Cargando…

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

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...

Descripción completa

Detalles Bibliográficos
Autores principales: Jozefkowicz, Cintia, Rosi, Pablo, Sigaut, Lorena, Soto, Gabriela, Pietrasanta, Lía Isabel, Amodeo, Gabriela, Alleva, Karina
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Public Library of Science 2013
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3587573/
https://www.ncbi.nlm.nih.gov/pubmed/23483963
http://dx.doi.org/10.1371/journal.pone.0057993
_version_ 1782261411399860224
author Jozefkowicz, Cintia
Rosi, Pablo
Sigaut, Lorena
Soto, Gabriela
Pietrasanta, Lía Isabel
Amodeo, Gabriela
Alleva, Karina
author_facet Jozefkowicz, Cintia
Rosi, Pablo
Sigaut, Lorena
Soto, Gabriela
Pietrasanta, Lía Isabel
Amodeo, Gabriela
Alleva, Karina
author_sort Jozefkowicz, Cintia
collection PubMed
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.
format Online
Article
Text
id pubmed-3587573
institution National Center for Biotechnology Information
language English
publishDate 2013
publisher Public Library of Science
record_format MEDLINE/PubMed
spelling pubmed-35875732013-03-12 Loop A Is Critical for the Functional Interaction of Two Beta vulgaris PIP Aquaporins Jozefkowicz, Cintia Rosi, Pablo Sigaut, Lorena Soto, Gabriela Pietrasanta, Lía Isabel Amodeo, Gabriela Alleva, Karina PLoS One Research Article 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. Public Library of Science 2013-03-04 /pmc/articles/PMC3587573/ /pubmed/23483963 http://dx.doi.org/10.1371/journal.pone.0057993 Text en © 2013 Jozefkowicz et al http://creativecommons.org/licenses/by/4.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are properly credited.
spellingShingle Research Article
Jozefkowicz, Cintia
Rosi, Pablo
Sigaut, Lorena
Soto, Gabriela
Pietrasanta, Lía Isabel
Amodeo, Gabriela
Alleva, Karina
Loop A Is Critical for the Functional Interaction of Two Beta vulgaris PIP Aquaporins
title 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_short 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
topic Research Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3587573/
https://www.ncbi.nlm.nih.gov/pubmed/23483963
http://dx.doi.org/10.1371/journal.pone.0057993
work_keys_str_mv AT jozefkowiczcintia loopaiscriticalforthefunctionalinteractionoftwobetavulgarispipaquaporins
AT rosipablo loopaiscriticalforthefunctionalinteractionoftwobetavulgarispipaquaporins
AT sigautlorena loopaiscriticalforthefunctionalinteractionoftwobetavulgarispipaquaporins
AT sotogabriela loopaiscriticalforthefunctionalinteractionoftwobetavulgarispipaquaporins
AT pietrasantaliaisabel loopaiscriticalforthefunctionalinteractionoftwobetavulgarispipaquaporins
AT amodeogabriela loopaiscriticalforthefunctionalinteractionoftwobetavulgarispipaquaporins
AT allevakarina loopaiscriticalforthefunctionalinteractionoftwobetavulgarispipaquaporins