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.
authors.affiliation: Department of Chemistry and Biochemistry, University of California, Los Angeles, California 90095, USA. sharmas@ucla.edu
authors.forename: Shivani
authors.initials: S
authors.lastname: Sharma
authors.forename: Elena E
authors.initials: EE
authors.lastname: Grintsevich
authors.forename: Martin L
authors.initials: ML
authors.lastname: Phillips
authors.forename: Emil
authors.initials: E
authors.lastname: Reisler
authors.forename: James K
authors.initials: JK
authors.lastname: Gimzewski
mesh_terms: D000199:Actins / Q000737:chemistry* / Q000648:ultrastructure*; D001665:Binding Sites; D018625:Microscopy, Atomic Force / Q000379:methods*; D009479:Neuropeptides / Q000737:chemistry*; D011485:Protein Binding; D011487:Protein Conformation
chemical_list: D000199:Actins; D009479:Neuropeptides; C053386:drebrins