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


ABSTRACT: The dinuclear RuII complex [(Ru(phen)2 )2 (tpphz)]4+ (phen=1,10-phenanthroline, tpphz=tetrapyridophenazine) "RuRuPhen" blocks the transformation of G-actin monomers 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 endosomal sorting complexes required for transport (ESCRT) complex recruitment.

SUBMITTER: Gill MR 

PROVIDER: S-EPMC9323417 | biostudies-literature | 2022 Jul

REPOSITORIES: biostudies-literature

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

Gill Martin R MR   Jarman Paul J PJ   Hearnden Vanessa V   Fairbanks Simon D SD   Bassetto Marcella M   Maib Hannes H   Palmer John J   Ayscough Kathryn R KR   Thomas Jim A JA   Smythe Carl C  

Angewandte Chemie (International ed. in English) 20220503 27


The dinuclear Ru<sup>II</sup> complex [(Ru(phen)<sub>2</sub> )<sub>2</sub> (tpphz)]<sup>4+</sup> (phen=1,10-phenanthroline, tpphz=tetrapyridophenazine) "RuRuPhen" blocks the transformation of G-actin monomers 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  ...[more]

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