ArticleProceedings of the National Academy of Sciences of the United States of America2003
Visualizing the Ca2+-dependent activation of gelsolin by using synchrotron footprinting.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.
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Who cites it
37 citing papers in PubMed.
- Neutrophil Mechanosignaling Promotes Integrin Engagement With Endothelial Cells and Motility Within Inflamed Vessels.Frontiers in immunology · 2018Trial
- Serum gelsolin as a biomarker for differentiating familial Mediterranean fever from juvenile idiopathic arthritis in children.Biomolecules & biomedicine · 2026Article
- Development of an obesity-related multi-gene prognostic model incorporating clinical characteristics in luminal breast cancer.iScience · 2024Article
- Enzymatically dissociated muscle fibers display rapid dedifferentiation and impaired mitochondrial calcium control.iScience · 2022Article
- Circulating Proteins Associated with Response and Resistance to Neoadjuvant Chemotherapy in HER2-Positive Breast Cancer.Cancers · 2022Article
- Composite Conformational Changes of Signaling Proteins upon Ligand Binding Revealed by a Single Approach: Calcium-Calmodulin Study.Analytical chemistry · 2019Article
- The XFP (17-BM) beamline for X-ray footprinting at NSLS-II.Journal of synchrotron radiation · 2019Article
- Visualizing Temperature Mediated Activation of Gelsolin and Its Deactivation By PipScientific reports · 2017Article
- Synchrotron X-ray footprinting as a method to visualize water in proteins.Journal of synchrotron radiation · 2016Article
- DHA-mediated regulation of lung cancer cell migration is not directly associated with Gelsolin or Vimentin expression.Life sciences · 2016Article
- Involvement of gelsolin in TGF-beta 1 induced epithelial to mesenchymal transition in breast cancer cells.Journal of biomedical science · 2015Article
- Quantitative protein topography analysis and high-resolution structure prediction using hydroxyl radical labeling and tandem-ion mass spectrometry (MS).Molecular & cellular proteomics : MCP · 2015Article
- Quantitative mapping of protein structure by hydroxyl radical footprinting-mediated structural mass spectrometry: a protection factor analysis.Biophysical journal · 2015Article
- Damage of hippocampal neurons in rats with chronic alcoholism.Neural regeneration research · 2014Article
- Single-molecule force spectroscopy reveals force-enhanced binding of calcium ions by gelsolin.Nature communications · 2014Article
- Development of a microsecond X-ray protein footprinting facility at the Advanced Light Source.Journal of synchrotron radiation · 2014Article
- Synchrotron X-ray footprinting on tour.Journal of synchrotron radiation · 2014Article
- 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
- Gelsolin activity controls efficient early HIV-1 infection.Retrovirology · 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
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Authors and funding
4 authors.
Funding
Abstract
Radiolytic protein footprinting with a synchrotron source is used to reveal detailed structural changes that occur in the Ca(2+)-dependent activation of gelsolin. More than 80 discrete peptides segments within the structure, covering 95% of the sequence in the molecule, were examined by footprinting and mass spectrometry for their solvent accessibility as a function of Ca(2+) concentration in solution. Twenty-two of the peptides exhibited detectable oxidation; for seven the oxidation extent was seen to be Ca(2+) sensitive. Ca(2+)titration isotherms monitoring the oxidation within residues 49-72 (within subdomain S1), 121-135 (S1), 162-166 (S2), and 722-748 (S6) indicate a three-state activation process with a intermediate that was populated at a Ca(2+) concentration of 1-5 microM that is competent for capping and severing activity. A second structural transition with a midpoint of approximately 60-100 microM, where the accessibility of the above four peptides is further increased, is also observed. Tandem mass spectrometry showed that buried residues within the helical "latch" of S6 (including Pro-745) that contact an F-actin-binding site on S2 and buried F-actin-binding residues within S2 (including Phe-163) are unmasked in the submicromolar Ca(2+) transition. However, residues within S4 that are part of an extended beta-sheet with S6 (including Tyr-453) are revealed only in the subsequent transition at higher Ca(2+) concentrations; the disruption of this extended contact between S4 and S6 (and likely the analogous contact between S1 and S3) likely results in an extended structure permitting additional functions consistent with the fully activated gelsolin molecule.
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