Proteomics

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O-GlcNAc crosstalks with ADP-ribosylation via PARG


ABSTRACT: O-GlcNAc glycosylation is a prevalent protein post-translational modification (PTM) that occurs intracellularly. Previous investigations have demonstrated that O-GlcNAcylation crosstalks with phosphorylation and ubiquitination, but it is unclear whether it interplays with other PTMs. Here we studied its relationship with ADP-ribosylation, which involves decorating target proteins with the ADP-ribose moiety. We discovered that one ADP-ribosylation “eraser”- ADP-ribose glycohydrolase (PARG)- is O-GlcNAcylated at Ser26. O-GlcNAcylation of PARG is essential to maintain its nuclear localization and chromatin association. In hepatocellular carcinoma (HCC) cells, PARG O-GlcNAcylation enhances DNA damage-binding protein 1 (DDB1) poly(ADP-ribosyl)ation (PARylation) and attenuates its ubiquitination. DDB1 is thus stabilized and degrades its downstream targets, such as c-Myc. We further utilized mouse xenograft models and demonstrated that PARG-S26A promoted HCC. Our study thus revealed that PARG O-GlcNAcylation inhibits HCC, and we propose that O-GlcNAc glycosylation may crosstalk with many other PTMs.

INSTRUMENT(S): LTQ Orbitrap Elite

ORGANISM(S): Homo Sapiens (human)

SUBMITTER: Wen Zhou  

LAB HEAD: Wen Zhou

PROVIDER: PXD041119 | Pride | 2024-01-26

REPOSITORIES: Pride

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21-108_LJ0324_PARG.msf Msf
21-108_LJ0324_PARG.mzML Mzml
21-108_LJ0324_PARG.mzid.gz Mzid
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Publications

O-GlcNAc has crosstalk with ADP-ribosylation via PARG.

Li Jie J   Liu Xiangxiang X   Peng Bin B   Feng Tingting T   Zhou Wen W   Meng Li L   Zhao Shanshan S   Zheng Xiyuan X   Wu Chen C   Wu Shian S   Chen Xing X   Xu Xingzhi X   Sun Jianwei J   Li Jing J  

The Journal of biological chemistry 20231017 11


O-linked N-acetylglucosamine (O-GlcNAc) glycosylation, a prevalent protein post-translational modification (PTM) that occurs intracellularly, has been shown to crosstalk with phosphorylation and ubiquitination. However, it is unclear whether it interplays with other PTMs. Here we studied its relationship with ADP-ribosylation, which involves decorating target proteins with the ADP-ribose moiety. We discovered that the poly(ADP-ribosyl)ation "eraser", ADP-ribose glycohydrolase (PARG), is O-GlcNAc  ...[more]

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