500.12110/paper_00278424_v111_n1_p231_Yaneff |
| institution |
Universidad de Buenos Aires |
| institution_str |
I-28 |
| repository_str |
R-134 |
| collection |
Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) |
| topic |
aquaporin membrane protein plasma membrane intrinsic protein 1 plasma membrane intrinsic protein 2 unclassified drug acidification article cell membrane channel gating mathematical model membrane permeability molecular dynamics permeability pH priority journal protein expression protein function protein interaction protein transport regulatory mechanism strawberry water flow water permeability Animals Aquaporins Bacterial Proteins Cell Membrane Cytosol Fragaria Gene Expression Regulation, Plant Hydrogen-Ion Concentration Lipid Bilayers Luminescent Proteins Microscopy, Confocal Models, Theoretical Mutagenesis, Site-Directed Oocytes Permeability Plant Proteins Protein Multimerization RNA, Complementary Water Xenopus laevis |
| spellingShingle |
aquaporin membrane protein plasma membrane intrinsic protein 1 plasma membrane intrinsic protein 2 unclassified drug acidification article cell membrane channel gating mathematical model membrane permeability molecular dynamics permeability pH priority journal protein expression protein function protein interaction protein transport regulatory mechanism strawberry water flow water permeability Animals Aquaporins Bacterial Proteins Cell Membrane Cytosol Fragaria Gene Expression Regulation, Plant Hydrogen-Ion Concentration Lipid Bilayers Luminescent Proteins Microscopy, Confocal Models, Theoretical Mutagenesis, Site-Directed Oocytes Permeability Plant Proteins Protein Multimerization RNA, Complementary Water Xenopus laevis Sigaut, Lorena Heteromerization of PIP aquaporins affects their intrinsic permeability |
| topic_facet |
aquaporin membrane protein plasma membrane intrinsic protein 1 plasma membrane intrinsic protein 2 unclassified drug acidification article cell membrane channel gating mathematical model membrane permeability molecular dynamics permeability pH priority journal protein expression protein function protein interaction protein transport regulatory mechanism strawberry water flow water permeability Animals Aquaporins Bacterial Proteins Cell Membrane Cytosol Fragaria Gene Expression Regulation, Plant Hydrogen-Ion Concentration Lipid Bilayers Luminescent Proteins Microscopy, Confocal Models, Theoretical Mutagenesis, Site-Directed Oocytes Permeability Plant Proteins Protein Multimerization RNA, Complementary Water Xenopus laevis |
| description |
The plant aquaporin plasma membrane intrinsic proteins (PIP) subfamily represents one of the main gateways for water exchange at the plasma membrane (PM). A fraction of this subfamily, known as PIP1, does not reach the PM unless they are coexpressed with a PIP2 aquaporin. Although ubiquitous and abundantly expressed, the role and properties of PIP1 aquaporins have therefore remained masked. Here, we unravel how FaPIP1;1, a fruit-specific PIP1 aquaporin from Fragaria x ananassa, contributes to the modulation of membrane water permeability (Pf) and pH aquaporin regulation. Our approach was to combine an experimental and mathematical model design to test its activity without affecting its trafficking dynamics. We demonstrate that FaPIP1;1 has a high water channel activity when coexpressed as well as how PIP1-PIP2 affects gating sensitivity in terms of cytosolic acidification. PIP1-PIP2 random heterotetramerization not only allows FaPIP1;1 to arrive at the PMbut also produces an enhancement of FaPIP2;1 activity. In this context, we propose that FaPIP1;1 is a key participant in the regulation of water movement across the membranes of cells expressing both aquaporins. |
| author |
Sigaut, Lorena |
| author_facet |
Sigaut, Lorena |
| author_sort |
Sigaut, Lorena |
| title |
Heteromerization of PIP aquaporins affects their intrinsic permeability |
| title_short |
Heteromerization of PIP aquaporins affects their intrinsic permeability |
| title_full |
Heteromerization of PIP aquaporins affects their intrinsic permeability |
| title_fullStr |
Heteromerization of PIP aquaporins affects their intrinsic permeability |
| title_full_unstemmed |
Heteromerization of PIP aquaporins affects their intrinsic permeability |
| title_sort |
heteromerization of pip aquaporins affects their intrinsic permeability |
| publishDate |
2014 |
| url |
https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00278424_v111_n1_p231_Yaneff http://hdl.handle.net/20.500.12110/paper_00278424_v111_n1_p231_Yaneff |
| work_keys_str_mv |
AT sigautlorena heteromerizationofpipaquaporinsaffectstheirintrinsicpermeability |
| _version_ |
1768543359248367616 |