CEP44的O-GlcNAcylation促进其滴状形成并调节其局部化
Mingzheng Hu1, Zihe Zhao1, Jinqiong Wang1
1Department of Genetics and Cell Biology, College of Life Sciences, State Key Laboratory of Medicinal Chemical Biology, Tianjin Union Medical Center, the First Affiliated Hospital of Nankai University, Nankai University, Tianjin, China.
Cytoskeleton (Hoboken, N.J.)
|September 4, 2025
概括
中体蛋白44 (CEP44) 可以通过液态相分离 (LLPS) 形成液滴. O-GlcNAcylation增强了CEP44滴体融合,影响了其在中心体组织中的功能.
科学领域:
- 细胞生物学
- 生物化学
- 分子生物学
背景情况:
- 中心体对于细胞的分裂和组织至关重要.
- 中位体蛋白44 (CEP44) 在中位体重复和螺旋体完整性中起着关键作用.
- 液相分离 (LLPS) 是形成细胞凝结物的机制,但其在CEP44功能中的作用尚不清楚.
研究的目的:
- 调查CEP44是否经过液态相分离 (LLPS).
- 确定O-GlcNAcylation在调节CEP44的相分离特性中的作用.
- 探索翻译后的修改如何影响CEP44的结构动态和本地化.
主要方法:
- 在CEP44中识别内在无序区域 (IDR).
- 在体外和体内测量液滴形成以评估LLPS.
- 检测CEP44 O-GlcNAcylation和与O-GlcNAc转移酶 (OGT) 的相互作用.
- 免疫覆盖可视化CEP44滴和评估O-GlcNAcylation对滴滴聚变的影响.
主要成果:
- CEP44在体外和体内形成液滴,证实了LLPS的能力.
- CEP44经历了O-GlcNAcylation,表明与OGT的相互作用.
- O-GlcNAcylation显著促进了CEP44滴状聚变.
- 计算分析表明O-GlcNAcylation和酸化在调节CEP44结构中的潜在相互作用.
结论:
- CEP44具有液态相分离 (LLPS) 的特性.
- O-GlcNAcylation是CEP44滴体融合的关键调节剂,并可能影响其亚细胞局部化.
- 这些发现为控制中心体组合和功能的分子机制提供了新的见解.
相关概念视频
Protein Folding Quality Check in the RER
3.8K
ER is the primary site for the maturation and folding of soluble and transmembrane secretory proteins. The calnexin cycle is a specific chaperone system that folds and assesses the confirmation of N-glycosylated proteins before they can exit the ER lumen. The primary players of this quality check pipeline are the lectins, ER-resident chaperones, and a glucosyl transferase enzyme. In case the calnexin system in the lumen fails to salvage a misfolded protein, it is transported to the cytoplasm...
3.8K
Coat Assembly and GTPases
3.6K
Vesicles incorporate different coat protein subunits in different cell locations, which changes the properties of the coat, such as the shape and geometry of the transport vesicles. Thus, vesicle coat proteins also play a significant role in cargo selection.
Coat assembly depends on the local availability of phosphatidylinositol phosphates or PIPs and GTP-binding proteins. Adaptor proteins, which link the coat proteins to the membrane, bind to these PIPs and play a crucial role in controlling...
Coat assembly depends on the local availability of phosphatidylinositol phosphates or PIPs and GTP-binding proteins. Adaptor proteins, which link the coat proteins to the membrane, bind to these PIPs and play a crucial role in controlling...
3.6K
Overview of Secretory Vesicles
8.6K
Secretory vesicles, also known as dense core vesicles (DCVs), are membrane-bound vesicles that transport secretory proteins, such as hormones or neurotransmitters. Regulated secretory vesicles transport proteins from the trans-Golgi network to the exterior of the cell. Proteins present in regulated secretory vesicles are required to be rapidly exocytosed in large amounts upon a specific stimulus.
Various proteins regulate the aggregation of molecules inside the secretory vesicles. Chromogranins...
Various proteins regulate the aggregation of molecules inside the secretory vesicles. Chromogranins...
8.6K
Oligosaccharide Assembly
3.0K
Protein glycosylation starts in the ER lumen and continues in the Golgi apparatus. Glycosyltransferases catalyze the addition of sugar molecules or glycosylation of proteins. Usually, these enzymes add sugars to the hydroxyl groups of selected serine or threonine residues to form O-linked glycans or the amino groups of asparagine residues to form N-linked glycans. Different positions on the same polypeptide chain can contain differently linked glycans.
Multiple sugar molecules that may or may...
Multiple sugar molecules that may or may...
3.0K
Clathrin Coated Vesicles
7.2K
Clathrin-coated vesicles use endocytosis to transport receptors and lysosomal hydrolases from the Golgi to the lysosome in the late secretory pathway. Clathrin-mediated endocytosis was the first described endocytic process, and Clathrin-coated vesicles remain one of the most well-studied transport vesicles. The molecular machinery that generates clathrin-coated vesicles comprises over 50 proteins that precisely coordinate vesicle formation. Cell surface receptors concentrated in indented sites...
7.2K
GPI Anchoring of Proteins in the ER Membrane
4.3K
GPI-anchoring is a post-translational, reversible protein modification that is ubiquitous in eukaryotes. Such proteins are primarily present on the exoplasmic leaflet of the plasma membrane.
GPI-anchor structure
A sequence of 11 enzymatic reactions results in the synthesis of the complete GPI anchor consisting of a hydrophobic and a hydrophilic portion. The hydrophobic portion comprises phosphatidylinositol, while the hydrophilic part comprises polar groups like phosphoethanolamine,...
GPI-anchor structure
A sequence of 11 enzymatic reactions results in the synthesis of the complete GPI anchor consisting of a hydrophobic and a hydrophilic portion. The hydrophobic portion comprises phosphatidylinositol, while the hydrophilic part comprises polar groups like phosphoethanolamine,...
4.3K


