S100A11通过肌酸II驱动的收缩性和Piezo1介导的Ca2+进入促进着焦点粘附解体
Tareg Omer Mohammed1, You-Rong Lin1, Lucky Akter1
1WPI Nano Life Science Institute, Kanazawa University, Kanazawa, 920-1192, Japan.
Journal of cell science
|January 26, 2024
概括
S100A11蛋白被招募到焦点粘附 (FA) 上,并促进它们的分解. 这一过程涉及actomyosin收缩性和通过Piezo1通道的流入,揭示了S100A11在细胞粘附动态中的新作用.
科学领域:
- 细胞生物学 细胞生物学
- 分子生物学分子生物学
- 生物化学 生物化学
背景情况:
- S100A11是一种激活蛋白,局部化到应力纤维.
- 焦点粘附 (FAs) 对于细胞粘附和迁移至关重要.
- 包括拆卸在内的FA动态的调节对于细胞过程至关重要.
研究的目的:
- 研究S100A11在焦点粘附动态中的作用和定位.
- 为了阐明S100A11介导的焦点粘附分解背后的分子机制.
- 了解S100A11之间的相互作用,信号传递,和在FA周转中的actomyosin收缩性.
主要方法:
- 使用显微镜对HeLa和U2OS细胞中S100A11的局部化研究.
- 使用ionomycin对细胞内水平的操纵.
- 抑制非肌肉肌肉蛋白II (NMII) 和Piezo1通道.
- 对外力对外围焦点粘附的施加.
- 对S100A11-Knockout细胞的分析.
主要成果:
- S100A11局部化到焦点粘附,并在FA拆卸前暂时丰富.
- 提高细胞内刺激S100A11的招募和FA的拆卸.
- 对于S100A11的招募,NMII和Piezo1活动是必需的,这表明一种由actomyosin驱动的机制涉及Piezo1依赖的流入.
- 外部力量可以独立于NMII招募S100A11,这表明机械敏感的招募.
- S100A11-Knockout细胞表现出扩大的FA和延迟拆卸,证实FA周转率受损.
结论:
- 在促进焦点粘附分解方面,S100A11发挥了新的作用.
- S100A11的招募和激活是由actomyosin收缩性和Piezo1介导的流量调节的.
- 在像膜收缩这样的细胞过程中,S100A11对于适当的焦点粘附周转是必不可少的.
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