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Title: Effects of basic calponin on the flexural mechanics and stability of F-actin.
Authors: Jensen, MH
Watt, J
Hodgkinson, JL
Gallant, C
Appel, S
El-Mezgueldi, M
Angelini, TE
Morgan, KG
Lehman, W
Moore, JR
First Published: Jan-2012
Citation: CYTOSKELETON (HOBOKEN), 2012, 69 (1), pp. 49-58
Abstract: The cellular actin cytoskeleton plays a central role in the ability of cells to properly sense, propagate, and respond to external stresses and other mechanical stimuli. Calponin, an actin-binding protein found both in muscle and non-muscle cells, has been implicated in actin cytoskeletal organization and regulation. In this work, we studied the mechanical and structural interaction of actin with basic calponin, a differentiation marker in smooth muscle cells, on a single filament level. We imaged fluorescently labeled thermally fluctuating actin filaments and found that at moderate calponin binding densities, actin filaments were more flexible, evident as a reduction in persistence length from 8.0 to 5.8 μm. When calponin-decorated actin filaments were subjected to shear, we observed a marked reduction of filament lengths after decoration with calponin, which we argue was due to shear-induced filament rupture rather than depolymerization. This increased shear susceptibility was exacerbated with calponin concentration. Cryo-electron microscopy results confirmed previously published negative stain electron microscopy results and suggested alterations in actin involving actin subdomain 2. A weakening of F-actin intermolecular association is discussed as the underlying cause of the observed mechanical perturbations.
DOI Link: 10.1002/cm.20548
eISSN: 1949-3592
Type: Journal Article
Appears in Collections:Published Articles, Dept. of Biochemistry

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