Proteasome-associated ubiquitin ligase relays target plant hormone-specific transcriptional activators

Zhishuo Wang, Beatriz Orosa-Puente, Mika Nomoto, Heather Grey, Thomas Potuschak, Takakazu Matsuura, Izumi C. Mori, Yasuomi Tada, Pascal Genschik, Steven H. Spoel

Research output: Contribution to journalArticlepeer-review


The ubiquitin-proteasome system is vital to hormone-mediated developmental and stress responses in plants. Ubiquitin ligases target hormone-specific transcriptional activators (TAs) for degradation, but how TAs are processed by proteasomes remains unknown. We report that in Arabidopsis, the salicylic acid– and ethylene-responsive TAs, NPR1 and EIN3, are relayed from pathway-specific ubiquitin ligases to proteasome-associated HECT-type UPL3/4 ligases. Activity and stability of NPR1 were regulated by sequential action of three ubiquitin ligases, including UPL3/4, while proteasome processing of EIN3 required physical handover between ethylene-responsive SCFEBF2 and UPL3/4 ligases. Consequently, UPL3/4 controlled extensive hormone-induced developmental and stress-responsive transcriptional programs. Thus, our findings identify unknown ubiquitin ligase relays that terminate with proteasome-associated HECT-type ligases, which may be a universal mechanism for processive degradation of proteasome-targeted TAs and other substrates.

Original languageEnglish
Article numbereabn4466
JournalScience Advances
Issue number42
Publication statusPublished - Oct 21 2022

ASJC Scopus subject areas

  • General


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