Transcription factor-dependent nuclear localization of a transcriptional repressor in jasmonate hormone signaling

The plant hormone jasmonate (JA) plays an important role in regulating growth, development and immunity. A key step in JA signaling is ligand-dependent assembly of a coreceptor complex consisting of the F-box protein COI1 and JAZ transcriptional repressors. Assembly of this receptor complex results in proteasome-mediated degradation of JAZ repressors, which at resting state bind to and repress the MYC transcription factors. Although the JA receptor complex is believed to function within the nucleus, how this receptor complex enters the nucleus and, more generally, the cell biology of jasmonate signaling are not well understood. In this study, we conducted mutational analysis of the C termini (containing the conserved Jas motif) of two JAZ repressors, JAZ1 and JAZ9. These analyses unexpectedly revealed different subcellular localization patterns of JAZ1 Delta Jas and JAZ9 Delta Jas, which were associated with differential interaction of JAZ1 Delta Jas and JAZ9 Delta Jas with MYC2 and differential repressor activity in vivo. Importantly, physical interaction with MYC2 appears to play an active role in the nuclear targeting of JAZ1 and JAZ9, and the nuclear localization of JAZ9 was compromised in myc2 mutant plants. We identified a highly conserved arginine residue in the Jas motif that is critical for coupling MYC2 interaction with nuclear localization of JAZ9 and JAZ9 repressor function in vivo. Our results suggest a model for explaining why some JAZ Delta Jas proteins, but not others, confer constitutive JA-insensitivity when overexpressed in plants. Results also provide evidence for a transcription factor-dependent mechanism for nuclear import of a cognate transcriptional repressor JAZ9 in plants.