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

Abstract : 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 SCF EBF2 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.
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Contributor : Thomas Potuschak Connect in order to contact the contributor
Submitted on : Tuesday, November 8, 2022 - 5:49:20 PM
Last modification on : Thursday, November 10, 2022 - 4:07:49 PM


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Zhishuo Wang, Beatriz Orosa-Puente, Mika Nomoto, Heather Grey, Thomas Potuschak, et al.. Proteasome-associated ubiquitin ligase relays target plant hormone-specific transcriptional activators. Science Advances , 2022, 8 (42), ⟨10.1126/sciadv.abn4466⟩. ⟨hal-03843751⟩



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