A ubiquitin-specific protease functions in regulating cell death and immune responses in rice.
Ting ZouGongwen LiMiaomiao LiuRui LiuShangyu YangKang WangLiuhui LuQiuyu YeJiaxu LiuJing LiangQiming DengShiquan WangJun ZhuYueyang LiangHuainian LiuXiumei YuChanghui SunPing LiShuangcheng LiPublished in: Plant, cell & environment (2023)
Ubiquitin-specific proteases (UBPs) process deubiquitination in eukaryotic organisms and are widely involved in plant development and responses to environmental stress. However, their role in cell death and plant immunity remains largely unknown. Here, we identified a rice lesion mimic mutant (LMM) and cloned its causative gene, LMM22. Both dysfunction and overexpression of LMM22 gave rise to the hypersensitive response-like cell death, reactive oxygen species bursts, and activated defense responses. LMM22 encodes an active UBP that is localized to the endoplasmic reticulum (ER) and displays a constitutive expression pattern in rice. LMM22 interacts with SPOTTED LEAF 35 (SPL35), a coupling of ubiquitin conjugation to ER degradation domain-containing protein that is known to participate in ubiquitination and the regulation of cell death and disease response in rice. Additional analyses suggest that LMM22 can positively regulate and stabilize the abundance of SPL35 protein likely through its deubiquitination activity. These data therefore improve our understanding of the function of UBP in rice innate immune responses by demonstrating that LMM22 functions as a critical regulator of SPL35 in cell death and disease resistance. This article is protected by copyright. All rights reserved.
Keyphrases
- cell death
- immune response
- endoplasmic reticulum
- cell cycle arrest
- reactive oxygen species
- binding protein
- small molecule
- poor prognosis
- cell proliferation
- protein protein
- gene expression
- transcription factor
- genome wide
- dna methylation
- copy number
- estrogen receptor
- big data
- amino acid
- human health
- artificial intelligence
- data analysis