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The research team led by Professor Sangho Lee in the Department of Biological Sciences (first author Dr. Yeongmok Lee) has uncovered the secret of how lipids regulate plant vacuoles through collaboration with scientists at the Institute for Plant Sciences of Montpellier (IPSiM) in France, the Department of Physics at Sungkyunkwan University and the Korea Basic Science Institute (KBSI). The team determined various structures of aluminum-activated malate transporter 9 (ALMT9) anion channel and proposed its structure-based activation mechanism.

Plant vacuoles are pivotal in storing and distributing various substances, thereby regulating stress resistance, volume, and other physiological processes. Diverse ion channels and transporters regulate the movement of substances in and out of vacuoles. Among them, the ALMT9 is reported to mediate crucial functions such as stomatal regulation and key determinants of fruit flavor.

The research team discovered unexpected lipid-bound states in various ALMT9 structures. Beyond structural analysis, collaboration with experts in mass spectrometry, electrophysiology, and molecular dynamics elucidated the crucial role of lipids in regulating ALMT9. This study sheds light on the roles of lipids in vacuolar regulation, paving the way for future research.

Prof. Sangho Lee remarked, "Through this study, the mystery of lipid function in regulating ALMT9 has finally been unveiled. This knowledge opens new frontiers in exploring the roles of lipids in biological phenomena." He also said, “It shows a research case using cryo-EM, a state-of-the-art device recently introduced in our university, emphasizing its potential for producing outstanding research outcomes.”

The research was published online in Nature Communications (IF: 14.7) on February 20th.

※ Title: Structural basis for malate-driven, pore lipid-regulated activation of the Arabidopsis vacuolar anion channel ALMT9

※ DOI:

※ Author: Ph.D. Yeongmok Lee (first author), Jaemin Yoo, Seoyeon Jung, Prof. Jejoong Yoo, Prof. Sangho Lee (corresponding author)

Figure 1. ALMT9 anion channel structures in various lipid-bound states