Synthesis of Na2S2O4 mediated cleavable affinity tag for labeling of O-GlcNAc modified proteins via azide-alkyne cycloaddition

Wang, Jiajia; Dou, Biao; Zheng, Lu; Cao, Wu; Zeng, Xueke; Wen, Yinhang; Ma, Jing; Li, Xia

doi:10.1016/j.bmcl.2021.128244

Cited by 6 publications

(4 citation statements)

References 27 publications

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“…We, therefore, identified 336 O- GlcNAc candidate substrates from HEK293T cells ( Supplementary file 1 ). To compare this result with known O- GlcNAc modifications, we compiled two lists of the previously identified O- GlcNAcylated proteins in HEK293T cells via either direct capture ( Zhao et al, 2011 ; Teo et al, 2010 ) or chemoenzymatic labeling methods ( Wang et al, 2021 ; Zhu et al, 2020 ; Li et al, 2019 ; Li et al, 2016 ; Hahne et al, 2013 ; Supplementary file 2 ). Gene ontology (GO) analysis on these three datasets showed that they were enriched in similar biological processes ( Figure 2—figure supplement 1E ).…”

Section: Resultsmentioning

confidence: 99%

Tissue-specific O-GlcNAcylation profiling identifies substrates in translational machinery in Drosophila mushroom body contributing to olfactory learning

Yu,

Liu,

Zhang

et al. 2024

eLife

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O-GlcNAcylation is a dynamic post-translational modification that diversifies the proteome. Its dysregulation is associated with neurological disorders that impair cognitive function, and yet identification of phenotype-relevant candidate substrates in a brain-region specific manner remains unfeasible. By combining an O-GlcNAc binding activity derived from Clostridium perfringens OGA (CpOGA) with TurboID proximity labeling in Drosophila, we developed an O-GlcNAcylation profiling tool that translates O-GlcNAc modification into biotin conjugation for tissue-specific candidate substrates enrichment. We mapped the O-GlcNAc interactome in major brain regions of Drosophila and found that components of the translational machinery, particularly ribosomal subunits, were abundantly O-GlcNAcylated in the mushroom body of Drosophila brain. Hypo-O-GlcNAcylation induced by ectopic expression of active CpOGA in the mushroom body decreased local translational activity, leading to olfactory learning deficits that could be rescued by dMyc overexpression-induced increase of protein synthesis. Our study provides a useful tool for future dissection of tissue-specific functions of O-GlcNAcylation in Drosophila, and suggests a possibility that O-GlcNAcylation impacts cognitive function via regulating regional translational activity in the brain.

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Section: Resultsmentioning

confidence: 99%

Tissue-specific O-GlcNAcylation profiling identifies substrates in translational machinery in Drosophila mushroom body contributing to olfactory learning

Yu,

Liu,

Zhang

et al. 2024

eLife

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“…ACAA2 was modified by glycosylation and OGT was its key glycosyltransferase according to the GeneCards database and research reports 26,27 . To confirm the relationship between ACAA2 and OGT, we conducted immunoprecipitation assays.…”

Section: Resultsmentioning

confidence: 99%

“…ACAA2 was modified by glycosylation and OGT was its key glycosyltransferase according to the GeneCards database and research reports. 26,27 To confirm the relationship between ACAA2 and OGT, we conducted immunoprecipitation assays. The immunoprecipitation assays indicated that the proteins ACAA2 and OGT had an interactive relationship (Figure 4A,B).…”

Section: Ogt Regulates the Nucleoplasmic Distribution Of The Acaa2 Pr...mentioning

confidence: 99%

The oncogenic role and regulatory mechanism of ACAA2 in human ovarian cancer

Leng,

Tian,

Tang

et al. 2024

Molecular Carcinogenesis

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Acetyl‐CoAacyltransferase2 (ACAA2) is a key enzyme in the fatty acid oxidation pathway that catalyzes the final step of mitochondrial β oxidation, which plays an important role in fatty acid metabolism. The expression of ACAA2 is closely related to the occurrence and malignant progression of tumors. However, the function of ACAA2 in ovarian cancer is unclear. The expression level and prognostic value of ACAA2 were analyzed by databases. Gain and loss of function were carried out to explore the function of ACAA2 in ovarian cancer. RNA‐seq and bioinformatics methods were applied to illustrate the regulatory mechanism of ACAA2. ACAA2 overexpression promoted the growth, proliferation, migration, and invasion of ovarian cancer, and ACAA2 knockdown inhibited the malignant progression of ovarian cancer as well as the ability of subcutaneous tumor formation in nude mice. At the same time, we found that OGT can induce glycosylation modification of ACAA2 and regulate the karyoplasmic distribution of ACAA2. OGT plays a vital role in ovarian cancer as a function of oncogenes. In addition, through RNA‐seq sequencing, we found that ACAA2 regulates the expression of DIXDC1. ACAA2 regulated the malignant progression of ovarian cancer through the WNT/β‐Catenin signaling pathway probably. ACAA2 is an oncogene in ovarian cancer and has the potential to be a target for ovarian cancer therapy.

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“…We therefore identified 336 O-GlcNAc candidate substrates from HEK293T cells (Table S1). To compare this result with known O-GlcNAc modifications, we compiled two lists of the previously identified O-GlcNAcylated proteins in HEK293T cells via either direct capture 46,47 or chemoenzymatic labeling methods [48][49][50][51][52] (Table S2). Gene ontology (GO) analysis on these three datasets showed that they were enriched in similar biological processes (Figure S2E).…”

Section: O-glcnacylation Profiling Through Cpoga Proximity Labelingmentioning

confidence: 99%

Olfactory learning inDrosophilarequires O-GlcNAcylation of mushroom body ribosomal subunits

Yu,

Liu,

Zhang

et al. 2023

Preprint

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O-GlcNAcylation is a dynamic post-translational modification that diversifies the proteome. Its dysregulation is associated with neurological disorders that impair cognitive function, and yet identification of phenotype-relevant candidate substrates in a brain-region specific manner remains unfeasible. By combining an O-GlcNAc binding activity derived fromClostridium perfringensOGA (Cp OGA) with TurboID proximity labeling inDrosophila, we developed an O-GlcNAcylation profiling tool that translates O-GlcNAc modification into biotin conjugation for tissue-specific candidate substrates enrichment. We mapped the O-GlcNAc interactome in major brain regions ofDrosophilaand found that components of the translational machinery, including many ribosomal subunits, were abundantly O-GlcNAcylated in the mushroom body, the computational center of theDrosophilabrain. Hypo-O-GlcNAcylation induced by ectopic expression of active Cp OGA in the mushroom body decreased local ribosomal activity, leading to olfactory learning deficits that could be rescued by increasing ribosome biogenesis. Our study reveals that O-GlcNAcylation contributes to the links between protein synthesis and cognitive function in the brain learning center, and provides a useful tool for future dissection of tissue-specific functions of O-GlcNAcylation inDrosophila.

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Synthesis of Na2S2O4 mediated cleavable affinity tag for labeling of O-GlcNAc modified proteins via azide-alkyne cycloaddition

Cited by 6 publications

References 27 publications

Tissue-specific O-GlcNAcylation profiling identifies substrates in translational machinery in Drosophila mushroom body contributing to olfactory learning

Tissue-specific O-GlcNAcylation profiling identifies substrates in translational machinery in Drosophila mushroom body contributing to olfactory learning

The oncogenic role and regulatory mechanism of ACAA2 in human ovarian cancer

Olfactory learning inDrosophilarequires O-GlcNAcylation of mushroom body ribosomal subunits

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