Loop A Is Critical for the Functional Interaction of Two Beta vulgaris PIP Aquaporins

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Research done in the last years strongly support the hypothesis that PIP aquaporin can form heterooligomeric assemblies, specially combining PIP2 monomers with PIP1 monomers. Nevertheless, the structural elements involved in the ruling of homo versus heterooligomeric organization are not completely...

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Autores principales:	Jozefkowicz, C., Rosi, P., Sigaut, L., Soto, G., Pietrasanta, L.I., Amodeo, G., Alleva, K.
Formato:	JOUR
Materias:	aquaporin complementary RNA article beet cell membrane confocal microscopy controlled study dose response molecular dynamics mutagenesis nonhuman nucleotide sequence oocyte pH phylogeny protein content protein expression protein function protein localization protein protein interaction RNA synthesis sequence analysis water permeability water transport Amino Acid Sequence Animals Aquaporins Beta vulgaris Cell Membrane Permeability Conserved Sequence Hydrogen-Ion Concentration Molecular Dynamics Simulation Molecular Sequence Data Mutant Proteins Osmosis Plant Proteins Protein Binding Protein Structure, Secondary Recombinant Proteins Structure-Activity Relationship Xenopus laevis
Acceso en línea:	http://hdl.handle.net/20.500.12110/paper_19326203_v8_n3_p_Jozefkowicz
Aporte de:	Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) de Universidad de Buenos Aires

id	todo:paper_19326203_v8_n3_p_Jozefkowicz
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spelling	todo:paper_19326203_v8_n3_p_Jozefkowicz2023-10-03T16:35:31Z Loop A Is Critical for the Functional Interaction of Two Beta vulgaris PIP Aquaporins Jozefkowicz, C. Rosi, P. Sigaut, L. Soto, G. Pietrasanta, L.I. Amodeo, G. Alleva, K. aquaporin complementary RNA article beet cell membrane confocal microscopy controlled study dose response molecular dynamics mutagenesis nonhuman nucleotide sequence oocyte pH phylogeny protein content protein expression protein function protein localization protein protein interaction RNA synthesis sequence analysis water permeability water transport Amino Acid Sequence Animals Aquaporins Beta vulgaris Cell Membrane Permeability Conserved Sequence Hydrogen-Ion Concentration Molecular Dynamics Simulation Molecular Sequence Data Mutant Proteins Osmosis Plant Proteins Protein Binding Protein Structure, Secondary Recombinant Proteins Structure-Activity Relationship Xenopus laevis Research done in the last years strongly support the hypothesis that PIP aquaporin can form heterooligomeric assemblies, specially combining PIP2 monomers with PIP1 monomers. Nevertheless, the structural elements involved in the ruling of homo versus heterooligomeric organization are not completely elucidated. In this work we unveil some features of monomer-monomer interaction in Beta vulgaris PIP aquaporins. Our results show that while BvPIP2;2 is able to interact with BvPIP1;1, BvPIP2;1 shows no functional interaction. The lack of functional interaction between BvPIP2;1 and BvPIP1;1 was further corroborated by dose-response curves of water permeability due to aquaporin activity exposed to different acidic conditions. We also found that BvPIP2;1 is unable to translocate BvPIP1;1-ECFP from an intracellular position to the plasma membrane when co-expressed, as BvPIP2;2 does. Moreover we postulate that the first extracellular loop (loop A) of BvPIP2;1, could be relevant for the functional interaction with BvPIP1;1. Thus, we investigate BvPIP2;1 loop A at an atomic level by Molecular Dynamics Simulation (MDS) and by direct mutagenesis. We found that, within the tetramer, each loop A presents a dissimilar behavior. Besides, BvPIP2;1 loop A mutants restore functional interaction with BvPIP1;1. This work is a contribution to unravel how PIP2 and PIP1 interact to form functional heterooligomeric assemblies. We postulate that BvPIP2;1 loop A is relevant for the lack of functional interaction with BvPIP1;1 and that the monomer composition of PIP assemblies determines their functional properties. © 2013 Jozefkowicz et al. Fil:Rosi, P. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Sigaut, L. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Soto, G. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. JOUR info:eu-repo/semantics/openAccess http://creativecommons.org/licenses/by/2.5/ar http://hdl.handle.net/20.500.12110/paper_19326203_v8_n3_p_Jozefkowicz
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 complementary RNA article beet cell membrane confocal microscopy controlled study dose response molecular dynamics mutagenesis nonhuman nucleotide sequence oocyte pH phylogeny protein content protein expression protein function protein localization protein protein interaction RNA synthesis sequence analysis water permeability water transport Amino Acid Sequence Animals Aquaporins Beta vulgaris Cell Membrane Permeability Conserved Sequence Hydrogen-Ion Concentration Molecular Dynamics Simulation Molecular Sequence Data Mutant Proteins Osmosis Plant Proteins Protein Binding Protein Structure, Secondary Recombinant Proteins Structure-Activity Relationship Xenopus laevis
spellingShingle	aquaporin complementary RNA article beet cell membrane confocal microscopy controlled study dose response molecular dynamics mutagenesis nonhuman nucleotide sequence oocyte pH phylogeny protein content protein expression protein function protein localization protein protein interaction RNA synthesis sequence analysis water permeability water transport Amino Acid Sequence Animals Aquaporins Beta vulgaris Cell Membrane Permeability Conserved Sequence Hydrogen-Ion Concentration Molecular Dynamics Simulation Molecular Sequence Data Mutant Proteins Osmosis Plant Proteins Protein Binding Protein Structure, Secondary Recombinant Proteins Structure-Activity Relationship Xenopus laevis Jozefkowicz, C. Rosi, P. Sigaut, L. Soto, G. Pietrasanta, L.I. Amodeo, G. Alleva, K. Loop A Is Critical for the Functional Interaction of Two Beta vulgaris PIP Aquaporins
topic_facet	aquaporin complementary RNA article beet cell membrane confocal microscopy controlled study dose response molecular dynamics mutagenesis nonhuman nucleotide sequence oocyte pH phylogeny protein content protein expression protein function protein localization protein protein interaction RNA synthesis sequence analysis water permeability water transport Amino Acid Sequence Animals Aquaporins Beta vulgaris Cell Membrane Permeability Conserved Sequence Hydrogen-Ion Concentration Molecular Dynamics Simulation Molecular Sequence Data Mutant Proteins Osmosis Plant Proteins Protein Binding Protein Structure, Secondary Recombinant Proteins Structure-Activity Relationship Xenopus laevis
description	Research done in the last years strongly support the hypothesis that PIP aquaporin can form heterooligomeric assemblies, specially combining PIP2 monomers with PIP1 monomers. Nevertheless, the structural elements involved in the ruling of homo versus heterooligomeric organization are not completely elucidated. In this work we unveil some features of monomer-monomer interaction in Beta vulgaris PIP aquaporins. Our results show that while BvPIP2;2 is able to interact with BvPIP1;1, BvPIP2;1 shows no functional interaction. The lack of functional interaction between BvPIP2;1 and BvPIP1;1 was further corroborated by dose-response curves of water permeability due to aquaporin activity exposed to different acidic conditions. We also found that BvPIP2;1 is unable to translocate BvPIP1;1-ECFP from an intracellular position to the plasma membrane when co-expressed, as BvPIP2;2 does. Moreover we postulate that the first extracellular loop (loop A) of BvPIP2;1, could be relevant for the functional interaction with BvPIP1;1. Thus, we investigate BvPIP2;1 loop A at an atomic level by Molecular Dynamics Simulation (MDS) and by direct mutagenesis. We found that, within the tetramer, each loop A presents a dissimilar behavior. Besides, BvPIP2;1 loop A mutants restore functional interaction with BvPIP1;1. This work is a contribution to unravel how PIP2 and PIP1 interact to form functional heterooligomeric assemblies. We postulate that BvPIP2;1 loop A is relevant for the lack of functional interaction with BvPIP1;1 and that the monomer composition of PIP assemblies determines their functional properties. © 2013 Jozefkowicz et al.
format	JOUR
author	Jozefkowicz, C. Rosi, P. Sigaut, L. Soto, G. Pietrasanta, L.I. Amodeo, G. Alleva, K.
author_facet	Jozefkowicz, C. Rosi, P. Sigaut, L. Soto, G. Pietrasanta, L.I. Amodeo, G. Alleva, K.
author_sort	Jozefkowicz, C.
title	Loop A Is Critical for the Functional Interaction of Two Beta vulgaris PIP Aquaporins
title_short	Loop A Is Critical for the Functional Interaction of Two Beta vulgaris PIP Aquaporins
title_full	Loop A Is Critical for the Functional Interaction of Two Beta vulgaris PIP Aquaporins
title_fullStr	Loop A Is Critical for the Functional Interaction of Two Beta vulgaris PIP Aquaporins
title_full_unstemmed	Loop A Is Critical for the Functional Interaction of Two Beta vulgaris PIP Aquaporins
title_sort	loop a is critical for the functional interaction of two beta vulgaris pip aquaporins
url	http://hdl.handle.net/20.500.12110/paper_19326203_v8_n3_p_Jozefkowicz
work_keys_str_mv	AT jozefkowiczc loopaiscriticalforthefunctionalinteractionoftwobetavulgarispipaquaporins AT rosip loopaiscriticalforthefunctionalinteractionoftwobetavulgarispipaquaporins AT sigautl loopaiscriticalforthefunctionalinteractionoftwobetavulgarispipaquaporins AT sotog loopaiscriticalforthefunctionalinteractionoftwobetavulgarispipaquaporins AT pietrasantali loopaiscriticalforthefunctionalinteractionoftwobetavulgarispipaquaporins AT amodeog loopaiscriticalforthefunctionalinteractionoftwobetavulgarispipaquaporins AT allevak loopaiscriticalforthefunctionalinteractionoftwobetavulgarispipaquaporins
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Loop A Is Critical for the Functional Interaction of Two Beta vulgaris PIP Aquaporins

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