Specific control of Arabidopsis BAK1/SERK4-regulated cell death by protein glycosylation

Autor: Xin Chen, Guangyuan Xu, Marcos V. V. de Oliveira, Ana Marcia E. de A. Manhães, Abbey L. Musinsky, Bo Li, Ping He, Xiao Yu, Suzane Ariádina de Souza, Libo Shan, Xiangzong Meng, Luciano de Souza Vespoli, Hisashi Koiwa, Gonçalo Apolinário de Souza Filho, Aline Chaves Intorne
Rok vydání: 2016
Předmět:
Zdroj: Nature Plants. 2
ISSN: 2055-0278
Popis: Precise control of cell death is essential for the survival of all organisms. Arabidopsis thaliana BRASSINOSTEROID INSENSITIVE 1-associated receptor kinase 1 (BAK1) and somatic embryogenesis receptor kinase 4 (SERK4) redundantly and negatively regulate cell death through elusive mechanisms. By deploying a genetic screen for suppressors of cell death triggered by virus-induced gene silencing of BAK1/SERK4 on Arabidopsis knockout collections, we identified STT3a, a protein involved in N-glycosylation modification, as an important regulator of bak1/serk4 cell death. Systematic investigation of glycosylation pathway and endoplasmic reticulum (ER) quality control (ERQC) components revealed distinct and overlapping mechanisms of cell death regulated by BAK1/SERK4 and their interacting protein BIR1. Genome-wide transcriptional analysis revealed the activation of members of cysteine-rich receptor-like kinase (CRK) genes in the bak1/serk4 mutant. Ectopic expression of CRK4 induced STT3a/N-glycosylation-dependent cell death in Arabidopsis and Nicotiana benthamiana. Therefore, N-glycosylation and specific ERQC components are essential to activate bak1/serk4 cell death, and CRK4 is likely to be among client proteins of protein glycosylation involved in BAK1/SERK4-regulated cell death. Control of cell death is crucial for plant life. A comprehensive screen for suppressors of BAK1/SERK4-mediated cell death identified a component of protein glycosylation pathways and ERQC, and its cysteine-rich receptor-like kinase (CRK) targets.
Databáze: OpenAIRE