ArticlePloS one2013
Loop A is critical for the functional interaction of two Beta vulgaris PIP aquaporins.
Article in PloS one, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed.
- A Ralstonia solanacearum effector RipAD perturbs aquaporin NbPIP oligomeric status to suppress plant immunity.The Plant journal : for cell and molecular biology · 2026Article
- Article
- Quaternary arrangements of membrane proteins: an aquaporin case.Biochemical Society transactions · 2024Review
- Membrane tension-dependent conformational change of Isoleucine 106 of loop B diminishes water permeability in FaPIP2;1.Protein science : a publication of the Protein Society · 2024Article
- Tissue-specific accumulation of PIP aquaporins of a particular heteromeric composition is part of the maize response to mycorrhiza and drought.Scientific reports · 2024Article
- Advancing Sustainable Malting Practices: Aquaporins as Potential Breeding Targets for Improved Water Uptake during Controlled Germination of Barley (Journal of agricultural and food chemistry · 2024Article
- Combined Soil Microorganism Amendments and Foliar Micronutrient Nanofertilization Increased the Production ofLife (Basel, Switzerland) · 2023Article
- Mechanosensitive aquaporins.Biophysical reviews · 2023Review
- Plasma membrane aquaporins interact with the endoplasmic reticulum resident VAP27 proteins at ER-PM contact sites and endocytic structures.The New phytologist · 2020Article
- Review
- Cooperativity in Plant Plasma Membrane Intrinsic Proteins (PIPs): Mechanism of Increased Water Transport in Maize PIP1 Channels in Hetero-tetramers.Scientific reports · 2018Article
- Heterotetramerization of Plant PIP1 and PIP2 Aquaporins Is an Evolutionary Ancient Feature to Guide PIP1 Plasma Membrane Localization and Function.Frontiers in plant science · 2018Article
- Plant and animal aquaporins crosstalk: what can be revealed from distinct perspectives.Biophysical reviews · 2017Review
- Article
- Two aquaporins, multiple ways of assembly.Channels (Austin, Tex.) · 2016Article
- PIP Water Transport and Its pH Dependence Are Regulated by Tetramer Stoichiometry.Biophysical journal · 2016Article
- Mutual Interactions between Aquaporins and Membrane Components.Frontiers in plant science · 2016Review
- Article
- Root hydraulic conductivity and adjustments in stomatal conductance: hydraulic strategy in response to salt stress in a halotolerant species.AoB PLANTS · 2015Article
- Prediction of aquaporin function by integrating evolutionary and functional analyses.The Journal of membrane biology · 2014Review
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Authors and funding
7 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
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.
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