Intracellular pH sensing is altered by plasma membrane PIP aquaporin co-expression

The plant plasma membrane barrier can express aquaporins (PIP1 and PIP2) that show two intriguing aspects: (1) the potential of modulating whole membrane water permeability by co-expression of both types, which have recently been distinguished for showing a different capacity to reach the plasma mem...

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Autor principal:	Soto, Gabriela Cynthia
Publicado:	2010
Materias:	Aquaporin gating Cytosolic acidification pH sensing Plasma membrane intrinsic proteins aquaporin plant DNA primer DNA recombinant protein vegetable protein water amino acid sequence animal article beet cell membrane permeability female gene expression genetics in vitro study intracellular fluid metabolism molecular genetics nucleotide sequence oocyte pH phylogeny plant gene plant root sequence homology Xenopus laevis Amino Acid Sequence Animals Aquaporins Base Sequence Beta vulgaris Cell Membrane Permeability DNA Primers DNA, Plant Female Gene Expression Genes, Plant Hydrogen-Ion Concentration Intracellular Fluid Molecular Sequence Data Oocytes Phylogeny Plant Proteins Plant Roots Recombinant Proteins Sequence Homology, Amino Acid Water Beta vulgaris subsp. vulgaris Pips
Acceso en línea:	https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_01674412_v74_n1_p105_Bellati http://hdl.handle.net/20.500.12110/paper_01674412_v74_n1_p105_Bellati
Aporte de:	Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) de Universidad de Buenos Aires

id	paper:paper_01674412_v74_n1_p105_Bellati
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spelling	paper:paper_01674412_v74_n1_p105_Bellati2023-06-08T15:16:22Z Intracellular pH sensing is altered by plasma membrane PIP aquaporin co-expression Soto, Gabriela Cynthia Aquaporin gating Cytosolic acidification pH sensing Plasma membrane intrinsic proteins aquaporin plant DNA primer DNA recombinant protein vegetable protein water amino acid sequence animal article beet cell membrane permeability female gene expression genetics in vitro study intracellular fluid metabolism molecular genetics nucleotide sequence oocyte pH phylogeny plant gene plant root sequence homology Xenopus laevis Amino Acid Sequence Animals Aquaporins Base Sequence Beta vulgaris Cell Membrane Permeability DNA Primers DNA, Plant Female Gene Expression Genes, Plant Hydrogen-Ion Concentration Intracellular Fluid Molecular Sequence Data Oocytes Phylogeny Plant Proteins Plant Roots Recombinant Proteins Sequence Homology, Amino Acid Water Xenopus laevis Beta vulgaris Beta vulgaris subsp. vulgaris Pips The plant plasma membrane barrier can express aquaporins (PIP1 and PIP2) that show two intriguing aspects: (1) the potential of modulating whole membrane water permeability by co-expression of both types, which have recently been distinguished for showing a different capacity to reach the plasma membrane; and (2) the faculty to reduce water permeation through the pore after cytosolic acidification, as a consequence of a gating process. Our working hypothesis is that these two key features might enhance plasticity of the membrane water transport capacity if they jointly trigger any cooperative interaction. In previous work, we proved by biophysical approaches that the plasma membrane of the halophyte Beta vulgaris storage root presents highly permeable aquaporins that can be shut down by acidic pH. Root Beta vulgaris PIPs were therefore subcloned and expressed in Xenopus oocytes. Co-expression of BvPIP1;1 and BvPIP2;2 not only enhances oocyte plasma membrane water permeability synergistically but also reinforces pH inhibitory response from partial to complete shut down after cytosolic pH acidification. This pH dependent behavior shows that PIP1-PIP2 co-expression accounts for a different pH sensitivity in comparison with PIP2 expression. These results prove for the first time that PIP co-expression modulates the membrane water permeability through a pH regulatory response, enhancing in this way membrane versatility to adjust its water transfer capacity. © 2010 Springer Science+Business Media B.V. Fil:Soto, G. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. 2010 https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_01674412_v74_n1_p105_Bellati http://hdl.handle.net/20.500.12110/paper_01674412_v74_n1_p105_Bellati
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 gating Cytosolic acidification pH sensing Plasma membrane intrinsic proteins aquaporin plant DNA primer DNA recombinant protein vegetable protein water amino acid sequence animal article beet cell membrane permeability female gene expression genetics in vitro study intracellular fluid metabolism molecular genetics nucleotide sequence oocyte pH phylogeny plant gene plant root sequence homology Xenopus laevis Amino Acid Sequence Animals Aquaporins Base Sequence Beta vulgaris Cell Membrane Permeability DNA Primers DNA, Plant Female Gene Expression Genes, Plant Hydrogen-Ion Concentration Intracellular Fluid Molecular Sequence Data Oocytes Phylogeny Plant Proteins Plant Roots Recombinant Proteins Sequence Homology, Amino Acid Water Xenopus laevis Beta vulgaris Beta vulgaris subsp. vulgaris Pips
spellingShingle	Aquaporin gating Cytosolic acidification pH sensing Plasma membrane intrinsic proteins aquaporin plant DNA primer DNA recombinant protein vegetable protein water amino acid sequence animal article beet cell membrane permeability female gene expression genetics in vitro study intracellular fluid metabolism molecular genetics nucleotide sequence oocyte pH phylogeny plant gene plant root sequence homology Xenopus laevis Amino Acid Sequence Animals Aquaporins Base Sequence Beta vulgaris Cell Membrane Permeability DNA Primers DNA, Plant Female Gene Expression Genes, Plant Hydrogen-Ion Concentration Intracellular Fluid Molecular Sequence Data Oocytes Phylogeny Plant Proteins Plant Roots Recombinant Proteins Sequence Homology, Amino Acid Water Xenopus laevis Beta vulgaris Beta vulgaris subsp. vulgaris Pips Soto, Gabriela Cynthia Intracellular pH sensing is altered by plasma membrane PIP aquaporin co-expression
topic_facet	Aquaporin gating Cytosolic acidification pH sensing Plasma membrane intrinsic proteins aquaporin plant DNA primer DNA recombinant protein vegetable protein water amino acid sequence animal article beet cell membrane permeability female gene expression genetics in vitro study intracellular fluid metabolism molecular genetics nucleotide sequence oocyte pH phylogeny plant gene plant root sequence homology Xenopus laevis Amino Acid Sequence Animals Aquaporins Base Sequence Beta vulgaris Cell Membrane Permeability DNA Primers DNA, Plant Female Gene Expression Genes, Plant Hydrogen-Ion Concentration Intracellular Fluid Molecular Sequence Data Oocytes Phylogeny Plant Proteins Plant Roots Recombinant Proteins Sequence Homology, Amino Acid Water Xenopus laevis Beta vulgaris Beta vulgaris subsp. vulgaris Pips
description	The plant plasma membrane barrier can express aquaporins (PIP1 and PIP2) that show two intriguing aspects: (1) the potential of modulating whole membrane water permeability by co-expression of both types, which have recently been distinguished for showing a different capacity to reach the plasma membrane; and (2) the faculty to reduce water permeation through the pore after cytosolic acidification, as a consequence of a gating process. Our working hypothesis is that these two key features might enhance plasticity of the membrane water transport capacity if they jointly trigger any cooperative interaction. In previous work, we proved by biophysical approaches that the plasma membrane of the halophyte Beta vulgaris storage root presents highly permeable aquaporins that can be shut down by acidic pH. Root Beta vulgaris PIPs were therefore subcloned and expressed in Xenopus oocytes. Co-expression of BvPIP1;1 and BvPIP2;2 not only enhances oocyte plasma membrane water permeability synergistically but also reinforces pH inhibitory response from partial to complete shut down after cytosolic pH acidification. This pH dependent behavior shows that PIP1-PIP2 co-expression accounts for a different pH sensitivity in comparison with PIP2 expression. These results prove for the first time that PIP co-expression modulates the membrane water permeability through a pH regulatory response, enhancing in this way membrane versatility to adjust its water transfer capacity. © 2010 Springer Science+Business Media B.V.
author	Soto, Gabriela Cynthia
author_facet	Soto, Gabriela Cynthia
author_sort	Soto, Gabriela Cynthia
title	Intracellular pH sensing is altered by plasma membrane PIP aquaporin co-expression
title_short	Intracellular pH sensing is altered by plasma membrane PIP aquaporin co-expression
title_full	Intracellular pH sensing is altered by plasma membrane PIP aquaporin co-expression
title_fullStr	Intracellular pH sensing is altered by plasma membrane PIP aquaporin co-expression
title_full_unstemmed	Intracellular pH sensing is altered by plasma membrane PIP aquaporin co-expression
title_sort	intracellular ph sensing is altered by plasma membrane pip aquaporin co-expression
publishDate	2010
url	https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_01674412_v74_n1_p105_Bellati http://hdl.handle.net/20.500.12110/paper_01674412_v74_n1_p105_Bellati
work_keys_str_mv	AT sotogabrielacynthia intracellularphsensingisalteredbyplasmamembranepipaquaporincoexpression
_version_	1768542733269467136

Intracellular pH sensing is altered by plasma membrane PIP aquaporin co-expression

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