Heteromerization of PIP aquaporins affects their intrinsic permeability

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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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Autores principales:	Yaneff, A., Sigaut, L., Marquez, M., Alleva, K., Pietrasanta, L.I., Amodeo, G.
Formato:	Artículo publishedVersion
Publicado:	2014
Materias:	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
Acceso en línea:	http://hdl.handle.net/20.500.12110/paper_00278424_v111_n1_p231_Yaneff https://repositoriouba.sisbi.uba.ar/gsdl/cgi-bin/library.cgi?a=d&c=artiaex&d=paper_00278424_v111_n1_p231_Yaneff_oai
Aporte de:	Repositorio Digital de la Universidad de Buenos Aires (UBA) de Universidad de Buenos Aires

id	I28-R145-paper_00278424_v111_n1_p231_Yaneff_oai
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spelling	I28-R145-paper_00278424_v111_n1_p231_Yaneff_oai2024-08-16 Yaneff, A. Sigaut, L. Marquez, M. Alleva, K. Pietrasanta, L.I. Amodeo, G. 2014 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. application/pdf http://hdl.handle.net/20.500.12110/paper_00278424_v111_n1_p231_Yaneff info:eu-repo/semantics/openAccess http://creativecommons.org/licenses/by/2.5/ar Proc. Natl. Acad. Sci. U. S. A. 2014;111(1):231-236 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 Heteromerization of PIP aquaporins affects their intrinsic permeability info:eu-repo/semantics/article info:ar-repo/semantics/artículo info:eu-repo/semantics/publishedVersion https://repositoriouba.sisbi.uba.ar/gsdl/cgi-bin/library.cgi?a=d&c=artiaex&d=paper_00278424_v111_n1_p231_Yaneff_oai
institution	Universidad de Buenos Aires
institution_str	I-28
repository_str	R-145
collection	Repositorio Digital de la Universidad de Buenos Aires (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 Yaneff, A. Sigaut, L. Marquez, M. Alleva, K. Pietrasanta, L.I. Amodeo, G. 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.
format	Artículo Artículo publishedVersion
author	Yaneff, A. Sigaut, L. Marquez, M. Alleva, K. Pietrasanta, L.I. Amodeo, G.
author_facet	Yaneff, A. Sigaut, L. Marquez, M. Alleva, K. Pietrasanta, L.I. Amodeo, G.
author_sort	Yaneff, A.
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	http://hdl.handle.net/20.500.12110/paper_00278424_v111_n1_p231_Yaneff https://repositoriouba.sisbi.uba.ar/gsdl/cgi-bin/library.cgi?a=d&c=artiaex&d=paper_00278424_v111_n1_p231_Yaneff_oai
work_keys_str_mv	AT yaneffa heteromerizationofpipaquaporinsaffectstheirintrinsicpermeability AT sigautl heteromerizationofpipaquaporinsaffectstheirintrinsicpermeability AT marquezm heteromerizationofpipaquaporinsaffectstheirintrinsicpermeability AT allevak heteromerizationofpipaquaporinsaffectstheirintrinsicpermeability AT pietrasantali heteromerizationofpipaquaporinsaffectstheirintrinsicpermeability AT amodeog heteromerizationofpipaquaporinsaffectstheirintrinsicpermeability
_version_	1809357080568528896

Heteromerization of PIP aquaporins affects their intrinsic permeability

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