COP9的多功能作用在真核生物的发育,免疫力和环境适应性方面具有重要意义
Ying Zhao1,2, Guangshuo Li3
1School of Enology and Horticulture, Ningxia University, Yinchuan, 750021, People's Republic of China. Y_zhaoying@163.com.
Planta
|December 18, 2025
概括
COP9信号体 (CSN) 是一个关键的植物调节器,协调脱,信号和应激反应. 它集成环境信号来微调发育和免疫力,作为真核细胞细胞功能的中心枢纽.
科学领域:
- 植物生物学 植物生物学
- 分子生物学分子生物学
- 细胞调节 细胞调节 细胞调节
背景情况:
- COP9信号体 (CSN) 是一个进化保守的多蛋白质复合体.
- CSN调节各种生物过程,包括蛋白质降解,激素信号,应激适应,发育和免疫.
- CSN的核心功能包括对库林-RING E3泛素酶的脱,通过泛素-蛋白酶体系统影响蛋白质周转.
研究的目的:
- 审查CSN在植物中的多功能作用和监管机制.
- 突出对CSN在转录和表观遗传调节中的作用的新见解.
- 通过整合最近的进展和跨王国的观点,为CSN作为真核细胞细胞功能的中心节点提供一个全面的框架.
主要方法:
- 文献综述和近期机械学进展的综合.
- 综合各种生物体和生物途径的发现.
- 专注于植物特异性作用,包括转录和表观遗传调节.
主要成果:
- CSN充当中央监管中心,协调植物的脱,信号,转录和应激反应.
- CSN集成外部信号 (光,病原体) 来调节发育计划和防御.
- 突出了在二次新陈代谢,开花时间,ROS恒温和压力诱导的表观遗传记忆中的新兴角色.
结论:
- CSN是植物发育和免疫力的关键调节者,协调关键的细胞过程.
- 病原体可以操纵CSN通路以抑制宿主免疫力.
- 了解CSN复杂的调节网络对于理解真核细胞细胞功能至关重要.
相关概念视频
Assembly of Signaling Complexes
6.4K
Multiprotein signaling complexes are formed in a dynamic process involving protein-protein interactions at the cytoplasmic domain of transmembrane receptors or enzymatic and non-enzymatic proteins associated with the receptor. These complexes ensure the activation and propagation of intracellular signals that regulate cell functions.
Interaction domains in cell signaling
Interaction domains recognize exposed features of their binding partners containing post-translationally modified sequences,...
Interaction domains in cell signaling
Interaction domains recognize exposed features of their binding partners containing post-translationally modified sequences,...
6.4K
Protein Complexes with Interchangeable Parts
2.8K
Groups of proteins may form a complex where each protein in this complex has a different role in the overall execution of the complex’s function. Often some of the proteins in the complex can be replaced by a closely related variant to give a complex that contains many of the same components yet is functionally distinct.
The SCF ubiquitin ligase is a protein complex of five individual proteins. This complex attaches ubiquitin to other target proteins to mark them for degradation. In order...
The SCF ubiquitin ligase is a protein complex of five individual proteins. This complex attaches ubiquitin to other target proteins to mark them for degradation. In order...
2.8K
Regulation of the Unfolded Protein Response
2.9K
Inositol-requiring kinase one or IRE1 is the most conserved eukaryotic unfolded protein response (UPR) receptor. It is a type I transmembrane protein kinase receptor with a distinctive site-specific RNase activity. As the binding mechanics of the misfolded proteins with the N-terminal domain of IRE-1 are unclear, three binding models — direct, indirect, and allosteric -- are proposed for receptor activation. Nevertheless, it is known that once a misfolded protein associates with IRE1, it...
2.9K
The JAK-STAT Signaling Pathway
11.8K
Several cytokine receptors have tightly bound Janus kinase or JAK proteins attached at their cytosolic tail. Small signaling molecules such as cytokines, growth hormones, or prolactins bind to the cytokine receptors and initiate their dimerization. The dimerization brings the cytosolic JAKs together that trans-phosphorylate and activates each other. The activated JAKs now phosphorylate cytosolic tails of the cytokine receptors, which serve as binding sites for adaptor proteins such as SH2...
11.8K
NF-κB-dependent Signaling Pathway
9.7K
The transcription factor NF-κB was discovered in 1986 in the lab of Nobel laureate Professor David Baltimore, for its interaction with the immunoglobulin light chain enhancer in B-cells. After more than three decades of study, it is now evident that NF-κB regulates the expression of over 100 genes. Most of these genes play an essential role in the innate and adaptive immune responses as well as the inflammatory responses of animals.
NF-κB-dependent Signaling Mechanism
The...
NF-κB-dependent Signaling Mechanism
The...
9.7K
Calmodulin-dependent Signaling
6.0K
Calmodulin (CaM) is a calcium-binding protein in eukaryotes that controls various calcium-regulated cellular processes. It has four calcium-binding sites that bind calcium to form the calcium-calmodulin ( Ca2+-CaM) complex. GPCR stimulation increases the calcium levels in the cells that bind to CaM and induces a conformational change.
The Ca2+-CaM complex does not have enzymatic activity by itself. Instead, the complex binds downstream target proteins, including membrane proteins or enzymes,...
The Ca2+-CaM complex does not have enzymatic activity by itself. Instead, the complex binds downstream target proteins, including membrane proteins or enzymes,...
6.0K


