Expression takes place for most of the jasmonic acid (JA)-induced genes in a COI1-dependent manner via perception of its conjugate JA-Ile in the SCF COI1 -JAZ co-receptor complex. There are, however, numerous genes and processes, which are preferentially induced COI1-independently by the precursor of JA, 12-oxophytodienoic acid (OPDA). After recent identification of the Ile-conjugate of OPDA, OPDA-Ile, biological activity of this compound could be unequivocally proven in terms of gene expression. Any interference of OPDA, JA, or JAIle in OPDA-Ile-induced gene expression could be excluded by using different genetic background. The data suggest individual signaling properties of OPDA-Ile. Future studies for analysis of an SCF COI1 -JAZ co-receptorindependent route of signaling are proposed. Ten years ago, the new family of JASMONATE ZIM DOMAIN (JAZ) proteins with 12 members was occasionally identified in Arabidopsis in 3 different labs. [1][2][3] This was a breakthrough in JA research, since JAZ proteins were characterized as repressors of JA-Ile-induced gene expression. With identification of these proteins, it became clear that JA-Ile is perceived by the SCF COI1 -JAZ co-receptor complex. Components of this complex are the F-box protein called CORONATINE INSENSI-TIVE 1 (COI1), the Skp1/Cullin/complex with E3 ubiquitin ligase activity and the targets of the F-box protein, the JAZ proteins. JAZ proteins repress in the absence of JA-Ile positively acting transcription factors (TFs), such as MYC2, which bind to JA responsive elements (G-boxes) in the promoters of JAIle-regulated genes. Upon stress or developmentally regulated processes, an increase in JA-Ile level occurs leading to its binding in the SCF COI1 -JAZ co-receptor complex followed by proteasomal degradation of JAZ. Consequently, the free, positively acting MYC2 can switch on JA-Ile-responsive gene expression. 4 This basic scenario could be explained mechanistically upon crystallization of the complex, where an inositol-pentakisphosphate (IP 5 ) activates JA-Ile binding. 5 Interaction of the F-box protein COI1 and one of the JAZ proteins requires the C-terminal jas domain of JAZ. 6 This interaction is promoted by JA-Ile. Among the various stereo-isomeric forms of JA-Ile, the (+)-7-iso-JA-Ile has the highest activity. 7 JA-Ile perception via the SCF COI1 -JAZ-co-receptor complex was confirmed in the last couple of years including identification of new co-repressors and adaptors (for reviews, see refs. [8][9][10] ).There is, however, one open question due to the structural specificity in binding of the ligand JA-Ile. Among 40 different jasmonate compounds the stereoisomer (+)-7-iso-JA-Ile, carrying a ring conformation similar to coronatine, was most active. 7 Even coronatine was 10-fold more active then JA-Ile, although this bacterial toxin does not occur in plants. For the methyl ester of JA, for 12-oxo-phytodienoic acid (OPDA, the precursor of JA biosynthesis), and for OPDA-Ile (Fig. 1) no detectable promotion of JAZ3-COI1 interaction was recorded...