Abstract
Protein arginylation is a unique and under-explored posttranslational modification, which governs many biological functions and the fate of affected proteins. Since ATE1 was discovered in 1963, a central tenet of protein arginylation is that arginylated proteins are destined for proteolysis. However, recent studies have shown that protein arginylation controls not only the half-life of a protein but also various signaling pathways. Here, we introduce a novel molecular tool to elucidate protein arginylation. This new tool, termed R-catcher, is derived from the ZZ domain of p62/sequestosome-1, an N-recognin of the N-degron pathway. The ZZ domain, which has been shown to strongly bind N-terminal arginine, has been modified at specific residues to increase specificity and affinity for N-terminal arginine. R-catcher is a powerful analysis tool allowing researchers to capture the cellular arginylation patterns under various stimuli and conditions, thereby identifying potential therapeutic targets in numerous diseases.
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Seo, T., Han, G., Cha-Molstad, H. (2023). N-Terminal Arginylation Pull-down Analysis Using the R-Catcher Tool. In: Kashina, A.S. (eds) Protein Arginylation. Methods in Molecular Biology, vol 2620. Humana, New York, NY. https://doi.org/10.1007/978-1-0716-2942-0_24
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DOI: https://doi.org/10.1007/978-1-0716-2942-0_24
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