首页> 外文OA文献 >The mechanics of F-actin microenvironments depend on the chemistry of probing surfaces.
【2h】

The mechanics of F-actin microenvironments depend on the chemistry of probing surfaces.

机译:F-肌动蛋白微环境的机制取决于探测表面的化学性质。

代理获取
本网站仅为用户提供外文OA文献查询和代理获取服务,本网站没有原文。下单后我们将采用程序或人工为您竭诚获取高质量的原文,但由于OA文献来源多样且变更频繁,仍可能出现获取不到、文献不完整或与标题不符等情况,如果获取不到我们将提供退款服务。请知悉。

摘要

To understand the microscopic mechanical properties of actin networks, we monitor the motion of embedded particles with controlled surface properties. The highly resolved Brownian motions of these particles reveal the viscoelastic character of the microenvironments around them. In both non-cross-linked and highly cross-linked actin networks, particles that bind F-actin report viscoelastic moduli comparable to those determined by macroscopic rheology experiments. By contrast, particles modified to prevent actin binding have weak microenvironments that are surprisingly insensitive to the introduction of filament cross-links. Even when adjacent in the same cross-linked gel, actin-binding and nonbinding particles report viscoelastic moduli that differ by two orders of magnitude at low frequencies (0.5-1.5 rad/s) but converge at high frequencies (> 10(4) rad/s). For all particle chemistries, electron and light microscopies show no F-actin recruitment or depletion, so F-actin microheterogeneities cannot explain the deep penetration (approximately 100 nm) of nonbinding particles. Instead, we hypothesize that a local depletion of cross-linking around nonbinding particles explains the phenomena. With implications for organelle mobility in cells, our results show that actin binding is required for microenvironments to reflect macroscopic properties, and conversely, releasing actin enhances particle mobility beyond the effects of mere biochemical untethering.
机译:为了了解肌动蛋白网络的微观机械性能,我们以受控的表面性能监控嵌入颗粒的运动。这些粒子的高度分解的布朗运动揭示了它们周围微环境的粘弹性特征。在非交联和高度交联的肌动蛋白网络中,与F-肌动蛋白结合的颗粒报告的粘弹性模量与宏观流变实验确定的相当。相反,经修饰以防止肌动蛋白结合的颗粒具有微弱的微环境,该微环境令人惊讶地对细丝交联的引入不敏感。即使在同一交联的凝胶中相邻,肌动蛋白结合和非结合粒子也报告粘弹性模量,它们在低频(0.5-1.5 rad / s)时相差两个数量级,但在高频(> 10(4)rad)时会聚/ s)。对于所有颗粒化学,电子和光显微镜检查均未显示F-肌动蛋白的募集或消耗,因此F-肌动蛋白的微异质性无法解释未结合颗粒的深度渗透(约100 nm)。取而代之的是,我们假设未结合颗粒周围的交联局部耗尽可以解释这种现象。对于细胞中细胞器的活动性有影响,我们的结果表明,肌动蛋白结合是微环境反映宏观特性所必需的,相反,释放肌动蛋白可以增强粒子的活动性,而不仅仅是单纯的生化解链作用。

著录项

相似文献

  • 外文文献
  • 中文文献
  • 专利
代理获取

客服邮箱:kefu@zhangqiaokeyan.com

京公网安备:11010802029741号 ICP备案号:京ICP备15016152号-6 六维联合信息科技 (北京) 有限公司©版权所有
  • 客服微信

  • 服务号