细胞的干扰会诱导光线ER蛋白质的分泌
Cell
|November 17, 1989
概括
离子体触发了来自小鼠纤维细胞的内质网膜 (ER) 网膜蛋白的分泌. 这种由引起的分泌物破坏了ER蛋白的保留,突出显示了.
科学领域:
- 细胞生物学 细胞生物学
- 分子生物学分子生物学
- 生物化学 生物化学
背景情况:
- 细胞内膜网膜 (ER) 含有称为网膜蛋白的光蛋白,通常保留在ER内,并被排除在分泌途径之外.
- 了解控制ER蛋白质保留的机制对于细胞平衡和蛋白质贩运至关重要.
研究的目的:
- 为了研究离子体对来自小鼠纤维细胞的视网胺分泌物的作用.
- 阐明细胞水平在ER中保留和分类网膜质蛋白中的作用.
主要方法:
- 用离子孔治疗小鼠纤维细胞.
- 使用凝流动性和内葡萄糖酶H敏感性的分泌和细胞内葡萄糖形式的分析.
- 微镜检查ER结构和蛋白质分布.
主要成果:
- 离子孔处理诱导了网膜质蛋白的高效分泌.
- 分泌和细胞内质蛋白表现出不同的凝流动性和内糖酶H敏感性.
- 视网质蛋白分泌导致ER枯竭和戈尔吉积累.
- 对离子体的ER应激反应导致了网膜质的重新积累和抑制的分泌.
- 在分泌过程中,ER结构和分布发生了变化.
结论:
- 细胞水平的扰乱破坏了网球质的ER保留机制.
- 离子可能在将网膜质蛋白从分泌蛋白分类中发挥重要作用.
- 这些发现表明,信号传递和蛋白质贩运在ER之间存在动态相互作用.
相关概念视频
Role of ER in the Secretory Pathway
Eukaryotic cells have a special pathway that enables communication between various intracellular membrane-bound compartments and also with the extracellular environment. This pathway is termed as the secretory pathway.
Components of the secretory pathway
About a third of proteins synthesized in the cell are sorted via the secretory route. They shuffle between different compartments in membrane-bound vesicles until they reach their final destination. The main intracellular compartments involved...
Components of the secretory pathway
About a third of proteins synthesized in the cell are sorted via the secretory route. They shuffle between different compartments in membrane-bound vesicles until they reach their final destination. The main intracellular compartments involved...
The Unfolded Protein Response
The ER is the hub of protein synthesis in a cell. It has robust systems to quality control protein folding and also for degradation of terminally misfolded proteins. Under normal conditions, a small proportion of misfolded proteins that cannot be salvaged need to be transported to the cytoplasm by the ER-associated degradation or ERAD pathways. However, if the ERAD cannot handle the misfolded proteins, the cell activates the unfolded protein response or UPR to adjust the protein folding...
Regulation of the Unfolded Protein Response
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...
Assembly of the Lipid Bilayer in the ER
Biological membranes are more than just a barrier separating cell cytoplasm from the outside environment. They are highly dynamic and help maintain the integrity and physiological stability of the cells as well as membrane-bound organelles. Membranes also play vital roles in cell-to-cell and intracellular communication.
A large chunk of any biological membrane is composed of phospholipids. These lipids have a heterogeneous distribution across different subcellular organelles and even between...
A large chunk of any biological membrane is composed of phospholipids. These lipids have a heterogeneous distribution across different subcellular organelles and even between...
Feedback Regulation of Calcium Concentration
Calcium is an essential signaling molecule required for various cellular functions. Calcium pumps and ion channels on cell and organellar membranes, such as those on the endoplasmic reticulum (ER), regulate calcium concentrations inside the cell. They remain closed, keeping the cytosolic calcium levels low at a resting state.
Various transmembrane receptors, such as G protein-coupled receptors (GPCRs), elicit a response to extracellular signals by increasing cytosolic calcium. Activated GPCRs...
Various transmembrane receptors, such as G protein-coupled receptors (GPCRs), elicit a response to extracellular signals by increasing cytosolic calcium. Activated GPCRs...
Calmodulin-dependent Signaling
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,...


