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非肌肉肌球蛋白 II 在细胞收缩系统组装中的功能。

Functions of nonmuscle myosin II in assembly of the cellular contractile system.

机构信息

Department of Biology, University of Pennsylvania, Philadelphia, Pennsylvania, United States of America.

出版信息

PLoS One. 2012;7(7):e40814. doi: 10.1371/journal.pone.0040814. Epub 2012 Jul 13.

Abstract

The contractile system of nonmuscle cells consists of interconnected actomyosin networks and bundles anchored to focal adhesions. The initiation of the contractile system assembly is poorly understood structurally and mechanistically, whereas system's maturation heavily depends on nonmuscle myosin II (NMII). Using platinum replica electron microscopy in combination with fluorescence microscopy, we characterized the structural mechanisms of the contractile system assembly and roles of NMII at early stages of this process. We show that inhibition of NMII by a specific inhibitor, blebbistatin, in addition to known effects, such as disassembly of stress fibers and mature focal adhesions, also causes transformation of lamellipodia into unattached ruffles, loss of immature focal complexes, loss of cytoskeleton-associated NMII filaments and peripheral accumulation of activated, but unpolymerized NMII. After blebbistatin washout, assembly of the contractile system begins with quick and coordinated recovery of lamellipodia and focal complexes that occurs before reappearance of NMII bipolar filaments. The initial formation of focal complexes and subsequent assembly of NMII filaments preferentially occurred in association with filopodial bundles and concave actin bundles formed by filopodial roots at the lamellipodial base. Over time, accumulating NMII filaments help to transform the precursor structures, focal complexes and associated thin bundles, into stress fibers and mature focal adhesions. However, semi-sarcomeric organization of stress fibers develops at much slower rate. Together, our data suggest that activation of NMII motor activity by light chain phosphorylation occurs at the cell edge and is uncoupled from NMII assembly into bipolar filaments. We propose that activated, but unpolymerized NMII initiates focal complexes, thus providing traction for lamellipodial protrusion. Subsequently, the mechanical resistance of focal complexes activates a load-dependent mechanism of NMII polymerization in association with attached bundles, leading to assembly of stress fibers and maturation of focal adhesions.

摘要

非肌肉细胞的收缩系统由相互连接的肌动球蛋白网络和束组成,并锚定在黏着斑上。收缩系统组装的起始在结构和机制上理解甚少,而系统的成熟则严重依赖于非肌肉肌球蛋白 II(NMII)。我们使用铂复制电子显微镜结合荧光显微镜,对收缩系统组装的结构机制以及 NMII 在该过程早期的作用进行了研究。我们发现,NMII 的特异性抑制剂 blebbistatin 的抑制作用,除了已知的作用,如应力纤维和成熟黏着斑的解聚,还会导致片状伪足转化为未附着的皱襞、不成熟黏着斑复合物的丢失、细胞骨架相关的 NMII 纤维的丢失以及激活但未聚合的 NMII 在周边的聚集。在 blebbistatin 洗脱后,收缩系统的组装开始于片状伪足和黏着斑复合物的快速和协调恢复,这发生在 NMII 双极纤维重新出现之前。最初的黏着斑复合物的形成和随后的 NMII 纤维的组装优先与丝状伪足束和由丝状伪足根形成的凹形肌动蛋白束相关联,这些结构位于片状伪足的基部。随着时间的推移,积累的 NMII 纤维有助于将前体结构、黏着斑复合物和相关的薄束转化为应力纤维和成熟的黏着斑。然而,应力纤维的半肌节组织的发展速度要慢得多。总之,我们的数据表明,NMII 马达活性的激活通过轻链磷酸化发生在细胞边缘,并且与 NMII 组装成双极纤维无关。我们提出,激活但未聚合的 NMII 启动黏着斑,从而为片状伪足的突起提供牵引力。随后,黏着斑复合物的机械阻力激活了一种负载依赖的 NMII 聚合机制,与附着的束相关联,导致应力纤维的组装和黏着斑的成熟。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/4c90/3396643/c89610189de5/pone.0040814.g001.jpg

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