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Title: Vinculin binding angle in podosomes revealed by high resolution microscopy
Authors: Walde, M.Monypenny, J.Heintzmann, R.Jones, G.E.Cox, S.
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Issue Date: 2014
Published in: PLoS ONE Vol. 9 (2014), No. 2
Publisher: San Francisco, CA : Public Library of Science
Abstract: Podosomes are highly dynamic actin-rich adhesive structures formed predominantly by cells of the monocytic lineage, which degrade the extracellular matrix. They consist of a core of F-actin and actin-regulating proteins, surrounded by a ring of adhesion-associated proteins such as vinculin. We have characterised the structure of podosomes in macrophages, particularly the structure of the ring, using three super-resolution fluorescence microscopy techniques: stimulated emission depletion microscopy, structured illumination microscopy and localisation microscopy. Rather than being round, as previously assumed, we found the vinculin ring to be created from relatively straight strands of vinculin, resulting in a distinctly polygonal shape. The strands bind preferentially at angles between 116° and 135°. Furthermore, adjacent vinculin strands are observed nucleating at the corners of the podosomes, suggesting a mechanism for podosome growth.
Keywords: actin; paxillin; talin; vinculin; article; cell composition; cell growth; cell membrane; cell structure; cellular distribution; controlled study; cytoskeleton; depletion; fluorescence microscopy; human; human cell; intermethod comparison; localisation microscopy; macrophage; podosome; protein binding; protein structure; stimulated emission depletion microscopy; structured illumination microscopy; Actin Cytoskeleton; Actins; Cell Adhesion; Cell Line; Cell Movement; Humans; Image Processing, Computer-Assisted; Macrophages; Microscopy; Microscopy, Fluorescence; Talin; Vinculin
DDC: 570
License: CC BY 3.0 Unported
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