The Ring-Type E3 Ubiquitin Ligase JUL1 Targets the VQ-Motif Protein JAV1 to Coordinate Jasmonate Signaling

Jasmonates regulate plant defense and development. In Arabidopsis ( ), JASMONATE-ASSOCIATED VQ-MOTIF 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 (...

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Veröffentlicht in:Plant physiology (Bethesda) 2019-04, Vol.179 (4), p.1273-1284
Hauptverfasser: Ali, Mohamed R M, Uemura, Takuya, Ramadan, Abdelaziz, Adachi, Kyoko, Nemoto, Keiichirou, Nozawa, Akira, Hoshino, Ryosuke, Abe, Hiroshi, Sawasaki, Tatsuya, Arimura, Gen-Ichiro
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container_issue 4
container_start_page 1273
container_title Plant physiology (Bethesda)
container_volume 179
creator Ali, Mohamed R M
Uemura, Takuya
Ramadan, Abdelaziz
Adachi, Kyoko
Nemoto, Keiichirou
Nozawa, Akira
Hoshino, Ryosuke
Abe, Hiroshi
Sawasaki, Tatsuya
Arimura, Gen-Ichiro
description Jasmonates regulate plant defense and development. In Arabidopsis ( ), JASMONATE-ASSOCIATED VQ-MOTIF 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 and 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 Gain or loss of function of JUL1 modulated the expression levels of the defensin gene in leaves, conferring on the plants various defense properties against the generalist herbivore Because neither the 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.
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In Arabidopsis ( ), JASMONATE-ASSOCIATED VQ-MOTIF 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 and 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 Gain or loss of function of JUL1 modulated the expression levels of the defensin gene in leaves, conferring on the plants various defense properties against the generalist herbivore Because neither the 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. 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source Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; Oxford University Press Journals All Titles (1996-Current)
title The Ring-Type E3 Ubiquitin Ligase JUL1 Targets the VQ-Motif Protein JAV1 to Coordinate Jasmonate Signaling
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