ArticleBiophysical journal2004
Formation and destabilization of actin filaments with tetramethylrhodamine-modified actin.
Article in Biophysical journal, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
19 citing papers in PubMed, 33 citations in OpenAlex.
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- Allosteric regulation controls actin-bundling properties of human plastins.Nature structural & molecular biology · 2022Article
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- Biochemical Activities of the Wiskott-Aldrich Syndrome Homology Region 2 Domains of Sarcomere Length Short (SALS) Protein.The Journal of biological chemistry · 2016Article
- ACTIN-DIRECTED TOXIN. ACD toxin-produced actin oligomers poison formin-controlled actin polymerization.Science (New York, N.Y.) · 2015Article
- Disulfide cross-linked antiparallel actin dimer.Biochemistry · 2013Article
- mDia1 and formins: screw cap of the actin filament.Biophysics (Nagoya-shi, Japan) · 2012Review
- Differential effects of caldesmon on the intermediate conformational states of polymerizing actin.The Journal of biological chemistry · 2010Article
- Differential regulation of actin polymerization and structure by yeast formin isoforms.The Journal of biological chemistry · 2009Article
- Mechanical distortion of single actin filaments induced by external force: detection by fluorescence imaging.Biophysical journal · 2009Article
- Connecting actin monomers by iso-peptide bond is a toxicity mechanism of the Vibrio cholerae MARTX toxin.Proceedings of the National Academy of Sciences of the United States of America · 2008Article
- Stochastic simulation of actin dynamics reveals the role of annealing and fragmentation.Journal of theoretical biology · 2008Article
- Actin hydrophobic loop 262-274 and filament nucleation and elongation.Journal of molecular biology · 2008Article
- The crystal structure of a cross-linked actin dimer suggests a detailed molecular interface in F-actin.Proceedings of the National Academy of Sciences of the United States of America · 2005Article
- BRCA2 BRC motifs bind RAD51-DNA filaments.Proceedings of the National Academy of Sciences of the United States of America · 2005Article
- Actin polymerization kinetics, cap structure, and fluctuations.Proceedings of the National Academy of Sciences of the United States of America · 2005Article
- Actin-destabilizing factors disrupt filaments by means of a time reversal of polymerization.Proceedings of the National Academy of Sciences of the United States of America · 2004Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Actin labeling at Cys(374) with tethramethylrhodamine derivatives (TMR-actin) has been widely used for direct observation of the in vitro filaments growth, branching, and treadmilling, as well as for the in vivo visualization of actin cytoskeleton. The advantage of TMR-actin is that it does not lock actin in filaments (as rhodamine-phalloidin does), possibly allowing for its use in investigating the dynamic assembly behavior of actin polymers. Although it is established that TMR-actin alone is polymerization incompetent, the impact of its copolymerization with unlabeled actin on filament structure and dynamics has not been tested yet. In this study, we show that TMR-actin perturbs the filaments structure when copolymerized with unlabeled actin; the resulting filaments are more fragile and shorter than the control filaments. Due to the increased severing of copolymer filaments, TMR-actin accelerates the polymerization of unlabeled actin in solution also at mole ratios lower than those used in most fluorescence microscopy experiments. The destabilizing and severing effect of TMR-actin is countered by filament stabilizing factors, phalloidin, S1, and tropomyosin. These results point to an analogy between the effects of TMR-actin and severing proteins on F-actin, and imply that TMR-actin may be inappropriate for investigations of actin filaments dynamics.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.