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E3 ubiquitin ligase IPI1 controls rice immunity and flowering via both E3 ligase-dependent and -independent pathways. | LitMetric

AI Article Synopsis

  • Immunity and flowering in rice are energy-intensive processes, and the study reveals how the E3 ligase IPI1 regulates both through distinct mechanisms.
  • IPI1 prevents the degradation of the E3 ligase APIP6 without using its own E3 ligase activity, which in turn helps in degrading APIP6's targets through the ubiquitin-proteasome system.
  • Additionally, IPI1 directly ubiquitinates OsELF3-1 and OsELF3-2, leading to their degradation and causing IPI1 knockout plants to flower early but lose resistance to rice blast disease.

Article Abstract

Immunity and flowering are energy-consuming processes. However, the mechanism underlying the balance between immunity and flowering remains to be elucidated. Here, we report that the E3 ligase ideal plant architecture 1 interactor 1 (IPI1) controls rice immunity and flowering via two different pathways, one dependent on and another independent of its E3 ligase activity. We found that IPI1, a RING-finger E3 ligase, interacts with another E3 ligase, AvrPiz-t-interacting protein 6 (APIP6), and protects APIP6 from degradation by preventing APIP6's self-ubiquitination. Stabilization of APIP6 by IPI1 requires no IPI1 E3 ligase activity and leads to degradation of APIP6 substrates via the ubiquitin-proteasome system (UPS). Meanwhile, IPI1 directly ubiquitinates OsELF3-1 and OsELF3-2, two homologs of EARLY FLOWERING3 (ELF3), targeting them for degradation via the 26S proteasome. IPI1 knockout plants display early flowering but compromised resistance to rice blast. Thus, IPI1 balances rice immunity and flowering via both E3 ligase-dependent and -independent pathways.

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Source
http://dx.doi.org/10.1016/j.devcel.2024.06.014DOI Listing

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