ArticleProtein science : a publication of the Protein Society1999
Identification of Tyr438 as the major in vitro c-Src phosphorylation site in human gelsolin: a mass spectrometric approach.
Article in Protein science : a publication of the Protein Society, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
13 citing papers in PubMed, 59 citations in OpenAlex.
- Gelsolin: A comprehensive pan-cancer analysis of potential prognosis, diagnostic, and immune biomarkers.Frontiers in genetics · 2023Article
- Investigation of post-translational modifications in type 2 diabetes.Clinical proteomics · 2018Review
- Article
- Src kinases regulate de novo actin polymerization during exocytosis in neuroendocrine chromaffin cells.PloS one · 2014Article
- Novel anti-HIV therapeutics targeting chemokine receptors and actin regulatory pathways.Immunological reviews · 2013Review
- Genistein interferes with SDF-1- and HIV-mediated actin dynamics and inhibits HIV infection of resting CD4 T cells.Retrovirology · 2013Article
- Role and regulation of sperm gelsolin prior to fertilization.The Journal of biological chemistry · 2010Article
- Mass spectrometric characterization of gelsolin isoforms.Rapid communications in mass spectrometry : RCM · 2010Article
- Vesicular egress of non-enveloped lytic parvoviruses depends on gelsolin functioning.PLoS pathogens · 2008Article
- Large-scale characterization of HeLa cell nuclear phosphoproteins.Proceedings of the National Academy of Sciences of the United States of America · 2004Article
- Regulation of the formation of osteoclastic actin rings by proline-rich tyrosine kinase 2 interacting with gelsolin.The Journal of cell biology · 2003Article
- Cytochalasin D reduces Ca2+ currents via cofilin-activated depolymerization of F-actin in guinea-pig cardiomyocytes.The Journal of physiology · 2001Article
- Regulation of Sperm Capacitation and the Acrosome Reaction by PIP 2 and Actin Modulation.Asian journal of andrologyReview
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
6 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Gelsolin is an actin-binding protein (82 kDa) consisting of six repeated segments (S1-S6), each approximately 120 residues long. It interacts with phospholipids and we previously showed that phosphatidylinositol 4,5-bisphosphate promotes phosphorylation of gelsolin by the tyrosine kinase c-Src. We used a combination of different methods, such as thin-layer chromatography and anti-phosphotyrosine-agarose immunoprecipitation of phosphopeptides combined with matrix assisted laser desorption ionization-mass spectrometry (MALDI-MS) and post source decay (PSD) analysis, to identify the phosphorylation sites in gelsolin. The major phosphorylation site (Tyr438) was located in subdomain 4 (S4). Phosphorylation of gelsolin in the gelsolin-actin2 complex was inhibited by 90%. Gelsolin phosphorylation by c-Src in the presence of lysophosphatidic acid also revealed Tyr438 as the most prominent site. Additional minor sites were found using the anti-phosphotyrosine bead immunoprecipitation method followed by MALDI-MS and PSD analysis. These sites, representing approximately 5% of the total phosphate incorporation, were identified as Tyr59, Tyr382, Tyr576, and Tyr624. Based on these results we generated antibodies which specifically recognize Tyr438 phosphorylated gelsolin.
Indexed as
Identifiers
What 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.