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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.

SUBMITTER: Sharma S

PROVIDER: S-EPMC3670797 | biostudies-literature | 2011 Feb

REPOSITORIES: biostudies-literature

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Atomic force microscopy reveals drebrin induced remodeling of f-actin with subnanometer resolution.

Sharma Shivani S Grintsevich Elena E EE Phillips Martin L ML Reisler Emil E Gimzewski James K JK

Nano letters 20101222 2

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 nan ...[more]

PMID: 21175132

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