ArticlePlant physiology2013
Identification of a probable pore-forming domain in the multimeric vacuolar anion channel AtALMT9.
Article in Plant physiology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.
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Who cites it
27 citing papers in PubMed, 43 citations in OpenAlex.
- Genome-wide identification of key genes related to chloride ion (ClBMC genomics · 2025Article
- A Synthetic Facultative CAM-Like Shuttle in CAdvanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025Article
- Structural basis for malate-driven, pore lipid-regulated activation of the Arabidopsis vacuolar anion channel ALMT9.Nature communications · 2025Article
- Identification and Analysis of Aluminum-Activated Malate Transporter Gene Family Reveals Functional Diversification in Orchidaceae and the Expression Patterns ofInternational journal of molecular sciences · 2024Article
- The Role of Low-Molecular-Weight Organic Acids in Metal Homeostasis in Plants.International journal of molecular sciences · 2024Review
- Systematic Investigation of Aluminum Stress-Related Genes and Their Critical Roles in Plants.International journal of molecular sciences · 2024Review
- Alternative Splicing Underpins the ALMT9 Transporter Function for Vacuolar Malic Acid Accumulation in Apple.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2024Article
- Recent Updates on ALMT Transporters' Physiology, Regulation, and Molecular Evolution in Plants.Plants (Basel, Switzerland) · 2023Review
- γ-Aminobutyric acid may directly or indirectly regulate Arabidopsis ALMT9.Plant physiology · 2022Article
- Heterologous expression reveals that GABA does not directly inhibit the vacuolar anion channel AtALMT9.Plant physiology · 2022Article
- Multiple ALMT subunits combine to form functional anion channels: A case study for rice ALMT7.Frontiers in plant science · 2022Article
- The Interaction Between CitMYB52 and CitbHLH2 Negatively Regulates Citrate Accumulation by ActivatingFrontiers in plant science · 2022Article
- Alluminating structure key to stress tolerance.Cell research · 2022Article
- Mechanisms and regulation of organic acid accumulation in plant vacuoles.Horticulture research · 2021Review
- GABA signalling modulates stomatal opening to enhance plant water use efficiency and drought resilience.Nature communications · 2021Article
- Identification of Genes Preferentially Expressed in Stomatal Guard Cells ofFrontiers in plant science · 2021Article
- Engineering Strategies to Boost Crop Productivity by Cutting Respiratory Carbon Loss.The Plant cell · 2019Review
- Identification of SLAC1 anion channel residues required for COProceedings of the National Academy of Sciences of the United States of America · 2018Article
- Cytosolic malate and oxaloacetate activate S-type anion channels in Arabidopsis guard cells.The New phytologist · 2018Article
- Aluminum-Activated Malate Transporters Can Facilitate GABA Transport.The Plant cell · 2018Article
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Aluminum-activated malate transporters (ALMTs) form an important family of anion channels involved in fundamental physiological processes in plants. Because of their importance, the role of ALMTs in plant physiology is studied extensively. In contrast, the structural basis of their functional properties is largely unknown. This lack of information limits the understanding of the functional and physiological differences between ALMTs and their impact on anion transport in plants. This study aimed at investigating the structural organization of the transmembrane domain of the Arabidopsis (Arabidopsis thaliana) vacuolar channel AtALMT9. For that purpose, we performed a large-scale mutagenesis analysis and found two residues that form a salt bridge between the first and second putative transmembrane α-helices (TMα1 and TMα2). Furthermore, using a combination of pharmacological and mutagenesis approaches, we identified citrate as an "open channel blocker" of AtALMT9 and used this tool to examine the inhibition sensitivity of different point mutants of highly conserved amino acid residues. By this means, we found a stretch within the cytosolic moiety of the TMα5 that is a probable pore-forming domain. Moreover, using a citrate-insensitive AtALMT9 mutant and biochemical approaches, we could demonstrate that AtALMT9 forms a multimeric complex that is supposedly composed of four subunits. In summary, our data provide, to our knowledge, the first evidence about the structural organization of an ion channel of the ALMT family. We suggest that AtALMT9 is a tetramer and that the TMα5 domains of the subunits contribute to form the pore of this anion channel.
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