纤维蛋白与细胞骨之间的两比克纽顿滑动键取决于塔林
Guoying Jiang1, Grégory Giannone, David R Critchley
1Department of Biological Sciences, Columbia University, 1212 Amsterdam Avenue, New York, New York 11027, USA.
Nature
|July 18, 2003
概括
研究人员发现了对细胞力学至关重要的分子滑动键. 这种结合,涉及纤维素和塔林1,需要2-pN力来打破,影响细胞活力和器官功能.
科学领域:
- 细胞生物学 细胞生物学
- 生物物理学的生物物理.
- 生物化学 生化学
背景情况:
- 细胞结构上的机械力量,如整体素-细胞骨联系,对于细胞活力,形态学和器官功能至关重要.
- 这些力量是由分子连接产生的,这些连接将细胞外矩阵-整合素复合体与细胞骨连接起来.
- 一个最小的矩阵复合体,纤维内素FNIII7-10域的三元体,介导整合素-细胞骨连接.
研究的目的:
- 为了研究参与细胞力量生成的最小矩阵复合体的机械特性.
- 确定分子参与者和参与建立整体素-细胞骨连接的力量.
- 阐明talin1在介导纤维素-整体素复合体和actin细胞骨架之间的力传递中的作用.
主要方法:
- 使用单片切割珠来研究纤维内素FNIII7-10切割器在强力下的机械行为.
- 应用蜂负载率 (60 nm x s(-1)) 来测量键断裂力.
- 通过评估其对滑动键形成和细胞骨结合的要求,研究了talin1的作用.
- 检查了抑制纤维素结合alpha(v) beta3整合素和β3删除对产生力的影响.
主要成果:
- 确定了一种特定的分子滑动键,在细胞负载率下被2pN力反复破坏.
- 这种2-pN滑动键在单一的三元珠中被观察到,但不是在单质单元中.
- 发现Talin1对于2-pN滑动键和快速细胞骨结合是必不可少的.
- 抑制纤维素-α ((v) beta3结合和β3删除显著降低了2-pN力峰值.
结论:
- 塔林1可能会在纤维素-整体素复合体和actin细胞骨架之间形成初始的分子滑动键.
- 这种滑动键机制允许对纤维肌菌素施加低级别的力,直到多个键形成或信号激活更强的力响应.
- 了解这些分子力机制对于理解细胞活力,形态和器官功能至关重要.
相关概念视频
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Structural proteins are a category of proteins responsible for functions ranging from cell shape and movement to providing support to major structures such as bones, cartilage, hair, and muscles. This group includes proteins such as collagen, actin, myosin, and keratin.
Collagen, the most abundant protein in mammals, is found throughout the body. In connective tissue, such as skin, ligaments, and tendons, it provides tensile strength and elasticity. In bones and teeth, it mineralizes to form...
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