Gill, M.R., Jarman, P.J., Hearnden, V. et al. (6 more authors) (2022) A ruthenium(II) polypyridyl complex disrupts actin cytoskeleton assembly and blocks cytokinesis. Angewandte Chemie International Edition, 61 (27). e202117449. ISSN 1433-7851
Abstract
The dinuclear Ru(II) complex [(Ru(phen) 2 ) 2 (tpphz)] 4+ (phen = 1,10-phenanthroline, tpphz = tetrapyridophenazine) “RuRuPhen” blocks the transformation of G-actin to F-actin filaments with no disassembly of pre-formed F-actin. Molecular docking studies indicate multiple RuRuPhen molecules bind to the surface of G-actin but not the binding pockets of established actin polymerisation inhibitors. In cells, addition of RuRuPhen causes rapid disruption to actin stress fibre organisation, compromising actomyosin contractility and cell motility, due to this effect RuRuPhen interferes with late-stage cytokinesis. Immunofluorescent microscopy reveals that RuRuPhen causes cytokinetic abscission failure by interfering with ESCRT complex recruitment
Metadata
Item Type: | Article |
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Authors/Creators: |
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Copyright, Publisher and Additional Information: | © 2022 The Authors. Angewandte Chemie International Edition published by Wiley-VCH GmbH. This is an open access article under the terms of the Creative Commons Attribution License, (http://creativecommons.org/licenses/by/4.0/) which permits use, distribution and reproduction in any medium, provided the original work is properly cited. |
Keywords: | ruthenium; actin; cytokinesis; cytoskeleton; polypyridyl complexes |
Dates: |
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Institution: | The University of Sheffield |
Academic Units: | The University of Sheffield > Faculty of Science (Sheffield) > Department of Chemistry (Sheffield) |
Funding Information: | Funder Grant number ENGINEERING AND PHYSICAL SCIENCE RESEARCH COUNCIL EP/M015572/1 |
Depositing User: | Symplectic Sheffield |
Date Deposited: | 27 Apr 2022 15:58 |
Last Modified: | 24 Feb 2023 10:37 |
Status: | Published |
Publisher: | Wiley |
Refereed: | Yes |
Identification Number: | 10.1002/anie.202117449 |
Related URLs: | |
Open Archives Initiative ID (OAI ID): | oai:eprints.whiterose.ac.uk:186092 |