ArticlePlant signaling & behavior2021
The roles of selectivity filters in determining aluminum transport by AtNIP1;2.
Article in Plant signaling & behavior, 2021. 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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Who cites it
5 citing papers in PubMed.
- Genome-Wide Identification and Expression Analysis of Aquaporin Gene Family in Tea Plant (Plants (Basel, Switzerland) · 2025Article
- Systematic Investigation of Aluminum Stress-Related Genes and Their Critical Roles in Plants.International journal of molecular sciences · 2024Review
- Structural assessment of OsNIP2;1 highlighted critical residues defining solute specificity and functionality of NIP class aquaporins.Journal of advanced research · 2024Article
- Involvement of cytokinins in STOP1-mediated resistance to proton toxicity.Stress biology · 2022Article
- The plasma membrane-localized OsNIP1;2 mediates internal aluminum detoxification in rice.Frontiers in plant science · 2022Article
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Authors and funding
9 authors.
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Abstract
Aquaporins (AQPs) are channel proteins involved in transporting a variety of substrates. It has been proposed that the constriction regions in the central pores of the AQP channels play a crucial role in determining transport substrates and activities of AQPs. Our previous results suggest that AtNIP1;2, a member of the AQP superfamily in Arabidopsis, facilitates aluminum transport across the plasma membrane. However, the functions of the constriction regions in AtNIP1;2-mediated transport activities are unclear. This study reports that residue substitutions of the constriction regions affect AtNIP1;2-mediated aluminum uptake, demonstrating the critical roles of the constriction regions for transport activities. Furthermore, a constriction region that partially or wholly mimics AtNIP5;1, a demonstrated boric-acid transporter, could not render the boric-acid transport activity to AtNIP1;2. Therefore, besides the constriction regions, other structural features are also involved in determining the nature of AtNIP1;2's transport activities.
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