TRIP6/LATS1复合体构成了α-catenin/vinculin在双细胞和三细胞结点上的张力传感器
Lin Xie1, Gangyun Wu1, Xiayu Liu1
1Center for Life Sciences, Yunnan University, Kunming, Yunnan 650500, China; Yunnan Key Laboratory of Cell Metabolism and Diseases, Kunming, Yunnan 650500, China.
European journal of cell biology
|May 28, 2024
概括
这项研究揭示了TRIP6和LATS1作为细胞张力传感器的新型组件,在细胞结点与α-catenin和vinculin一起工作. 这个复合体是机械敏感的,局部化到双细胞和三细胞结点.
科学领域:
- 细胞生物学 细胞生物学
- 生物物理学的生物物理.
- 分子生物学分子生物学
背景情况:
- 细胞-细胞机械传导对于组织发育和恒常状态至关重要.
- α-catenin (α-catenin) 和vinculin形成了一个核心复合体,该复合体在粘附结处感知和转化机械信号,影响细胞行为和像Hippo路径这样的途径.
- 基于α-catenin的张力传感器在细胞结点的精确组成和定位仍然不完全理解.
研究的目的:
- 调查TRIP6和LATS1与细胞-细胞结合处的α-catenin/vinculin复合物的相关性.
- 为了确定TRIP6/LATS1复合体的机械敏感性和局部化模式.
- 开发和验证一种新的机械传感器,用于研究细胞结点的张力.
主要方法:
- 在双细胞结 (BCJs) 和三细胞结 (TCJs) 上与α-catenin/vinculin共同定位TRIP6/LATS1的研究.
- 在影响细胞骨张力的条件下评估TRIP6/LATS1局部化 (cytochalasin B,Y-27632,blebbistatin) 并涉及ROCK1和α-catenin.
- 基于α-catenin/vinculin双分子光补充 (BiFC) 的机制传感器的开发和验证.
主要成果:
- 发现TRIP6/LATS1复合体在BCJ和TCJ中与α-catenin/vinculin共同局部化.
- TRIP6/LATS1到BCJs和TCJs的结点局部化取决于ROCK1和α-catenin,对机械干扰很敏感.
- α-catenin/vinculin/TRIP6/LATS1复合体在TCJs和BCJs表现出明显的局部化模式,而开发的机械传感器在BCJs表现出动态行为.
结论:
- TRIP6和LATS1被确定为基于α-catenin/vinculin的机械敏感张力传感器综合体的新型组件.
- 这种复合物局部存在于BCJ和TCJ,这表明它在多个结类型的紧张感应中的作用.
- 这些发现为细胞-细胞机制传导和细胞结合的调节的分子机制提供了新的见解.
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