Abstract
SLAC1 is a slow-anion channel which has a central role in the control of stomatal closure and its activity is regulated by ABA and CO2. Regarding ABA sensing mechanism of SLAC1, it has been reported that this channel is activated by phosphorylation of Ser 120 in its N-terminal region from the OST1 kinase which is a positive regulator of ABA signaling. In contrast, its CO2 sensing mechanism remains unknown. To search for the regulatory region involved in the CO2 response, N- or C-terminal deletion SLAC1 genes (S1ΔN, S1ΔC ) were introduced into slac1-2 mutant. S1ΔN and S1ΔC can complement the CO2-insensitive phenotype of slac1-2. This result suggests that transmembrane region of SLAC1 (180~504 a.a.) have some regulatory site involved in stomatal CO2 response, and we hypothesized that direct phosphorylation of this transmembrane region is critical in CO2 signaling. Based on a 3D structural model of the SLAC1 channel, we discuss phosphprylation sites in the SLAC1 transmembrane region.