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Spatial and temporal proteomics reveals distinct distribution and dynamics of O-GlcNAcylated proteins

ABSTRACT: Protein O-GlcNAcylation plays critical roles in many cellular events, and its dysregulation is related to multiple diseases. Integrating bioorthogonal chemistry and multiplexed proteomics, we systematically and site-specifically study the distributions and dynamics of protein O-GlcNAcylation in the nucleus and the cytoplasm of human cells. The results demonstrate that O-GlcNAcylated proteins with different functions have distinct distribution patterns, and the distributions vary site-specifically. Moreover, the dynamics of O-GlcNAcylated proteins and non-modified ones in these two compartments are comprehensively analyzed, respectively, and the half-lives of glycoproteins in different compartments are markedly different with the median half-life in the cytoplasm being about two times longer than that in the nucleus. Additionally, glycoproteins in the nucleus are more dramatically stabilized than those in the cytoplasm under the O-GlcNAcase inhibition. The comprehensive spatial and temporal analyses of protein O-GlcNAcylation provide valuable information and advance our understanding of this important modification.

INSTRUMENT(S): LTQ Orbitrap Elite

ORGANISM(S): Homo Sapiens (ncbitaxon:9606)

SUBMITTER: Ronghu Wu

PROVIDER: MSV000089413 | MassIVE | Tue May 03 19:34:00 BST 2022

REPOSITORIES: MassIVE

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