Proteasome-associated ubiquitin ligase relays target plant hormone-specific transcriptional activators
| Autor: | Heather Grey, Thomas Potuschak, Yasuomi Tada, Pascal Genschik, Mika Nomoto, Takakazu Matsuura, Steven H. Spoel, Zhishuo Wang, Izumi C. Mori, Beatriz Orosa-Puente |
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| Přispěvatelé: | Center for Gene Research [Nagoya, Japan], Nagoya University, Institut de biologie moléculaire des plantes (IBMP), Centre National de la Recherche Scientifique (CNRS)-Université de Strasbourg (UNISTRA) |
| Jazyk: | angličtina |
| Rok vydání: | 2021 |
| Předmět: |
0303 health sciences
Multidisciplinary biology Chemistry [SDV]Life Sciences [q-bio] 030302 biochemistry & molecular biology biology.organism_classification NPR1 Cell biology Ubiquitin ligase 03 medical and health sciences Ubiquitin Proteasome Arabidopsis biology.protein Plant hormone 030304 developmental biology |
| Zdroj: | Wang, Z, Orosa-Puente, B, Nomoto, M, Grey, H, Potuschak, T, Matsuura, T, Mori, I C, Tada, Y, Genschik, P & Spoel, S H 2022, ' Proteasome-associated ubiquitin ligase relays target plant hormone-specific transcriptional activators ', Science Advances, vol. 8, no. 42, eabn4466 . https://doi.org/10.1126/sciadv.abn4466 bioRxiv |
| DOI: | 10.1126/sciadv.abn4466 |
| Popis: | 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 was 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 programmes. 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.One-Sentence SummaryTranscriptional activators are targeted by proteasomal ubiquitin ligase relays that control their activity and stability. |
| Databáze: | OpenAIRE |
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