ArticleInternational journal of molecular sciences2023
Plant Aquaporin Gating Is Reversed by Phosphorylation on Intracellular Loop D-Evidence from Molecular Dynamics Simulations.
Article in International journal of molecular sciences, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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5 citing papers in PubMed, 9 citations in OpenAlex.
- Scaffold protein RhCASPL1D1 stabilizes RhPIP2 aquaporins and promotes flower recovery after dehydration in rose (Horticulture research · 2025Article
- Post-translational modification acts as a digital like switch influencing AtPIP2;1 water and cation permeability.Scientific reports · 2025Article
- Aquaporin Modulation by Cations, a Review.Current issues in molecular biology · 2024Review
- Article
- Methods for studying mammalian aquaporin biology.Biology methods & protocols · 2023Review
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Aquaporins (AQPs) constitute a wide and ancient protein family of transmembrane channels dedicated to the regulation of water exchange across biological membranes. In plants, higher numbers of AQP homologues have been conserved compared to other kingdoms of life such as in animals or in bacteria. As an illustration of this plant-specific functional diversity, plasma membrane intrinsic proteins (PIPs, i.e., a subfamily of plant AQPs) possess a long intracellular loop D, which can gate the channel by changing conformation as a function of the cellular environment. However, even though the closure of the AQP by loop D conformational changes is well described, the opening of the channel, on the other hand, is still misunderstood. Several studies have pointed to phosphorylation events as the trigger for the transition from closed- to open-channel states. Nonetheless, no clear answer has been obtained yet. Hence, in order to gain a more complete grasp of plant AQP regulation through this intracellular loop D gating, we investigated the opening of the channel in silico through molecular dynamics simulations of the crystallographic structure of
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