The LINC-anchored actin cap connects the extracellular milieu to the nucleus for ultrafast mechanotransduction.
The LINC-anchored actin cap connects the extracellular milieu to the nucleus for ultrafast mechanotransduction.
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DOI：
10.1038/srep01087
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发表时间：
2013
影响因子：
4.6
通讯作者：
Wirtz, Denis
中科院分区：
文献类型：
--
作者：
Chambliss, Allison B.;Khatau, Shyam B.;Erdenberger, Nicholas;Robinson, D. Kyle;Hodzic, Didier;Longmore, Gregory D.;Wirtz, Denis
细胞通过其细胞骨架持续感知和响应外部机械力。在这里，我们表明，只有一个小的子集的肌动蛋白纤维，那些形成核周肌动蛋白帽，包裹在细胞核周围，形成在低生理机械应力粘附成纤维细胞。虽然传统的基底应力纤维形成仅超过0.5达因/厘米2的阈值剪切应力，肌动蛋白帽纤维形成的剪切应力低50倍，数量级快于生化刺激。 这种快速的差异反应是唯一介导的粘着斑蛋白zyxin在低剪切应力和肌动蛋白帽的肌动球蛋白纤维。我们确定了核纤层蛋白A/C和细胞核骨架（LINC）分子nesprin 2巨人和nesprin 3，它的锚肌动蛋白帽纤维的细胞核的连接器的其他角色。这些结果表明，一个相互关联的物理通路的mechanotransduction，从细胞外环境的核。
Cells continuously sense and respond to external mechanical forces through their cytoskeleton. Here we show that only a small subset of actin fibers, those forming the perinuclear actin cap that wraps around the nucleus, form in response to low physiological mechanical stresses in adherent fibroblasts. While conventional basal stress fibers form only past a threshold shear stress of 0.5 dyn/cm2, actin-cap fibers are formed at shear stresses 50 times lower and orders-of-magnitude faster than biochemical stimulation. This fast differential response is uniquely mediated by focal adhesion protein zyxin at low shear stress and actomyosin fibers of the actin cap. We identify additional roles for lamin A/C of the nuclear lamina and linkers of nucleus to cytoskeleton (LINC) molecules nesprin2giant and nesprin3, which anchor actin cap fibers to the nucleus. These results suggest an interconnected physical pathway for mechanotransduction, from the extracellular milieu to the nucleus.
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影响因子：
56.9
作者：
Campbell, JJ;Hedrick, J;Butcher, EC
通讯作者：
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影响因子：
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作者：
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通讯作者：
Wirtz, Denis
DOI：
10.1152/ajpheart.00369.2009
发表时间：
2009-10-01
影响因子：
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作者：
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作者：
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通讯作者：
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影响因子：
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作者：
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