The MATH-BTB BPM3 and BPM5 subunits of Cullin3-RING E3 ubiquitin ligases target PP2CA and other clade A PP2Cs for degradation
Author(s) -
Jose Julian,
Alberto Coego,
Jorge LozanoJuste,
Esther Lechner,
Qian Wu,
Xu Zhang,
Ebe Merilo,
Borja BeldaPalazón,
SangYoul Park,
Sean R. Cutler,
Chengcai An,
Pascal Genschik,
Pedro L. Rodrı́guez
Publication year - 2019
Publication title -
proceedings of the national academy of sciences
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.011
H-Index - 771
eISSN - 1091-6490
pISSN - 0027-8424
DOI - 10.1073/pnas.1908677116
Subject(s) - ubiquitin , phosphatase , microbiology and biotechnology , abscisic acid , ubiquitin ligase , f box protein , protein subunit , protein degradation , chemistry , biochemistry , biology , phosphorylation , gene
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.
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