O-GlcNAcylation site mapping by (azide-alkyne) click chemistry and mass spectrometry following intensive fractionation of skeletal muscle cells proteins

Journal of Proteomics
Barbara DeracinoisCaroline Cieniewski-Bernard

Abstract

The O-linked-N-acetyl-d-glucosaminylation (O-GlcNAcylation) modulates numerous aspects of cellular processes. Akin to phosphorylation, O-GlcNAcylation is highly dynamic, reversible, and responds rapidly to extracellular demand. Despite the absolute necessity to determine post-translational sites to fully understand the role of O-GlcNAcylation, it remains a high challenge for the major reason that unmodified proteins are in excess comparing to the O-GlcNAcylated ones. Based on a click chemistry approach, O-GlcNAcylated proteins were labelled with azido-GalNAc and coupled to agarose beads. The proteome extracted from C2C12 myotubes was submitted to an intensive fractionation prior to azide-alkyne click chemistry. This combination of fractionation and click chemistry is a powerful methodology to map O-GlcNAc sites; indeed, 342 proteins were identified through the identification of 620 peptides containing one or more O-GlcNAc sites. We localized O-GlcNAc sites on proteins involved in signalling pathways or in protein modification, as well as structural proteins. Considering the recent role of O-GlcNAcylation in the modulation of sarcomere morphometry and interaction between key structural protein, we focused on proteins involved in...Continue Reading

Citations

Apr 16, 2019·Frontiers in Endocrinology·Elia Torres-GutiérrezPaz María Salazar-Schettino
Jan 31, 2019·Frontiers in Endocrinology·Marine FerronBenjamin Lauzier
Jan 9, 2021·Chemical Reviews·Junfeng MaGerald W Hart
Jul 31, 2020·Physiological Reviews·John C ChathamAdam R Wende
Jun 18, 2021·Advances and Applications in Bioinformatics and Chemistry : AABC·Theo MauriGuillaume Brysbaert
Jun 19, 2021·Frontiers in Endocrinology·Jie Ning, Huixia Yang
Jul 24, 2021·The Biochemical Journal·Aaron T Balana, Matthew R Pratt

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