Phosphatidic acid directly binds with rice potassium channel OsAKT2 to inhibit its activity
| العنوان: | Phosphatidic acid directly binds with rice potassium channel OsAKT2 to inhibit its activity |
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| المؤلفون: | Yue Shen, Hongsheng Zhang, Zhenzhen Zhou, Qi Wu, Qun Zhang, Wenhua Zhang, Lele Yang, Like Shen, Yiyuan Shi, Quanxiang Tian |
| المصدر: | The Plant Journal. 102:649-665 |
| بيانات النشر: | Wiley, 2020. |
| سنة النشر: | 2020 |
| مصطلحات موضوعية: | 0106 biological sciences, 0301 basic medicine, Potassium Channels, Arginine, Arabidopsis, Phosphatidic Acids, Plant Science, Biology, 01 natural sciences, 03 medical and health sciences, chemistry.chemical_compound, Genetics, Membrane potential, Arabidopsis Proteins, Cell Membrane, food and beverages, Oryza, Depolarization, Cell Biology, Phosphatidic acid, biology.organism_classification, Potassium channel, 030104 developmental biology, chemistry, Seedlings, Second messenger system, Biophysics, Phloem, 010606 plant biology & botany |
| الوصف: | The plant Shaker K+ channel AtAKT2 has been identified as a weakly rectifying channel that can stabilize membrane potentials to promote photoassimilate phloem loading and translocation. Thus, studies on functional characterization and regulatory mechanisms of AtAKT2-like channels in crops are highly important for improving crop production. Here, we identified the rice OsAKT2 as the ortholog of Arabidopsis AtAKT2, which is primarily expressed in the shoot phloem and localized at the plasma membrane. Using an electrophysiological assay, we found that OsAKT2 operated as a weakly rectifying K+ channel, preventing H+ /sucrose-symport-induced membrane depolarization. Three critical amino acid residues (K193, N206, and S326) are essential to the phosphorylation-mediated gating change of OsAKT2, consistent with the roles of the corresponding sites in AtAKT2. Disruption of OsAKT2 results in delayed growth of rice seedlings under short-day conditions. Interestingly, the lipid second messenger phosphatidic acid (PA) inhibits OsAKT2-mediated currents (both instantaneous and time-dependent components). Lipid dot-blot assay and liposome-protein binding analysis revealed that PA directly bound with two adjacent arginine residues in the ANK domain of OsAKT2, which is essential to PA-mediated inhibition of OsAKT2. Electrophysiological and phenotypic analyses also showed the PA-mediated inhibition of AtAKT2 and the negative correlation between intrinsic PA level and Arabidopsis growth, suggesting that PA may inhibit AKT2 function to affect plant growth and development. Our results functionally characterize the Shaker K+ channel OsAKT2 and reveal a direct link between phospholipid signaling and plant K+ channel modulation. |
| تدمد: | 1365-313X 0960-7412 |
| URL الوصول: | https://explore.openaire.eu/search/publication?articleId=doi_dedup___::be87218e8aac61d8b552f9c1d24477dd https://doi.org/10.1111/tpj.14731 |
| حقوق: | CLOSED |
| رقم الأكسشن: | edsair.doi.dedup.....be87218e8aac61d8b552f9c1d24477dd |
| قاعدة البيانات: | OpenAIRE |
| تدمد: | 1365313X 09607412 |
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