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National Academy of Sciences, Proceedings of the National Academy of Sciences, 31(116), p. 15725-15734, 2019

DOI: 10.1073/pnas.1908677116

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The MATH-BTB BPM3 and BPM5 subunits of Cullin3-RING E3 ubiquitin ligases target PP2CA and other clade A PP2Cs for degradation

Journal article published in 2019 by Jose Julian ORCID, Alberto Coego, Jorge Lozano-Juste ORCID, Esther Lechner, Qian Wu, Xu Zhang, Ebe Merilo, Borja Belda-Palazon ORCID, Sang-Youl Park, Sean R. Cutler, Chengcai An, Pascal Genschik ORCID, Pedro L. Rodriguez
This paper is made freely available by the publisher.
This paper is made freely available by the publisher.

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Abstract

Significance Relief of repression imposed by negative regulators is a crucial mechanism for plant hormone signaling. Clade A PP2Cs are key negative regulators of ABA signaling that are inhibited by ABA receptors. Degradation of PP2Cs is a complementary mechanism to PYR/PYL/RCAR-mediated ABA-dependent inhibition of PP2Cs. We reveal that BTB/POZ AND MATH DOMAIN proteins (BPMs), substrate adaptors of the multimeric cullin3 (CUL3)-RING-based E3 ligases (CRL3s), target PP2Cs for degradation. BPM-dependent degradation of PP2Cs is required for ABA-induced stomatal closure to counteract ABA-induced accumulation of PP2Cs and to reset resting phosphatase levels that allow efficient ABA signaling. Therefore, BPM-mediated proteolysis of transcription factors and clade A PP2Cs emerges as a general mechanism to regulate stress response and ABA signaling.