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

Shivani Sharma; Elena E. Grintsevich; Martin L. Phillips; Emil Reisler; James K. Gimzewski

doi:10.1021/nl104159v

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

Shivani Sharma^*, Elena E. Grintsevich, Martin L. Phillips, Emil Reisler, James K. Gimzewski

^*Corresponding author for this work

School of Physics

Research output: Contribution to journal › Article (Academic Journal) › peer-review

88 Citations (Scopus)

Abstract

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.

Original language	English
Pages (from-to)	825-827
Number of pages	3
Journal	Nano Letters
Volume	11
Issue number	2
DOIs	https://doi.org/10.1021/nl104159v
Publication status	Published - Feb 2011

Keywords

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

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@article{973206549d4746cbb3689f2651faf9e8,

title = "Atomic Force Microscopy Reveals Drebrin Induced Remodeling of F-Actin with Subnanometer Resolution",

abstract = "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.",

keywords = "F-actin remodeling, drebrin, AFM, neuron cytoskeleton, nanofilament mechanics, FILAMENTS, FLEXIBILITY, DISRUPTION, DISORDERS, DYNAMICS, BINDING, PROTEIN, MODEL",

author = "Shivani Sharma and Grintsevich, \{Elena E.\} and Phillips, \{Martin L.\} and Emil Reisler and Gimzewski, \{James K.\}",

year = "2011",

month = feb,

doi = "10.1021/nl104159v",

language = "English",

volume = "11",

pages = "825--827",

journal = "Nano Letters",

issn = "1530-6984",

publisher = "American Chemical Society",

number = "2",

}

TY - JOUR

T1 - Atomic Force Microscopy Reveals Drebrin Induced Remodeling of F-Actin with Subnanometer Resolution

AU - Sharma, Shivani

AU - Grintsevich, Elena E.

AU - Phillips, Martin L.

AU - Reisler, Emil

AU - Gimzewski, James K.

PY - 2011/2

Y1 - 2011/2

N2 - 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.

AB - 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.

KW - F-actin remodeling

KW - drebrin

KW - AFM

KW - neuron cytoskeleton

KW - nanofilament mechanics

KW - FILAMENTS

KW - FLEXIBILITY

KW - DISRUPTION

KW - DISORDERS

KW - DYNAMICS

KW - BINDING

KW - PROTEIN

KW - MODEL

U2 - 10.1021/nl104159v

DO - 10.1021/nl104159v

M3 - Article (Academic Journal)

C2 - 21175132

SN - 1530-6984

VL - 11

SP - 825

EP - 827

JO - Nano Letters

JF - Nano Letters

IS - 2

ER -

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

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Keywords

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