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

Détails

ID Serval
serval:BIB_7E6031362103
Type
Article: article d'un périodique ou d'un magazine.
Collection
Publications
Institution
Titre
The MATH-BTB BPM3 and BPM5 subunits of Cullin3-RING E3 ubiquitin ligases target PP2CA and other clade A PP2Cs for degradation.
Périodique
Proceedings of the National Academy of Sciences of the United States of America
Auteur(s)
Julian J., Coego A., Lozano-Juste J., Lechner E., Wu Q., Zhang X., Merilo E., Belda-Palazon B., Park S.Y., Cutler S.R., An C., Genschik P., Rodriguez P.L.
ISSN
1091-6490 (Electronic)
ISSN-L
0027-8424
Statut éditorial
Publié
Date de publication
30/07/2019
Peer-reviewed
Oui
Volume
116
Numéro
31
Pages
15725-15734
Langue
anglais
Notes
Publication types: Journal Article ; Research Support, Non-U.S. Gov't
Publication Status: ppublish
Résumé
Early abscisic acid signaling involves degradation of clade A protein phosphatases type 2C (PP2Cs) as a complementary mechanism to PYR/PYL/RCAR-mediated inhibition of PP2C activity. At later steps, ABA induces up-regulation of PP2C transcripts and protein levels as a negative feedback mechanism. Therefore, resetting of ABA signaling also requires PP2C degradation to avoid excessive ABA-induced accumulation of PP2Cs. It has been demonstrated that ABA induces the degradation of existing ABI1 and PP2CA through the PUB12/13 and RGLG1/5 E3 ligases, respectively. However, other unidentified E3 ligases are predicted to regulate protein stability of clade A PP2Cs as well. In this work, we identified BTB/POZ AND MATH DOMAIN proteins (BPMs), substrate adaptors of the multimeric cullin3 (CUL3)-RING-based E3 ligases (CRL3s), as PP2CA-interacting proteins. BPM3 and BPM5 interact in the nucleus with PP2CA as well as with ABI1, ABI2, and HAB1. BPM3 and BPM5 accelerate the turnover of PP2Cs in an ABA-dependent manner and their overexpression leads to enhanced ABA sensitivity, whereas bpm3 bpm5 plants show increased accumulation of PP2CA, ABI1 and HAB1, which leads to global diminished ABA sensitivity. Using biochemical and genetic assays, we demonstrated that ubiquitination of PP2CA depends on BPM function. Given the formation of receptor-ABA-phosphatase ternary complexes is markedly affected by the abundance of protein components and ABA concentration, we reveal that BPMs and multimeric CRL3 E3 ligases are important modulators of PP2C coreceptor levels to regulate early ABA signaling as well as the later desensitizing-resetting steps.
Mots-clé
Abscisic Acid/pharmacokinetics, Amino Acid Motifs, Arabidopsis/genetics, Arabidopsis/metabolism, Arabidopsis Proteins/genetics, Arabidopsis Proteins/metabolism, Cullin Proteins/genetics, Cullin Proteins/metabolism, Phosphoprotein Phosphatases/genetics, Phosphoprotein Phosphatases/metabolism, Proteolysis, ABA, BPM, CRL3, PP2Cs, substrate receptor
Pubmed
Web of science
Open Access
Oui
Création de la notice
22/07/2019 16:11
Dernière modification de la notice
05/04/2020 5:20
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