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A Ruthenium(II) Polypyridyl Complex Disrupts Actin Cytoskeleton Assembly and Blocks Cytokinesis

Martin Gill Orcid Logo, Paul J. Jarman, Vanessa Hearnden, Simon D Fairbanks, Marcella Bassetto, Hannes Maib, John Palmer, Kathryn R. Ayscough, Jim A. Thomas Orcid Logo, Carl Smythe

Angewandte Chemie International Edition, Volume: 61, Issue: 27, Start page: e202117449

Swansea University Authors: Martin Gill Orcid Logo, Marcella Bassetto

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DOI (Published version): 10.1002/anie.202117449

Abstract

The dinuclear RuII complex [(Ru(phen)2)2(tpphz)]4+ binds to G-actin monomers, preventing assembly into F-actin. This inhibits actin fibre assemblies within live cells and causes disruption to late cytokinesis by interfering with the function of endosomal sorting complexes required for transport (ESC...

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Published in: Angewandte Chemie International Edition
ISSN: 1433-7851 1521-3773
Published: Wiley 2022
Online Access: Check full text

URI: https://cronfa.swan.ac.uk/Record/cronfa59895
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Abstract: The dinuclear RuII complex [(Ru(phen)2)2(tpphz)]4+ binds to G-actin monomers, preventing assembly into F-actin. This inhibits actin fibre assemblies within live cells and causes disruption to late cytokinesis by interfering with the function of endosomal sorting complexes required for transport (ESCRT) during abscission. These results reveal new possibilities for metal complexes as biomedical tools and novel therapeutic leads.
Keywords: Actin ;Cytokinesis; Cytoskeleton; Polypyridyl Complexes; Ruthenium
College: Faculty of Science and Engineering
Funders: Medical Research Council. Grant Number: R/162348
Issue: 27
Start Page: e202117449