SRC调解了疫苗病毒从微管到基于actin的移动性的转换
Timothy P Newsome1, Niki Scaplehorn, Michael Way
1Cell Motility Laboratory, Room 529, Cancer Research UK, London Research Institute, Lincoln's Inn Fields Laboratories, 44 Lincoln's Inn Fields, London WC2A 3PX, UK.
概括
疫苗病毒的活性聚合需要Src-依赖的A36R酸化. 病毒蛋白B5R激活Src,触发A36R酸化并调节细胞移动性的素招募.
科学领域:
- 病毒学 病毒学
- 细胞生物学 细胞生物学
- 分子生物学分子生物学
背景情况:
- 疫苗病毒感染触发了actin聚合,这一过程对病毒传播至关重要.
- 众所周知,这种actin聚合由病毒膜蛋白A36R通过Src-依赖的氨酸酸化来调节.
研究的目的:
- 阐明调节Src激活和A36R酸化的上游信号事件.
- 了解Src活性在疫苗病毒运动性从基于微管的传输转变为基于actin的运动性中的作用.
主要方法:
- 研究了病毒膜蛋白B5R在激活Src. kinase中的作用.
- 分析了A36R对B5R信号的反应中的酸化状态.
- 研究了Src介导的A36R化对病毒颗粒对常规素的招募和释放的影响.
主要成果:
- 由病毒蛋白B5R启动的局部外进信号级联对于在血膜上强大的Src激活至关重要.
- 由B5R诱导的Src激活导致A36R的氨酸酸化.
- 通过Src介导的A36R酸化会影响病毒颗粒与常规素的相互作用,影响它们的运输.
结论:
- Src 激酶作为疫苗病毒运动性的关键调节剂.
- 由B5R启动的信号通路控制了微管体依赖的细胞质运输和细胞表面的基于actin的运动之间的切换.
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