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  The Architecture of Traveling Actin Waves Revealed by Cryo-Electron Tomography

Jasnin, M., Beck, F., Ecke, M., Fukuda, Y., Martinez Sanchez, A., Baumeister, W., et al. (2019). The Architecture of Traveling Actin Waves Revealed by Cryo-Electron Tomography. STRUCTURE, 27(8), 1211-1223.e5. doi:10.1016/j.str.2019.05.009.

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Item Permalink: http://hdl.handle.net/21.11116/0000-0005-88A0-C Version Permalink: http://hdl.handle.net/21.11116/0000-0005-88A1-B
Genre: Journal Article

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 Creators:
Jasnin, Marion1, Author              
Beck, Florian1, Author              
Ecke, Mary2, Author              
Fukuda, Yoshiyuki1, Author              
Martinez Sanchez, Antonio1, Author              
Baumeister, Wolfgang1, Author              
Gerisch, Günther2, Author              
Affiliations:
1Baumeister, Wolfgang / Molecular Structural Biology, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565142              
2Gerisch, Günther / Cell Dynamics, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565149              

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Free keywords: ARP2/3 COMPLEX; DIRECT VISUALIZATION; MEMBRANE; DYNAMICS; CELLS; FILAMENTS; NETWORKS; PROTEIN; ORGANIZATION; ELONGATIONBiochemistry & Molecular Biology; Biophysics; Cell Biology;
 Abstract: Actin waves are dynamic supramolecular structures involved in cell migration, cytokinesis, adhesion, and neurogenesis. Although wave-like propagation of actin networks is a widespread phenomenon, the actin architecture underlying wave propagation remained unknown. In situ cryo-electron tomography of Dictyostelium cells unveils the wave architecture and provides evidence for wave progression by de novo actin nucleation. Subtomogram averaging reveals the structure of Arp2/3 complex-mediated branch junctions in their native state, and enables quantitative analysis of the 3D organization of branching within the waves. We find an excess of branches directed toward the substrate-attached membrane, and tent-like structures at sites of branch clustering. Fluorescence imaging shows that Arp2/3 clusters follow accumulation of the elongation factor VASP. We propose that filament growth toward the membrane lifts up the actin network as the wave propagates, until depolymerization of oblique filaments at the back causes the collapse of horizontal filaments into a compact layer.

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Language(s): eng - English
 Dates: 2019
 Publication Status: Published in print
 Pages: 18
 Publishing info: -
 Table of Contents: -
 Rev. Method: Peer
 Identifiers: ISI: 000478962400006
DOI: 10.1016/j.str.2019.05.009
 Degree: -

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Title: STRUCTURE
Source Genre: Journal
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Publ. Info: 50 HAMPSHIRE ST, FLOOR 5, CAMBRIDGE, MA 02139 USA : CELL PRESS
Pages: - Volume / Issue: 27 (8) Sequence Number: - Start / End Page: 1211 - 1223.e5 Identifier: ISSN: 0969-2126