• ALGAE
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• 제36권4호
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• pp.315-326
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• 2021

Ion channels are membrane protein complexes mediating passive ion flux across the cell membranes. Every organism has a certain set of ion channels that define its physiology. Dinoflagellates are ecologically important microorganisms characterized by effective physiological adaptability, which backs up their massive proliferations that often result in harmful blooms (red tides). In this study, we used a bioinformatics approach to identify homologs of known ion channels that belong to 36 ion channel families. We demonstrated that the versatility of the dinoflagellate physiology is underpinned by a high diversity of ion channels including homologs of animal and plant proteins, as well as channels unique to protists. The analysis of 27 transcriptomes allowed reconstructing a consensus ion channel repertoire (channelome) of dinoflagellates including the members of 31 ion channel families: inwardly-rectifying potassium channels, two-pore domain potassium channels, voltage-gated potassium channels (K_v), tandem K_v, cyclic nucleotide-binding domain-containing channels (CNBD), tandem CNBD, eukaryotic ionotropic glutamate receptors, large-conductance calcium-activated potassium channels, intermediate/small-conductance calcium-activated potassium channels, eukaryotic single-domain voltage-gated cation channels, transient receptor potential channels, two-pore domain calcium channels, four-domain voltage-gated cation channels, cation and anion Cys-loop receptors, small-conductivity mechanosensitive channels, large-conductivity mechanosensitive channels, voltage-gated proton channels, inositole-1,4,5-trisphosphate receptors, slow anion channels, aluminum-activated malate transporters and quick anion channels, mitochondrial calcium uniporters, voltage-dependent anion channels, vesicular chloride channels, ionotropic purinergic receptors, animal volage-insensitive cation channels, channelrhodopsins, bestrophins, voltage-gated chloride channels H⁺/Cl^- exchangers, plant calcium-permeable mechanosensitive channels, and trimeric intracellular cation channels. Overall, dinoflagellates represent cells able to respond to physical and chemical stimuli utilizing a wide range of G-protein coupled receptors- and Ca²⁺-dependent signaling pathways. The applied approach not only shed light on the ion channel set in dinoflagellates, but also provided the information on possible molecular mechanisms underlying vital cellular processes dependent on the ion transport.

• The Korean Journal of Physiology and Pharmacology
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• 제24권6호
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• pp.555-561
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• 2020

TWIK-related two-pore domain K⁺ channel-2 (TREK-2) has voltage-independent activity and shows additional activation by acidic intracellular pH (pH_i) via neutralizing the E³³² in the cytoplasmic C terminal (Ct). We reported opposite regulations of TREK-2 by phosphatidylinositol 4,5-bisphosphate (PIP₂) via the alkaline K³³⁰ and triple Arg residues (R^355-357); inhibition and activation, respectively. The G³³⁴ between them appeared critical because its mutation (G³³⁴A) endowed hTREK-2 with tonic activity, similar to the mutation of the inhibitory K³³⁰ (K³³⁰A). To further elucidate the role of putative bent conformation at G³³⁴, we compared the dual mutation forms, K³³⁰A/G³³⁴A and G³³⁴A/R^355-7A, showing higher and lower basal activity, respectively. The results suggested that the tonic activity of G³³⁴A owes to a dominant influence from R^355-7. Since there are additional triple Arg residues (R^377-9) distal to R^355-7, we also examined the triple mutant (G³³⁴A/R^355-7A/R^377-9A) that showed tonic inhibition same with G³³⁴A/R^355-7A. Despite the state of tonic inhibition, the activation by acidic pH_i was preserved in both G³³⁴A/R^355-7A and G³³⁴A/R^355-7A/R^377-9A, similar to the R^355-7A. Also, the inhibitory effect of ATP could be commonly demonstrated under the activation by acidic pH_i in R^355-7A, G³³⁴A/R^355-7A, and G³³⁴A/R^355-7A/R^377-9A. These results suggest that the putative bent conformation at G³³⁴ is important to set the tug-of-war between K³³⁰ and R^355-7 in the PIP₂-dependent regulation of TREK-2.