Martin R Gill, Paul J Jarman, Vanessa Hearnden, Simon D Fairbanks, Marcella Bassetto, Hannes Maib, John Palmer, Kathryn R Ayscough, Jim A Thomas, Carl Smythe
{"title":"一种钌（II）多吡啶络合物能破坏肌动蛋白细胞骨架的组装并阻断细胞分裂。","authors":"Martin R Gill, Paul J Jarman, Vanessa Hearnden, Simon D Fairbanks, Marcella Bassetto, Hannes Maib, John Palmer, Kathryn R Ayscough, Jim A Thomas, Carl Smythe","doi":"10.1002/ange.202117449","DOIUrl":null,"url":null,"abstract":"<p><p>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 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.</p>","PeriodicalId":72198,"journal":{"name":"Angewandte Chemie (Weinheim an der Bergstrasse, Germany)","volume":null,"pages":null},"PeriodicalIF":0.0000,"publicationDate":"2022-07-04","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10947085/pdf/","citationCount":"0","resultStr":"{\"title\":\"A Ruthenium(II) Polypyridyl Complex Disrupts Actin Cytoskeleton Assembly and Blocks Cytokinesis.\",\"authors\":\"Martin R Gill, Paul J Jarman, Vanessa Hearnden, Simon D Fairbanks, Marcella Bassetto, Hannes Maib, John Palmer, Kathryn R Ayscough, Jim A Thomas, Carl Smythe\",\"doi\":\"10.1002/ange.202117449\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<p><p>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 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.</p>\",\"PeriodicalId\":72198,\"journal\":{\"name\":\"Angewandte Chemie (Weinheim an der Bergstrasse, Germany)\",\"volume\":null,\"pages\":null},\"PeriodicalIF\":0.0000,\"publicationDate\":\"2022-07-04\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10947085/pdf/\",\"citationCount\":\"0\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Angewandte Chemie (Weinheim an der Bergstrasse, Germany)\",\"FirstCategoryId\":\"1085\",\"ListUrlMain\":\"https://doi.org/10.1002/ange.202117449\",\"RegionNum\":0,\"RegionCategory\":null,\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"2022/5/9 0:00:00\",\"PubModel\":\"Epub\",\"JCR\":\"\",\"JCRName\":\"\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Angewandte Chemie (Weinheim an der Bergstrasse, Germany)","FirstCategoryId":"1085","ListUrlMain":"https://doi.org/10.1002/ange.202117449","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"2022/5/9 0:00:00","PubModel":"Epub","JCR":"","JCRName":"","Score":null,"Total":0}
A Ruthenium(II) Polypyridyl Complex Disrupts Actin Cytoskeleton Assembly and Blocks Cytokinesis.
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.
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