监禁NLRP3可以服炎症体活动
Kate Schroder1, Rebecca C Coll2
1Institute for Molecular Bioscience and IMB Centre for Inflammation and Disease Research, The University of Queensland, St. Lucia, QLD 4072, Australia.
Cell
|December 23, 2021
概括
一个关键的危险传感器NLRP3炎症体是由一个新的双环结构调节的. 这种不活跃的形式屏蔽了pyrin域,揭示了炎症控制的新机制.
科学领域:
- 免疫学
- 分子生物学
- 结构生物学
背景情况:
- 作为先天免疫的关键组成部分,NLRP3炎症酶的激活机制尚不完全理解.
- NLRP3炎症酶激活与各种炎症性疾病有关.
研究的目的:
- 阐明非活性NLRP3炎症体的结构基础.
- 发现NLRP3炎症酶激活的机制.
主要方法:
- 使用冷电子显微镜 (cryo-EM) 来确定非活性NLRP3的结构.
- 进行了生物化学和结构分析.
主要成果:
- 非活性NLRP3形成一个由12-16个单体组成的稳定双环.
- 这种双环结构封锁了皮林域,防止了自发的炎细胞组合.
- 通过冷电磁检测, 发现了不活跃复合体的精确结构.
结论:
- NLRP3炎症酶的激活是由以前未知的双环抑制机制调节的.
- 这一发现为炎症细胞组合和调节提供了新的见解.
- 这些发现为治疗NLRP3相关的炎症条件提供了潜在的点.
相关概念视频
NF-κB-dependent Signaling Pathway
7.9K
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...
7.9K
Regulation of Nuclear Protein Sorting
2.6K
Nuclear protein sorting regulates nucleus composition and gene expression, crucial for determining the fate of a eukaryotic cell. Hence, the entry and exit of molecules across the nuclear envelope is a tightly controlled process. Nuclear protein sorting can be inhibited by one of the following ways: 1) masking cargo signal sequences, 2) modifying the nuclear receptor's affinity for cargo, 3) controlling the nuclear pore size, 4) retaining the cargo during its transit to the cytosol or the...
2.6K
Regulation of the Unfolded Protein Response
2.7K
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...
2.7K


