Name: Site mapping of PGK1 O-GlcNAcylation
Keywords: Pgk1

Dataset Information

Site mapping of PGK1 O-GlcNAcylation

ABSTRACT: To identify the site(s) of O-GlcNAcylation on PGK1, we transiently co-expressed Flag-tagged PGK1 and OGT in HEK293T cells. After immunoprecipitation using anti-Flag M2 beads and in-gel trypsin digestion, resulted peptides were subjected to mass spectrometry analysis

INSTRUMENT(S): LTQ Orbitrap

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Cell Culture

SUBMITTER: Hao Nie

LAB HEAD: Wen Yi

PROVIDER: PXD015659 | Pride | 2019-11-06

REPOSITORIES: Pride

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Publications

O-GlcNAcylation of PGK1 coordinates glycolysis and TCA cycle to promote tumor growth.

Nie Hao H Ju Haixing H Fan Jiayi J Shi Xiaoliu X Cheng Yaxian Y Cang Xiaohui X Zheng Zhiguo Z Duan Xiaotao X Yi Wen W

Nature communications 20200107 1

Many cancer cells display enhanced glycolysis and suppressed mitochondrial metabolism. This phenomenon, known as the Warburg effect, is critical for tumor development. However, how cancer cells coordinate glucose metabolism through glycolysis and the mitochondrial tricarboxylic acid (TCA) cycle is largely unknown. We demonstrate here that phosphoglycerate kinase 1 (PGK1), the first ATP-producing enzyme in glycolysis, is reversibly and dynamically modified with O-linked N-acetylglucosamine (O-Glc ...[more]

PMID: 31911580

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Project description:Ubiquitination is a post-translational protein modification that has been shown to have a range of effects, including regulation of protein function, interaction, localization, and degradation. We have previously shown that the muscle-specific ubiquitin E3 ligase, ASB2β, is down-regulated in models of muscle growth and that overexpression ASB2 is sufficient to induce muscle atrophy. To gain insight into the effects of increased ASB2 expression on skeletal muscle mass and function, we used liquid chromatography coupled to tandem mass spectrometry to investigate ASB2-mediated changes to the skeletal muscle proteome and ubiquitinome, via a parallel analysis of remnant di-Gly-modified peptides. The results show that viral vector-mediated ASB2β overexpression in murine muscles causes progressive muscle atrophy and impairment of force-producing capacity, while ASB2β knockdown induces mild muscle hypertrophy. ASB2β-induced muscle atrophy and dysfunction were associated with the early downregulation of mitochondrial and contractile protein abundance, and the upregulation of proteins involved in proteasome-mediated protein degradation (including other E3 ligases), protein synthesis and the cytoskeleton/sarcomere. The overexpression ASB2β also resulted in marked changes in protein ubiquitination, however, there was no simple relationship between changes in ubiquitination status and protein abundance. To investigate proteins that interact with ASB2 and, therefore, potential ASB2 targets, Flag-tagged wild type ASB2, and a mutant ASB2 lacking the C-terminal SOCS box domain (dSOCS) were immunoprecipitated from C2C12 myotubes and subjected to label-free proteomic analysis to determine the ASB2 interactome. ASB2β was found to interact with a range of cytoskeletal and nuclear proteins. When combined with the in vivo ubiquitinomic data, our studies have identified novel putative ASB2β target substrates that warrant further investigation. These findings provide novel insight into the complexity of proteome and ubiquitinome changes that occur during E3 ligase-mediated skeletal muscle atrophy and dysfunction.

Dataset Information

Site mapping of PGK1 O-GlcNAcylation

Publications

O-GlcNAcylation of PGK1 coordinates glycolysis and TCA cycle to promote tumor growth.

Similar Datasets

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