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• W4212903443 startingPage "109" @default.
• W4212903443 abstract "Post-translational modifications of cellular substrates by members of the ubiquitin (Ub) and ubiquitin-like (UbL) family are crucial for regulating protein homeostasis in organisms. The term ubiquitin code encapsulates how this diverse family of modifications, via adding single UbLs or different types of UbL chains, leads to specific fates for substrates. Cancer, neurodegeneration and other conditions are sometimes linked to underlying errors in this code. Studying these modifications in cells is particularly challenging since they are usually transient, scarce, and compartment-specific. Advances in the use of biotin-based methods to label modified proteins, as well as their proximally-located interactors, facilitate isolation and identification of substrates, modification sites, and the enzymes responsible for writing and erasing these modifications, as well as factors recruited as a consequence of the substrate being modified. In this review, we discuss site-specific and proximity biotinylation approaches being currently applied for studying modifications by UbLs, highlighting the pros and cons, with mention of complementary methods when possible. Future improvements may come from bioengineering and chemical biology but even now, biotin-based technology is uncovering new substrates and regulators, expanding potential therapeutic targets to manipulate the Ub code." @default.
• W4212903443 created "2022-02-24" @default.
• W4212903443 creator A5006502512 @default.
• W4212903443 creator A5019935493 @default.
• W4212903443 creator A5044982971 @default.
• W4212903443 creator A5048624077 @default.
• W4212903443 creator A5074486047 @default.
• W4212903443 creator A5091098231 @default.
• W4212903443 date "2022-12-01" @default.
• W4212903443 modified "2023-10-10" @default.
• W4212903443 title "Studying the ubiquitin code through biotin-based labelling methods" @default.
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