ArticleProceedings of the National Academy of Sciences of the United States of America2005
Gelsolin mediates calcium-dependent disassembly of Listeria actin tails.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed, 41 citations in OpenAlex.
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- Oligodendrocyte calcium signaling promotes actin-dependent myelin sheath extension.Nature communications · 2024Article
- The role of the cytoskeleton in fibrotic diseases.Frontiers in cell and developmental biology · 2024Review
- MSN, MWCNT and ZnO nanoparticle-induced CHO-K1 cell polarisation is linked to cytoskeleton ablation.Journal of nanobiotechnology · 2021Article
- Cellular Mechanisms of NETosis.Annual review of cell and developmental biology · 2020Review
- Plasma gelsolin levels in patients with psoriatic arthritis: a possible novel marker.Clinical rheumatology · 2020Article
- Active contractions in single suspended epithelial cells.European biophysics journal : EBJ · 2014Article
- Local cytosolic Ca2+ elevations are required for stromal interaction molecule 1 (STIM1) de-oligomerization and termination of store-operated Ca2+ entry.The Journal of biological chemistry · 2011Article
- BCL2 inhibits cell adhesion, spreading, and motility by enhancing actin polymerization.Cell research · 2010Article
- VSOP/Hv1 proton channels sustain calcium entry, neutrophil migration, and superoxide production by limiting cell depolarization and acidification.The Journal of experimental medicine · 2010Article
- Villin severing activity enhances actin-based motility in vivo.Molecular biology of the cell · 2007Article
- Stimulation of actin polymerization by filament severing.Biophysical journal · 2006Article
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Authors and funding
10 authors at 4 institutions in 2 countries.
Funding
Abstract
The role of intracellular Ca2+ in the regulation of actin filament assembly and disassembly has not been clearly defined. We show that reduction of intracellular free Ca2+ concentration ([Ca2+]i) to <40 nM in Listeria monocytogenes-infected, EGFP-actin-transfected Madin-Darby canine kidney cells results in a 3-fold lengthening of actin filament tails. This increase in tail length is the consequence of marked slowing of the actin filament disassembly rate, without a significant change in assembly rate. The Ca2+-sensitive actin-severing protein gelsolin concentrates in the Listeria rocket tails at normal resting [Ca2+]i and disassociates from the tails when [Ca2+]i is lowered. Reduction in [Ca2+]i also blocks the severing activity of gelsolin, but not actin-depolymerizing factor (ADF)/cofilin microinjected into Listeria-infected cells. In Xenopus extracts, Listeria tail lengths are also calcium-sensitive, markedly shortening on addition of calcium. Immunodepletion of gelsolin, but not Xenopus ADF/cofilin, eliminates calcium-sensitive actin-filament shortening. Listeria tail length is also calcium-insensitive in gelsolin-null mouse embryo fibroblasts. We conclude that gelsolin is the primary Ca2+-sensitive actin filament recycling protein in the cell and is capable of enhancing Listeria actin tail disassembly at normal resting [Ca2+]i (145 nM). These experiments illustrate the unique and complementary functions of gelsolin and ADF/cofilin in the recycling of actin filaments.
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