ArticleThe Journal of cell biology1986
The actin filament-severing domain of plasma gelsolin.
Article in The Journal of cell biology, 1986. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 51 papers.
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Who cites it
51 citing papers in PubMed, 173 citations in OpenAlex.
- Article
- Gold-Induced Cytokine (GOLDIC®) Therapy in the Management of Knee Osteoarthritis: An Observational Study.Cureus · 2023Article
- Contribution of mechanical homeostasis to epithelial-mesenchymal transition.Cellular oncology (Dordrecht, Netherlands) · 2022Review
- Traumatic injury is associated with reduced deoxyribonuclease activity and dysregulation of the actin scavenging system.Burns & trauma · 2021Article
- Cholesterol-Dependent Phase-Demixing in Lipid Bilayers as a Switch for the Activity of the Phosphoinositide-Binding Cytoskeletal Protein Gelsolin.Biochemistry · 2016Article
- Calcium-controlled conformational choreography in the N-terminal half of adseverin.Nature communications · 2015Article
- Global shapes of F-actin depolymerization-competent minimal gelsolins: insight into the role of g2-g3 linker in pH/Ca2+ insensitivity of the first half.The Journal of biological chemistry · 2013Article
- Regulatory role of the second gelsolin-like domain of Caenorhabditis elegans gelsolin-like protein 1 (GSNL-1) in its calcium-dependent conformation and actin-regulatory activities.Cytoskeleton (Hoboken, N.J.) · 2013Article
- Isolation, electron microscopy and 3D reconstruction of invertebrate muscle myofilaments.Methods (San Diego, Calif.) · 2012Review
- Calcium-sensitive activity and conformation of Caenorhabditis elegans gelsolin-like protein 1 are altered by mutations in the first gelsolin-like domain.The Journal of biological chemistry · 2011Article
- Gelsolin and non-muscle myosin IIA interact to mediate calcium-regulated collagen phagocytosis.The Journal of biological chemistry · 2011Article
- Article
- Head-head interaction characterizes the relaxed state of Limulus muscle myosin filaments.Journal of molecular biology · 2009Article
- Accelerators, Brakes, and Gears of Actin Dynamics in Dendritic Spines.The open neuroscience journal · 2009Article
- Blebbistatin stabilizes the helical order of myosin filaments by promoting the switch 2 closed state.Biophysical journal · 2008Article
- Decreased levels of the gelsolin plasma isoform in patients with rheumatoid arthritis.Arthritis research & therapy · 2008Article
- Gelsolin binds to polyphosphoinositide-free lipid vesicles and simultaneously to actin microfilaments.The Biochemical journal · 2005Article
- Topological assignment of the N-terminal extension of plasma gelsolin to the gelsolin surface.The Biochemical journal · 2005Article
- Visualizing the Ca2+-dependent activation of gelsolin by using synchrotron footprinting.Proceedings of the National Academy of Sciences of the United States of America · 2003Article
- Steered molecular dynamics simulations on the "tail helix latch" hypothesis in the gelsolin activation process.Biophysical journal · 2002Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Gelsolin, a multifunctional actin-modulating protein, has two actin-binding sites which may interact cooperatively. Native gelsolin requires micromolar Ca2+ for optimal binding of actin to both sites, and for expression of its actin filament-severing function. Recent work has shown that an NH2-terminal chymotryptic 17-kD fragment of human plasma gelsolin contains one of the actin-binding sites, and that this fragment binds to and severs actin filaments weakly irrespective of whether Ca2+ is present. The other binding site is Ca2+ sensitive, and is found in a chymotryptic peptide derived from the COOH-terminal two-thirds of plasma gelsolin; this fragment does not sever F-actin or accelerate the polymerization of actin. This paper documents that larger thermolysin-derived fragments encompassing the NH2-terminal half of gelsolin sever actin filaments as effectively as native plasma gelsolin, although in a Ca2+-insensitive manner. This result indicates that the NH2-terminal half of gelsolin is the actin-severing domain. The stringent Ca2+ requirement for actin severing found in intact gelsolin is not due to a direct effect of Ca2+ on the severing domain, but indirectly through an effect on domains in the COOH-terminal half of the molecule to allow exposure of both actin-binding sites.
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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.