2019
DOI: 10.1101/828921
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Selective protein O-GlcNAcylation in cells by a proximity-directed O-GlcNAc transferase

Abstract: O-Linked N-acetylglucosamine (O-GlcNAc) is a monosaccharide that plays an essential role in cellular signaling throughout the nucleocytoplasmic proteome of eukaryotic cells. Yet, the study of post-translational modifications like O-GlcNAc has been limited by the lack of strategies to induce O-GlcNAcylation on a target protein in cells. Here, we report a generalizable genetic strategy to induce O-GlcNAc to specific target proteins in cells using a nanobody as a proximitydirecting agent fused to O-GlcNAc transfe… Show more

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Cited by 2 publications
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“…Directed protein manipulation in specific cell types has multiple applications, from developmental studies to designing synthetic biology systems and eventually to therapeutic uses. A similar nanobody-based paradigm has been recently applied to induce glycosylation and deglycosylation of desired target proteins in cells ( Ramirez et al, 2019 ; Ge et al, 2021 ). Furthermore, in the elegant work by Karginov et al (2014b) , a rapamycin-regulated engineered Src kinase was used in cultured cells to dissect the effect of Src-dependent phosphorylation of its two substrates, FAK and p130Cas, on cell morphology and filopodia formation.…”
Section: Discussionmentioning
confidence: 99%
“…Directed protein manipulation in specific cell types has multiple applications, from developmental studies to designing synthetic biology systems and eventually to therapeutic uses. A similar nanobody-based paradigm has been recently applied to induce glycosylation and deglycosylation of desired target proteins in cells ( Ramirez et al, 2019 ; Ge et al, 2021 ). Furthermore, in the elegant work by Karginov et al (2014b) , a rapamycin-regulated engineered Src kinase was used in cultured cells to dissect the effect of Src-dependent phosphorylation of its two substrates, FAK and p130Cas, on cell morphology and filopodia formation.…”
Section: Discussionmentioning
confidence: 99%
“…Protein binder-based approaches for directing a given enzymatic function to a specific, single target open new avenues for unravelling protein-protein interactions in a given cell type and for manipulating them in a desired way, both for developmental studies, for designing synthetic biology systems or eventually for therapeutic goals. Similar nanobody-based paradigm has been recently applied to induce glycosylation and deglycosylation of desired target proteins in cells 93,94 . Furthermore, in the elegant work by Karginov et al, a rapamycin-regulated engineered Src kinase was used in cultured cell to dissect the effect of Src-dependent phosphorylation of its two substrates, FAK and p130Cas (containing a modified rapamycin– binding domain insertion), on cell morphology and filopodia formation 95 .…”
Section: Discussionmentioning
confidence: 99%