ArticleCancer science2008
The cysteine-cluster motif of c-Src: its role for the heavy metal-mediated activation of kinase.
Article in Cancer science, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
What it found
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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.
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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.
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Who cites it
8 citing papers in PubMed, 20 citations in OpenAlex.
- Pervanadate-induced oxidation relieves autoinhibition of the protein tyrosine kinase SRC.Science signaling · 2026Article
- Redox regulation of tyrosine kinase signalling: more than meets the eye.Journal of biochemistry · 2020Review
- Direct cysteine sulfenylation drives activation of the Src kinase.Nature communications · 2018Article
- Hydrogen peroxide as a damage signal in tissue injury and inflammation: murderer, mediator, or messenger?Journal of cellular biochemistry · 2014Review
- Article
- The role of Src kinase in macrophage-mediated inflammatory responses.Mediators of inflammation · 2012Review
- Article
- S-nitrosylation at cysteine 498 of c-Src tyrosine kinase regulates nitric oxide-mediated cell invasion.The Journal of biological chemistry · 2010Article
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 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
We have previously reported that c-Src is activated by mercuric chloride (HgCl(2)). We investigated the mechanism of this activation and found that in vitro activation of c-Src by HgCl(2) did not require tyrosine residues at 416 and 527. Both SH2 and SH3 domains of c-Src were dispensable for the activation by HgCl(2). In contrast, iodoacetoamide (IAA) that binds to thiol side chain of cysteine blocked the activation of c-Src by HgCl(2). To obtain more clues, each cysteine residue of c-Src was replaced with alanine. Of six cysteine residues in the kinase domain of c-Src, Cys483 and Cys498 located in the C-terminal portion as a cysteine-cluster (CC) motif were critical for the activation. In addition, other Src family kinases, Yes and Lyn, were activated by treatment with HgCl(2), and cysteine residues, especially those correspond to Cys498 of Src in the CC motif of these kinases, were also required for the activation of the kinases by HgCl(2). In addition to these observations, treatment of cells with HgCl(2) dramatically activated the wild-type c-Src, whereas it could not activate the mutant form of Src with a substitution of Cys498. Taken together, our results disclose that cysteine residues in the CC motif of c-Src, Cys483 and Cys498, act as a module for the activation of the kinase by a heavy metal compound, mercuric chloride.
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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.