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
收藏
页码：825 / 827
页数：3
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