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Text: Xiaotong Liu, Yuanyuan Zhou and Dongping Lu Translated by: Yuanlong Liu, TPC Assistant Features Editor The research paper "dependent protein kinase CPK28 is targeted by the ubiquitin ligases ATL31 and ATL6 for proteasome-mediated degradation to fine-tune immune signaling in Arabidopsis" revealed the regulation of innate immunity in Arabidopsis
.
Background: Plants rely on innate immunity to defend against microbial pathogens
.
When immune receptors recognize microbial molecules, an immune response is triggered
.
The cytoplasmic kinase BOTRYTIS-INDUCED KINASE 1 (BIK1) plays an important role in distributing upstream immune signals from different receptors to different substrate proteins
.
Homeostasis of BIK1 is tightly controlled and maintained by a regulatory module in which the calcium-dependent protein kinase CPK28 helps maintain BIK1 homeostasis
.
Research question: Is CPK28 protein regulated to maintain BIK1 homeostasis while fine-tuning immune signaling? Findings: This study found that CPK28 protein was modified by ubiquitination and subsequently degraded by the 26S proteasome
.
Interestingly, bacterial flagellin treatment enhanced the ubiquitination and degradation of CPK28 protein
.
Arabidopsis TÓXICOS EN LEVADURA 31 (ATL31) and ATL6, two ubiquitin ligases, directly interact with CPK28 and mediate its ubiquitination, resulting in protein degradation of CPK28 and attenuation of CPK28 function
.
Thus, ATL31 and ATL6 regulate BIK1 homeostasis and regulate immune signaling by mediating CPK28 degradation
.
This study reveals how CPK28 is controlled to maintain BIK1 homeostasis and enhance immune responses
.
Research Outlook: The next research goal is to study how signals are transmitted from immune receptors to ATL31 and ATL6 to mediate the degradation of CPK28
.
Original link: https://doi.
org/10.
1093/plcell/koab242****Long press the QR code below to identify and follow***
.
Background: Plants rely on innate immunity to defend against microbial pathogens
.
When immune receptors recognize microbial molecules, an immune response is triggered
.
The cytoplasmic kinase BOTRYTIS-INDUCED KINASE 1 (BIK1) plays an important role in distributing upstream immune signals from different receptors to different substrate proteins
.
Homeostasis of BIK1 is tightly controlled and maintained by a regulatory module in which the calcium-dependent protein kinase CPK28 helps maintain BIK1 homeostasis
.
Research question: Is CPK28 protein regulated to maintain BIK1 homeostasis while fine-tuning immune signaling? Findings: This study found that CPK28 protein was modified by ubiquitination and subsequently degraded by the 26S proteasome
.
Interestingly, bacterial flagellin treatment enhanced the ubiquitination and degradation of CPK28 protein
.
Arabidopsis TÓXICOS EN LEVADURA 31 (ATL31) and ATL6, two ubiquitin ligases, directly interact with CPK28 and mediate its ubiquitination, resulting in protein degradation of CPK28 and attenuation of CPK28 function
.
Thus, ATL31 and ATL6 regulate BIK1 homeostasis and regulate immune signaling by mediating CPK28 degradation
.
This study reveals how CPK28 is controlled to maintain BIK1 homeostasis and enhance immune responses
.
Research Outlook: The next research goal is to study how signals are transmitted from immune receptors to ATL31 and ATL6 to mediate the degradation of CPK28
.
Original link: https://doi.
org/10.
1093/plcell/koab242****Long press the QR code below to identify and follow***
