Phosphatidic acid directly binds with rice potassium channel OsAKT2 to inhibit its activity.

The Plant Journal : for Cell and Molecular Biology
Like ShenWenhua Zhang

Abstract

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 do...Continue Reading

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Citations

Jul 1, 2020·Essays in Biochemistry·Sang-Chul Kim, Xuemin Wang
Jun 26, 2020·Plant, Cell & Environment·Daniela KocourkováJan Martinec
May 22, 2020·The Plant Journal : for Cell and Molecular Biology·Lyza Maron
Sep 20, 2020·International Journal of Molecular Sciences·Fumio SakaneChiaki Murakami
Sep 2, 2020·Trends in Plant Science·Ingo DreyerRainer Hedrich

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