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肌动蛋白束的纳米力学和组织受大分子拥挤和静电相互作用的调节。

Actin Bundle Nanomechanics and Organization Are Modulated by Macromolecular Crowding and Electrostatic Interactions.

作者信息

Castaneda Nicholas, Feuillie Cecile, Molinari Michael, Kang Ellen Hyeran

机构信息

NanoScience Technology Center, University of Central Florida, Orlando, FL, United States.

Burnett School of Biomedical Sciences, College of Medicine, University of Central Florida, Orlando, FL, United States.

出版信息

Front Mol Biosci. 2021 Nov 26;8:760950. doi: 10.3389/fmolb.2021.760950. eCollection 2021.

DOI:10.3389/fmolb.2021.760950
PMID:34901154
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC8662701/
Abstract

The structural and mechanical properties of actin bundles are essential to eukaryotic cells, aiding in cell motility and mechanical support of the plasma membrane. Bundle formation occurs in crowded intracellular environments composed of various ions and macromolecules. Although the roles of cations and macromolecular crowding in the mechanics and organization of actin bundles have been independently established, how changing both intracellular environmental conditions influence bundle mechanics at the nanoscale has yet to be established. Here we investigate how electrostatics and depletion interactions modulate the relative Young's modulus and height of actin bundles using atomic force microscopy. Our results demonstrate that cation- and depletion-induced bundles display an overall reduction of relative Young's modulus depending on either cation or crowding concentrations. Furthermore, we directly measure changes to cation- and depletion-induced bundle height, indicating that bundles experience alterations to filament packing supporting the reduction to relative Young's modulus. Taken together, our work suggests that electrostatic and depletion interactions may act counteractively, impacting actin bundle nanomechanics and organization.

摘要

肌动蛋白束的结构和力学特性对真核细胞至关重要,有助于细胞运动和对质膜的机械支撑。束的形成发生在由各种离子和大分子组成的拥挤细胞内环境中。尽管阳离子和大分子拥挤在肌动蛋白束的力学和组织中的作用已分别得到证实,但改变这两种细胞内环境条件如何在纳米尺度上影响束的力学仍有待确定。在这里,我们使用原子力显微镜研究静电和耗尽相互作用如何调节肌动蛋白束的相对杨氏模量和高度。我们的结果表明,阳离子诱导和耗尽诱导的束显示出相对杨氏模量的总体降低,这取决于阳离子或拥挤浓度。此外,我们直接测量了阳离子诱导和耗尽诱导的束高度的变化,表明束经历了细丝堆积的改变,支持相对杨氏模量的降低。综上所述,我们的工作表明静电和耗尽相互作用可能起反作用,影响肌动蛋白束的纳米力学和组织。

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本文引用的文献

1
Crowding tunes the organization and mechanics of actin bundles formed by crosslinking proteins.拥挤现象调节了交联蛋白形成的肌动蛋白束的组织和力学性质。
FEBS Lett. 2021 Jan;595(1):26-40. doi: 10.1002/1873-3468.13949. Epub 2020 Oct 21.
2
The elastic properties and deformation mechanisms of actin filament networks crosslinked by filamins.由细丝蛋白交联的肌动蛋白丝网络的弹性特性和变形机制。
J Mech Behav Biomed Mater. 2020 Dec;112:104075. doi: 10.1016/j.jmbbm.2020.104075. Epub 2020 Sep 6.
3
Gelsolin-mediated actin filament severing in crowded environments.
胶溶蛋白介导的拥挤环境下的肌动蛋白丝断裂。
Biochem Biophys Res Commun. 2020 Nov 19;532(4):548-554. doi: 10.1016/j.bbrc.2020.08.041. Epub 2020 Sep 6.
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Force Production by a Bundle of Growing Actin Filaments Is Limited by Its Mechanical Properties.一束生长中的肌动蛋白丝产生的力受其机械性能限制。
Biophys J. 2020 Jan 7;118(1):182-192. doi: 10.1016/j.bpj.2019.10.039. Epub 2019 Nov 6.
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Crowding Induces Entropically-Driven Changes to DNA Dynamics That Depend on Crowder Structure and Ionic Conditions.拥挤诱导由熵驱动的DNA动力学变化,这种变化取决于拥挤剂结构和离子条件。
Front Phys. 2018;6. doi: 10.3389/fphy.2018.00053. Epub 2018 Jun 5.
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Spatial high resolution of actin filament organization by PeakForce atomic force microscopy.利用原子力显微镜的峰值力模式获得肌动蛋白丝组织的空间高分辨率。
Cell Prolif. 2020 Jan;53(1):e12670. doi: 10.1111/cpr.12670. Epub 2019 Sep 30.
7
Actin Filament Mechanics and Structure in Crowded Environments.在拥挤环境中肌动蛋白丝的力学和结构。
J Phys Chem B. 2019 Apr 4;123(13):2770-2779. doi: 10.1021/acs.jpcb.8b12320. Epub 2019 Mar 19.
8
Cations Modulate Actin Bundle Mechanics, Assembly Dynamics, and Structure.阳离子调节肌动蛋白束力学、组装动力学和结构。
J Phys Chem B. 2018 Apr 12;122(14):3826-3835. doi: 10.1021/acs.jpcb.8b00663. Epub 2018 Apr 2.
9
Adaptive Response of Actin Bundles under Mechanical Stress.机械应力作用下肌动蛋白束的适应性反应。
Biophys J. 2017 Sep 5;113(5):1072-1079. doi: 10.1016/j.bpj.2017.07.017.
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Soft interactions and crowding.软相互作用与拥挤效应
Biophys Rev. 2013 Jun;5(2):187-194. doi: 10.1007/s12551-013-0104-4. Epub 2013 Feb 21.