UNC5B是一个依赖异型的目标,用于ectodomain脱落
Kotaro Sugimoto1, Eichi Watabe2,3, Mio Takuma1
1Department of Biomedical Sciences, College of Life Sciences, Ritsumeikan University, Shiga 525-8577, Japan.
Journal of biochemistry
|July 9, 2025
概括
作为一种蛋白质加工事件,ectodomain shedding受替代拼接的影响. 这项研究表明,跳过特定的外显子会改变Netrin-1受体UNC5B的分泌,影响其生物作用.
科学领域:
- 分子生物学分子生物学
- 细胞生物学 细胞生物学
- 神经科学是一个神经科学.
背景情况:
- 生体主区脱落是一种翻译后的修改,调节了膜蛋白的功能.
- 生理学上,ectodomain 脱落的作用尚不完全理解.
- 柔膜区域的替代拼接可以影响蛋白质分离.
研究的目的:
- 为了研究替代拼接对膜蛋白质的ectodomain脱落的影响.
- 为了确定外子跳转是否影响Netrin-1受体UNC5B的分泌易感性.
主要方法:
- 对膜蛋白进行查,以检测由于外子跳跃而改变的分泌易感性.
- 对UNC5B拼接变体及其脱落特征的分析.
主要成果:
- 确定跳过或包含编码柔膜区域的特定外显子会改变UNC5B脱落.
- 证明了UNC5B脱落的拼接异形依赖调节.
结论:
- 柔膜区域的替代拼接是一种调节UNC5B脱落的机制.
- 由拼接异型分子调节的UNC5B脱落可能在神经电路形成,血管生成和癌症发育中发挥作用.
相关概念视频
Insertion of Single-pass Transmembrane Proteins in the RER
7.4K
Integral membrane proteins are proteins adhered to the lipid bilayer of a cell organelle or membrane. They can be of two types: transmembrane integral proteins that span the lipid bilayer and monotopic proteins that are attached to either side of the membrane but do not pass through it.
Integral transmembrane proteins possess transmembrane and extra membrane domains. The transmembrane domains are primarily made of 20-25 hydrophobic amino acids arranged in a helical secondary confirmation. These...
Integral transmembrane proteins possess transmembrane and extra membrane domains. The transmembrane domains are primarily made of 20-25 hydrophobic amino acids arranged in a helical secondary confirmation. These...
7.4K
Pinching-off of Coated Vesicles
3.3K
Vesicle budding is orchestrated by distinct cytosolic proteins such as adaptor proteins, coat proteins, and GTPases. To initiate vesicle budding, membrane-bending proteins containing crescent-shaped BAR domains bind to the lipid heads in the bilayer and distort the membrane to form a protein-coated vesicle bud. Adaptors proteins such as AP2 for clathrin-coated vesicles can nucleate on the deformed membrane. Finally, coat proteins such as clathrin or COPI and COPII assemble into a coat forming...
3.3K
Vesicular Tubular Clusters
2.6K
After budding out from the ER membrane, some COPII vesicles lose their coat and fuse with one another to form larger vesicles and interconnected tubules called vesicular tubular clusters or VTCs. These clusters constitute a compartment at the ER-Golgi interface known as ERGIC (Endoplasmic Reticulum Golgi Intermediate Compartment). The ERGIC is a mobile membrane-bound cargo transport system that sorts proteins secreted from ER and delivers them to the Golgi.
With the help of motor proteins such...
With the help of motor proteins such...
2.6K
Export of Misfolded Proteins out of the ER
3.9K
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...
3.9K
Clathrin Coated Vesicles
7.3K
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...
7.3K
Regulation of the Unfolded Protein Response
2.6K
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...
2.6K


