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相关概念视频

Protein Modifications in the RER01:26

Protein Modifications in the RER

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Modification of secretory and transmembrane proteins entering the rough ER begins in the ER lumen. These modifications aid in protein folding and stabilize the acquired tertiary structure. Protein modifications in the rough ER co-occur at different stages of protein folding.
Broadly, these modifications can be categorized into four main categories — glycosylation, formation of disulfide bonds, assembly of protein subunits, and specific proteolytic cleavages like removal of signal...
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G protein-coupled receptor (GPCR) signaling plays a crucial role in cell functioning. GPCR desensitization is an equally essential process. It allows cells to respond to changing environments and regain sensitivity to new stimuli while preventing unnecessary stimulation when no longer needed. Prolonged exposure to stimuli leads to GPCR desensitization. It involves blocking the receptors from binding and activating additional G proteins. This inhibits activation of downstream effectors, thereby...
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Activation and Inactivation of G Proteins01:22

Activation and Inactivation of G Proteins

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Heterotrimeric G proteins are guanine nucleotide-binding proteins. As the name suggests, heterotrimeric G proteins are composed of three subunits: alpha, beta, and gamma. They remain GDP-bound or GTP-bound inside the cells and switch between inactive/active states. The Gα subunit possesses the nucleotide-binding pocket that binds guanine nucleotides and switches between GDP or GTP-bound states. In contrast, the Gꞵ and Gγ subunits are always bound together with high...
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Amplifying Signals via Enzymatic Cascade01:22

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When a ligand binds to a cell-surface receptor, the receptor's intracellular domain changes shape, which may either activate its enzyme function or allow its binding to other molecules. The initial signal is amplified by most signal transduction pathways. This means that a single ligand molecule can activate multiple molecules of a downstream target. Proteins that relay a signal are most commonly phosphorylated at one or more sites, activating or inactivating the protein. Kinases catalyze...
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The Unfolded Protein Response01:37

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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...
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Export of Misfolded Proteins out of the ER01:32

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After folding, the ER assesses the quality of secretory and membrane proteins. The correctly folded proteins are cleared by the calnexin cycle for transport to their final destination, while misfolded proteins are held back in the ER lumen. The ER chaperones attempt to unfold and refold the misfolded proteins but sometimes fail to achieve the correct native conformation. Such terminally misfolded proteins are then exported to the cytosol by ER-associated degradation or ERAD pathway for...
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相关实验视频

Updated: Jun 28, 2025

Live Imaging Assay for Assessing the Roles of Ca2+ and Sphingomyelinase in the Repair of Pore-forming Toxin Wounds
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有关ROS的S-palmitoylation激活物分离和完整的Gasdermin D

Gang Du1,2, Liam B Healy3,4, Liron David5,6,7

  • 1Department of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, MA, USA. gdu@crystal.harvard.edu.

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|April 10, 2024
PubMed
概括
此摘要是机器生成的。

气体皮质D (GSDMD) 是棕化,这是一种在热过程中对孔隙形成至关重要的改变. 这种可逆的棕化作为GSDMD激活的关键开关,挑战了先前的分裂是唯一的触发因素.

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科学领域:

  • 细胞生物学
  • 免疫学
  • 生物化学

背景情况:

  • 气体皮质D (GSDMD) 是炎症酶激活的关键因子,通过形成跨膜毛孔来调解细胞因子分泌和热.
  • 主要归因于其N终端域 (GSDMD-NT) 的孔形成.

研究的目的:

  • 调查除了裂变之外的翻译后修改在GSDMD激活中的作用.
  • 找出控制 GSDMD 中介性热的新调节机制.

主要方法:

  • 在Cys191中使用生物化学测定来评估GSDMD的棕化.
  • 通过裂变缺陷突变物和脂质体泄漏试验,研究S-palmitoylation对GSDMD孔隙形成和热的影响.
  • 识别GSDMD棕转移酶 (ZDHHC5,ZDHHC9) 并通过炎酶激活和活性氧物种 (ROS) 分析它们的调节.

主要成果:

  • GSDMD Cys191是S-palmitoylated,这种修饰对于孔隙形成至关重要,独立于酶裂变.
  • 来自线粒体的活性氧物种 (ROS) 增强了GSDMD的棕化.
  • 棕化GSDMD,包括裂变缺陷的形式,诱导脂质体泄漏和热,棕化作为气皮胺家族的关键激活开关.

结论:

  • 可逆S-palmitoylation是Gasdermin D孔隙形成和热的关键检查点,作为Gasdermin家族的一般激活开关.
  • 这一发现挑战了酶媒介裂变是GSDMD激活的唯一触发因素的范式.
  • 棕化是调节炎症反应的新型治疗点.