ArticleThe EMBO journal2004
Structure of the N-terminal half of gelsolin bound to actin: roles in severing, apoptosis and FAF.
Article in The EMBO journal, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 62 papers.
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Who cites it
62 citing papers in PubMed, 137 citations in OpenAlex.
- The structure of an actin nucleus stabilized by villin.Science advances · 2025Article
- Microscopic and structural observations of actin filament capping and severing by cytochalasin D.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Mechanism of actin filament severing and capping by gelsolin.Nature structural & molecular biology · 2025Article
- Electrical Forces Improve Memory in Old Age.Reviews of physiology, biochemistry and pharmacology · 2025Review
- Cytoskeleton-associated gelsolin responds to the midgut distention process in saline meal-fed Aedes aegypti and affects arbovirus dissemination from the midgut.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2024Article
- The therapeutic potential of gelsolin in attenuating cytokine storm, ARDS, and ALI in severe COVID-19.Frontiers in pharmacology · 2024Review
- A census of actin-associated proteins in humans.Frontiers in cell and developmental biology · 2023Article
- Enzymatically dissociated muscle fibers display rapid dedifferentiation and impaired mitochondrial calcium control.iScience · 2022Article
- Actin-Binding Proteins in Cardiac Hypertrophy.Cells · 2022Review
- Structural and biochemical evidence for the emergence of a calcium-regulated actin cytoskeleton prior to eukaryogenesis.Communications biology · 2022Article
- The p53 and Calcium Regulated Actin Rearrangement in Model Cells.International journal of molecular sciences · 2022Article
- Actin-Associated Proteins and Small Molecules Targeting the Actin Cytoskeleton.International journal of molecular sciences · 2022Review
- Zero-mode waveguides visualize the first steps during gelsolin-mediated actin filament formation.Biophysical journal · 2022Article
- Novel inter-domain CaJournal of muscle research and cell motility · 2020Review
- The Activities of the Gelsolin Homology Domains of Flightless-I in Actin Dynamics.Frontiers in molecular biosciences · 2020Article
- The role of gelsolin domain 3 in familial amyloidosis (Finnish type).Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- ATP competes with PIP2 for binding to gelsolin.PloS one · 2018Article
- Advillin acts upstream of phospholipase C ϵ1 in steroid-resistant nephrotic syndrome.The Journal of clinical investigation · 2017Article
- Gelsolin dysfunction causes photoreceptor loss in induced pluripotent cell and animal retinitis pigmentosa models.Nature communications · 2017Article
- Visualizing Temperature Mediated Activation of Gelsolin and Its Deactivation By PipScientific reports · 2017Article
2 more citing papers are in PubMed but not listed here.
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The actin filament-severing functionality of gelsolin resides in its N-terminal three domains (G1-G3). We have determined the structure of this fragment in complex with an actin monomer. The structure reveals the dramatic domain rearrangements that activate G1-G3, which include the replacement of interdomain interactions observed in the inactive, calcium-free protein by new contacts to actin, and by a novel G2-G3 interface. Together, these conformational changes are critical for actin filament severing, and we suggest that their absence leads to the disease Finnish-type familial amyloidosis. Furthermore, we propose that association with actin drives the calcium-independent activation of isolated G1-G3 during apoptosis, and that a similar mechanism operates to activate native gelsolin at micromolar levels of calcium. This is the first structure of a filament-binding protein bound to actin and it sets stringent, high-resolution limitations on the arrangement of actin protomers within the filament.
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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.