| Literature DB >> 26228148 |
David B Heisler1, Elena Kudryashova2, Dmitry O Grinevich3, Cristian Suarez4, Jonathan D Winkelman4, Konstantin G Birukov5, Sainath R Kotha6, Narasimham L Parinandi6, Dimitrios Vavylonis7, David R Kovar8, Dmitri S Kudryashov9.
Abstract
The actin cross-linking domain (ACD) is an actin-specific toxin produced by several pathogens, including life-threatening spp. of Vibrio cholerae, Vibrio vulnificus, and Aeromonas hydrophila. Actin cross-linking by ACD is thought to lead to slow cytoskeleton failure owing to a gradual sequestration of actin in the form of nonfunctional oligomers. Here, we found that ACD converted cytoplasmic actin into highly toxic oligomers that potently "poisoned" the ability of major actin assembly proteins, formins, to sustain actin polymerization. Thus, ACD can target the most abundant cellular protein by using actin oligomers as secondary toxins to efficiently subvert cellular functions of actin while functioning at very low doses.Entities:
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Year: 2015 PMID: 26228148 PMCID: PMC4648357 DOI: 10.1126/science.aab4090
Source DB: PubMed Journal: Science ISSN: 0036-8075 Impact factor: 47.728