ArticleProceedings of the National Academy of Sciences of the United States of America2012
Intermittent depolymerization of actin filaments is caused by photo-induced dimerization of actin protomers.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.
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Who cites it
26 citing papers in PubMed, 38 citations in OpenAlex.
- Molecular mechanisms of inorganic-phosphate release from the core and barbed end of actin filaments.Nature structural & molecular biology · 2023Article
- Celebrating 20 years of live single-actin-filament studies with five golden rules.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Actin filament oxidation by MICAL1 suppresses protections from cofilin-induced disassembly.EMBO reports · 2021Article
- Catastrophic actin filament bursting by cofilin, Aip1, and coronin.The Journal of biological chemistry · 2020Article
- The advantages of microfluidics to study actin biochemistry and biomechanics.Journal of muscle research and cell motility · 2020Review
- Mechanism of synergistic actin filament pointed end depolymerization by cyclase-associated protein and cofilin.Nature communications · 2019Article
- Cortactin stabilization of actin requires actin-binding repeats and linker, is disrupted by specific substitutions, and is independent of nucleotide state.The Journal of biological chemistry · 2018Article
- Article
- ADF/Cofilin Accelerates Actin Dynamics by Severing Filaments and Promoting Their Depolymerization at Both Ends.Current biology : CB · 2017Article
- Enhanced Depolymerization of Actin Filaments by ADF/Cofilin and Monomer Funneling by Capping Protein Cooperate to Accelerate Barbed-End Growth.Current biology : CB · 2017Article
- Oxidation of F-actin controls the terminal steps of cytokinesis.Nature communications · 2017Article
- Single Filaments to Reveal the Multiple Flavors of Actin.Biophysical journal · 2016Review
- Interferometric scattering microscopy and its combination with single-molecule fluorescence imaging.Nature protocols · 2016Article
- Covalent Ras Dimerization on Membrane Surfaces through Photosensitized Oxidation.Journal of the American Chemical Society · 2016Article
- Single-molecule visualization of a formin-capping protein 'decision complex' at the actin filament barbed end.Nature communications · 2015Article
- Single-molecule imaging of a three-component ordered actin disassembly mechanism.Nature communications · 2015Article
- Article
- The synthetic thyroid hormone, levothyroxine, protects cholinergic neurons in the hippocampus of naturally aged mice.Neural regeneration research · 2014Article
- Spire and Formin 2 synergize and antagonize in regulating actin assembly in meiosis by a ping-pong mechanism.PLoS biology · 2014Article
- Interaction of profilin with the barbed end of actin filaments.Biochemistry · 2013Article
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Authors and funding
8 authors at 4 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Actin, one of the most abundant proteins within eukaryotic cells, assembles into long filaments that form intricate cytoskeletal networks and are continuously remodelled via cycles of actin polymerization and depolymerization. These cycles are driven by ATP hydrolysis, a process that also acts to destabilize the filaments as they grow older. Recently, abrupt dynamical changes during the depolymerization of single filaments have been observed and seemed to imply that old filaments are more stable than young ones [Kueh HY, et al. (2008) Proc Natl Acad Sci USA 105:16531-16536]. Using improved experimental setups and quantitative theoretical analysis, we show that these abrupt changes represent actual pauses in depolymerization, unexpectedly caused by the photo-induced formation of actin dimers within the filaments. The stochastic dimerization process is triggered by random transitions of single, fluorescently labeled protomers. Each pause represents the delayed dissociation of a single actin dimer, and the statistics of these single molecule events can be determined by optical microscopy. Unlabeled actin filaments do not exhibit pauses in depolymerization, which implies that, in vivo, older filaments become destabilized by ATP hydrolysis, unless this aging effect is overcompensated by actin-binding proteins. The latter antagonism can now be systematically studied for single filaments using our combined experimental and theoretical method. Furthermore, the dimerization process discovered here provides a molecular switch, by which one can control the length of actin filaments via changes in illumination. This process could also be used to locally "freeze" the dynamics within networks of filaments.
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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.