BIK1 protein homeostasis is maintained by the interplay of different ubiquitin ligases in immune signaling.
Protein Serine-Threonine Kinases
/ genetics
Botrytis
/ metabolism
Arabidopsis Proteins
/ genetics
Phosphorylation
Arabidopsis
/ metabolism
Ligases
/ metabolism
Ubiquitin
/ metabolism
Proteostasis
Protein Kinases
/ genetics
Plant Proteins
/ metabolism
Receptors, Pattern Recognition
/ metabolism
Homeostasis
Ubiquitin-Protein Ligases
/ genetics
Plant Immunity
/ physiology
Journal
Nature communications
ISSN: 2041-1723
Titre abrégé: Nat Commun
Pays: England
ID NLM: 101528555
Informations de publication
Date de publication:
02 08 2023
02 08 2023
Historique:
received:
20
10
2022
accepted:
25
07
2023
medline:
4
8
2023
pubmed:
3
8
2023
entrez:
2
8
2023
Statut:
epublish
Résumé
Pathogen-associated molecular patterns (PAMPs) trigger plant innate immunity that acts as the first line of inducible defense against pathogen infection. A receptor-like cytoplasmic kinase BOTRYTIS-INDUCED KINASE 1 (BIK1) functions as a signaling hub immediately downstream of multiple pattern recognition receptors (PRRs). It is known that PLANT U-BOX PROTEIN 25 (PUB25) and PUB26 ubiquitinate BIK1 and mediate BIK1 degradation. However, how BIK1 homeostasis is maintained is not fully understood. Here, we show that two closely related ubiquitin ligases, RING DOMAIN LIGASE 1 (RGLG1) and RGLG2, preferentially associate with the hypo-phosphorylated BIK1 and promote the association of BIK1 with the co-receptor for several PRRs, BRI1-ASSOCIATED RECEPTOR KINASE1 (BAK1). PUB25 interacts with RGLG2 and mediates its degradation. In turn, RGLG2 represses the ubiquitin ligase activity of PUB25. RGLG1/2 suppress PUB25-mediated BIK1 degradation, promote BIK1 protein accumulation, and positively regulate immune signaling in a ubiquitin ligase activity-dependent manner. Our work reveals how BIK1 homeostasis is maintained by the interplay of different ubiquitin ligases.
Identifiants
pubmed: 37532719
doi: 10.1038/s41467-023-40364-0
pii: 10.1038/s41467-023-40364-0
pmc: PMC10397244
doi:
Substances chimiques
Protein Serine-Threonine Kinases
EC 2.7.11.1
Arabidopsis Proteins
0
Ligases
EC 6.-
Ubiquitin
0
Protein Kinases
EC 2.7.-
Plant Proteins
0
Receptors, Pattern Recognition
0
Ubiquitin-Protein Ligases
EC 2.3.2.27
BIK1 protein, Arabidopsis
EC 2.7.11.1
RGLG2 protein, Arabidopsis
EC 2.3.2.27
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
4624Informations de copyright
© 2023. The Author(s).
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