Tyrosine phosphorylation of the GARU E3 ubiquitin ligase promotes gibberellin signalling by preventing GID1 degradation

Keiichirou Nemoto, Abdelaziz Ramadan, Gen-ichiro Arimura, Kenichiro Imai, Kentaro Tomii, Kazuo Shinozaki and Tatsuya Sawasaki ()
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Keiichirou Nemoto: Ehime University
Abdelaziz Ramadan: Ehime University
Gen-ichiro Arimura: Tokyo University of Science
Kenichiro Imai: National Institute of Advanced Industrial Science and Technology (AIST)
Kentaro Tomii: National Institute of Advanced Industrial Science and Technology (AIST)
Kazuo Shinozaki: RIKEN Center for Sustainable Resource Science
Tatsuya Sawasaki: Ehime University

Nature Communications, 2017, vol. 8, issue 1, 1-15

Abstract: Abstract Gibberellin (GA) is a major hormone for plant growth and development. GA response is derived from the degradation of DELLA repressor proteins after GA-dependent complex formation of the GID1 GA receptor with DELLA. Genistein is a known tyrosine (Tyr) kinase inhibitor and inhibits DELLA degradation. However, the biological role of Tyr phosphorylation on the GA response remains unclear. Here, we demonstrate that GARU (GA receptor RING E3 ubiquitin ligase) mediates ubiquitin-dependent degradation of GID1, and that the TAGK2 plant Tyr-kinase is a target of genistein and inhibits GARU–GID1A interactions by phosphorylation of GARU at Tyr321. Genistein induces degradation of GID1 and accumulation of DELLA. Conversely, Arabidopsis garu mutant and TAGK2-overexpressing plants accelerate GID1 stabilization and DELLA degradation. Under salt stress, GARU suppresses seed germination. We propose that GA response is negatively regulated by GARU-dependent GID1 ubiquitination and positively by Tyr phosphorylation of GARU by TAGK2, and genistein inhibits GA signaling by TAGK2 inhibition.

Date: 2017
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DOI: 10.1038/s41467-017-01005-5

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