TY - JOUR
T1 - Proteasome-associated ubiquitin ligase relays target plant hormone-specific transcriptional activators
AU - Wang, Zhishuo
AU - Orosa-Puente, Beatriz
AU - Nomoto, Mika
AU - Grey, Heather
AU - Potuschak, Thomas
AU - Matsuura, Takakazu
AU - Mori, Izumi C.
AU - Tada, Yasuomi
AU - Genschik, Pascal
AU - Spoel, Steven H.
N1 - Funding Information:
This work was supported by the European Research Council (ERC) under the European Union’s Horizon 2020 research and innovation program, grant agreement no. 678511 (to S.H.S.), Biotechnology and Biological Sciences Research Council (BBSRC) grant BB/S016767/1 (to S.H.S.), Darwin Trust PhD studentship (to Z.W.), Royal Society International Exchanges grant IEC\R3\170118 (to S.H.S. and Y.T.), SPS Grant-in-Aid for Scientific Research (B) grant 16H05065 (to Y.T.), and Agence Nationale de la Recherche (ANR) grant ANR-10-IDEX-0002 and IMCBio ANR-17-EURE-0023 (to T.P. and P.G.).
Publisher Copyright:
Copyright © 2022 The Authors.
PY - 2022/10/21
Y1 - 2022/10/21
N2 - 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.
AB - 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.
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U2 - 10.1126/sciadv.abn4466
DO - 10.1126/sciadv.abn4466
M3 - Article
C2 - 36269824
AN - SCOPUS:85140347831
SN - 2375-2548
VL - 8
JO - Science advances
JF - Science advances
IS - 42
M1 - eabn4466
ER -