ArticleThe Biochemical journal2000
Calcium-dependent conformational stability of modules 1 and 2 of human gelsolin.
Article in The Biochemical journal, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 31 citations in OpenAlex.
- A molecular perspective of gelsolin amyloidosis: An old foe with new faces.Cellular and molecular life sciences : CMLS · 2026Review
- The structure of N184K amyloidogenic variant of gelsolin highlights the role of the H-bond network for protein stability and aggregation properties.European biophysics journal : EBJ · 2020Article
- Single-molecule force spectroscopy reveals force-enhanced binding of calcium ions by gelsolin.Nature communications · 2014Article
- N-terminal region of gelsolin induces apoptosis of activated hepatic stellate cells by a caspase-dependent mechanism.PloS one · 2012Article
- Lack of gelsolin promotes perpetuation of atrial fibrillation in the mouse heart.Journal of interventional cardiac electrophysiology : an international journal of arrhythmias and pacing · 2009Article
- The crystal structure of the C-terminus of adseverin reveals the actin-binding interface.Proceedings of the National Academy of Sciences of the United States of America · 2009Article
- Structure of the N-terminal half of gelsolin bound to actin: roles in severing, apoptosis and FAF.The EMBO journal · 2004Article
- Furin initiates gelsolin familial amyloidosis in the Golgi through a defect in Ca(2+) stabilization.The EMBO journal · 2001Article
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Gelsolin modulates the actin cytoskeleton in the cytoplasm and clears the circulation of stray filaments. In vitro, gelsolin cleaves, nucleates and caps actin filaments, activities that are calcium-dependent. Both cellular and secreted forms share a sequence of 730 residues comprising six homologous modules termed G1-G6. A disulphide bond is formed in secreted G2, whereas in the cytoplasm it remains reduced. A point mutation in G2 causes an amyloidosis with neurological, ophthalmological and dermatological symptoms. This mutation does not affect the cytoplasmic form, while the secreted form is proteolysed. As a first step towards understanding how gelsolin folds and functions in different cellular compartments, we have characterized at equilibrium the urea-induced unfolding of G1 and G2, with or without calcium and/or disulphide bond. G1 and G2 both exhibit two-state unfolding behaviour and are stabilized by calcium. The disulphide bond also contributes to the stability of G2. In the absence of Ca(2+) and disulphide bond, G2 adopts a non-native conformation, suggesting that folding of G2 in the cytoplasm relies on the presence of surrounding modules or other molecular partners.
Indexed as
Identifiers
10970804PMC1221322W2024862945What OpenQuestion holds
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.