Atomic Force Microscopy Reveals Drebrin Induced Remodeling of F-Actin with Subnanometer Resolution

被引：74

作者：

Sharma, Shivani ^{[1
,2
]}

Grintsevich, Elena E. ^{[1
]}

Phillips, Martin L. ^{[1
]}

Reisler, Emil ^{[1
,3
]}

Gimzewski, James K. ^{[1
,2
,4
]}

机构：

[1] Univ Calif Los Angeles, Dept Chem & Biochem, Los Angeles, CA 90095 USA

[2] Univ Calif Los Angeles, Calif NanoSyst Inst, Los Angeles, CA 90095 USA

[3] Univ Calif Los Angeles, Inst Mol Biol, Los Angeles, CA 90095 USA

[4] Natl Inst Mat Sci, Int Ctr Mat Nanoarchitecton Satellite MANA, Tsukuba, Ibaraki 3050047, Japan

来源：

NANO LETTERS | 2011年 / 11卷 / 02期

关键词：

F-actin remodeling; drebrin; AFM; neuron cytoskeleton; nanofilament mechanics; FILAMENTS; FLEXIBILITY; DISRUPTION; DISORDERS; DYNAMICS; BINDING; PROTEIN; MODEL;

D O I：

10.1021/nl104159v

中图分类号：

O6 [化学];

学科分类号：

0703 ;

摘要：

We show by high-resolution atomic force microscopy analysis that drebrin A (a major neuronal actin binding protein) induced F-actin structural and mechanical remodeling involves significant changes in helical twist and filament stiffness (+55% persistence length). These results provide evidence of a unique mechanical role of drebrin in the dendrites, contribute to current molecular-level understanding of the properties of the neuronal cytoskeleton, and reflect the role of biomechanics at the nanoscale, to modulate nanofilament-structure assemblies such as F-actin.

引用

页码：825 / 827

页数：3

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