ArticleProceedings of the National Academy of Sciences of the United States of America2016
In cellulo phosphorylation induces pharmacological reprogramming of maurocalcin, a cell-penetrating venom peptide.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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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
7 citing papers in PubMed, 11 citations in OpenAlex.
- Old dog, new trick: Charybdotoxin as a novel ryanodine receptor blocker.The Journal of physiology · 2026Article
- The venom ofFrontiers in pharmacology · 2025Article
- Cryo-EM analysis of scorpion toxin binding to Ryanodine Receptors reveals subconductance that is abolished by PKA phosphorylation.Science advances · 2023Article
- Cell-penetrating peptides improve pharmacokinetics and pharmacodynamics of anticancer drugs.Tissue barriers · 2022Review
- Overview of protein posttranslational modifications in Arthropoda venoms.The journal of venomous animals and toxins including tropical diseases · 2022Review
- Article
- Maurocalcin phosphorylated at threonin 26 maintains its activity on ryanodine receptor-mediated Ca2+ release in intact muscle fibers.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
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Authors and funding
12 authors at 6 institutions in 2 countries.
Funding
Abstract
The venom peptide maurocalcin (MCa) is atypical among toxins because of its ability to rapidly translocate into cells and potently activate the intracellular calcium channel type 1 ryanodine receptor (RyR1). Therefore, MCa is potentially subjected to posttranslational modifications within recipient cells. Here, we report that MCa Thr(26) belongs to a consensus PKA phosphorylation site and can be phosphorylated by PKA both in vitro and after cell penetration in cellulo. Unexpectedly, phosphorylation converts MCa from positive to negative RyR1 allosteric modulator. Thr(26) phosphorylation leads to charge neutralization of Arg(24), a residue crucial for MCa agonist activity. The functional effect of Thr(26) phosphorylation is partially mimicked by aspartyl mutation. This represents the first case, to our knowledge, of both ex situ posttranslational modification and pharmacological reprogramming of a small natural cystine-rich peptide by target cells. So far, phosphorylated MCa is the first specific negative allosteric modulator of RyR1, to our knowledge, and represents a lead compound for further development of phosphatase-resistant analogs.
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Registered trials
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