The ring-type E3 ubiquitin ligase JUL1 targets the vq-motif protein JAV1 to coordinate jasmonate signaling

Mohamed R.M. Ali, Takuya Uemura, Abdelaziz Ramadan, Kyoko Adachi, Keiichirou Nemoto, Akira Nozawa, Ryosuke Hoshino, Hiroshi Abe, Tatsuya Sawasaki, Gen Ichiro Arimura

Research output: Contribution to journalArticlepeer-review

48 Citations (Scopus)

Abstract

Jasmonates regulate plant defense and development. In Arabidopsis (Arabidopsis thaliana), JASMONATE-ASSOCIATED VQMOTIF GENE1 (JAV1/VQ22) is a repressor of jasmonate-mediated defense responses and is degraded through the ubiquitin-26S proteasome system after herbivory. We found that JAV1-ASSOCIATED UBIQUITIN LIGASE1 (JUL1), a RING-type E3 ubiquitin ligase, interacted with JAV1. JUL1 interacted with JAV1 in the nucleus to ubiquitinate JAV1, leading to proteasomal degradation of JAV1. The transcript levels of JUL1 and JAV1 were coordinately and positively regulated by the CORONATINE INSENSITIVE1- dependent signaling pathway in the jasmonate signaling network, but in a manner that was not dependent on CORONATINE INSENSITIVE1-mediated signaling upon herbivory by Spodoptera litura. Gain or loss of function of JUL1 modulated the expression levels of the defensin gene PDF1.2 in leaves, conferring on the plants various defense properties against the generalist herbivore S. litura. Because neither the JUL1 mutant nor overexpression lines showed any obvious developmental defects, we concluded that the JAV1/JUL1 system functions as a specific coordinator of reprogramming of plant defense responses. Altogether, our findings offer insight into the mechanisms by which the JAV1/JUL1 system acts specifically to coordinate plant defense responses without interfering with plant development or growth.

Original languageEnglish
Pages (from-to)1273-1284
Number of pages12
JournalPlant physiology
Volume179
Issue number4
DOIs
Publication statusPublished - Apr 2019

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