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arXiv 0709.4019q-bio.CBphysics.bio-ph
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解剖亚秒钙粘蛋白结合态揭示了细胞实现超快探测其环境的有效方法

Dissecting Subsecond Cadherin Bound States Reveals an Efficient Way for Cells to Achieve Ultrafast Probing of their Environment

Anne Pierres, Anil Prakasam, Dominique Touchard, Anne-Marie Benoliel, Pierre Bongrand, Deborah Leckband

摘要:

细胞用膜受体不断探测它们的环境,实现其行为的亚秒级适应[1-3]。最近,发现几种受体,包括钙粘蛋白,结合配体的寿命为一秒的顺序。在这里,我们表明在单分子水平,同型C-钙粘蛋白协会涉及短暂的中间体持续不到几十毫秒。此外,这些中间体向更稳定的状态过渡,动力学速率随着皮牛顿力呈指数下降。这些特征使细胞能够在几分之一秒内检测配体或测量周围的机械行为,比以前认为的要快得多。

英文摘要:

Cells continuously probe their environment with membrane receptors, achieving subsecond adaptation of their behaviour [1-3]. Recently, several receptors, including cadherins, were found to bind ligands with a lifetime of order of one second. Here we show at the single molecule level that homotypic C-cadherin association involves transient intermediates lasting less than a few tens of milliseconds. Further, these intermediates transitionned towards more stable states with a kinetic rate displaying exponential decrease with piconewton forces. These features enable cells to detect ligands or measure surrounding mechanical behaviour within a fraction of a second, much more rapidly than was previously thought.

机构、总结、中文摘要均由AI分析而来,可能存在错误,请以论文正文为准。

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