相关实验视频
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Novel RNA-Binding Proteins Isolation by the RaPID Methodology
Published on: September 30, 2016
Yip3催化了内体Rab-GDI复合物的解离
Ulf Sivars1, Dikran Aivazian, Suzanne R Pfeffer
1Department of Biochemistry, Stanford University School of Medicine, Stanford, California 94305-5307, USA.
Nature
|October 24, 2003
概括
整体膜蛋白Yip3作为GDI移位因子,从GDI释放Rab GTPases以向膜. 这一发现对于了解真核细胞中的Rab蛋白调节至关重要.
科学领域:
- 细胞生物学 细胞生物学
- 分子生物学分子生物学
- 膜贩卖 膜贩卖 膜贩卖 膜贩卖
背景情况:
- 拉布GTPases是细胞内膜贩运的关键调节者.
- 前化Rab蛋白循环在细胞质中不活跃的GDP-bound状态 (绑定GDI) 和特定膜区的活跃的GTP-bound状态之间.
- 拉布蛋白精确地传递到它们正确的膜区,对于细胞功能至关重要.
研究的目的:
- 为了确定负责Rab-GDI复合体解离的因素.
- 阐明Rab蛋白向特定膜区的机制.
- 研究Yip3在Rab GTPase调节中的作用.
主要方法:
- 生物化学测定用于测试GDI移位活动.
- 描述 Yip3 作为一个不可分割的膜蛋白.
- 在实验室中复制Rab-GDI复合物解离和膜传递.
主要成果:
- 综合膜蛋白Yip3被确定为一种催化GDI移位因子.
- Yip3促进了从关氨酸核酸解离抑制剂 (GDI) 脱离预化Rab蛋白的解离.
- Yip3调解了Rab蛋白从GDI传递到膜的目标.
结论:
- 保存的 Yip 蛋白质作为 GDI 位移因子起作用.
- 益普蛋白对于Rab GTPases对细胞膜的准确向至关重要.
- 这种机制对于调节真核细胞中Rab介导的膜贩运至关重要.
相关概念视频
Coat Assembly and GTPases
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...
Rab Proteins
Rab proteins constitute the largest family of monomeric GTPases, of which 70 members are present in humans. Rab proteins and their effectors regulate consecutive stages of vesicle transport such as vesicle transport, docking, and fusion to the correct recipient membrane.
Rab proteins switch between a cytosolic, GDP-bound inactive state and a membrane-anchored, GTP-bound active state. By themselves, Rabs show slow rates of GDP/GTP exchange and GTP hydrolysis. Thus, Rab proteins are considered...
Rab proteins switch between a cytosolic, GDP-bound inactive state and a membrane-anchored, GTP-bound active state. By themselves, Rabs show slow rates of GDP/GTP exchange and GTP hydrolysis. Thus, Rab proteins are considered...
Rab Cascades
Rab GTPases act in a regulated cascade during membrane fusion, helping the lipid bilayers mix. The Rab family of proteins are active when bound to GTP, and inactive when bound to GDP. Hence, they act as guanine nucleotide-dependent molecular switches. Rab-GTP recognizes and binds to long or short-range tethering proteins to capture the target vesicle. These tethers coordinate with SNAREs on the vesicle and the target membrane to assemble the trans SNARE complex that locks the mixing bilayers.
Small GTPases - Ras and Rho
Ras and Rho are small monomeric GTPases that act downstream of receptor tyrosine kinase (RTK) and regulate various cellular processes. These GTPases switch between active and inactive states by binding to guanine nucleotides.
Three regulatory proteins control their activity:
Three regulatory proteins control their activity:
IP3/DAG Signaling Pathway
Membrane lipids such as phosphatidylinositol (PI) are precursors for several membrane-bound and soluble second messengers. Specific kinases phosphorylate PI and produce phosphorylated inositol phospholipids. One such inositol phospholipids are the phosphatidylinositol-4,5 bisphosphate [PI(4,5)P2], present in the inner half of the lipid bilayer. Upon ligand binding, GPCR stimulates Gq proteins to turn on phospholipase Cꞵ. Activated phospholipase Cꞵ cleaves PI(4,5)P2 and produces two-second...

