A chemical glycoproteomics platform reveals O-GlcNAcylation of mitochondrial voltage-dependent anion channel 2.
Protein modification by O-linked β-N-acetylglucosamine (O-GlcNAc) is a critical cell signaling modality, but identifying signal-specific O-GlcNAcylation events remains a significant experimental challenge. Here, we describe a method for visualizing and analyzing organelle- and stimulus-specific O-GlcNAcylated proteins and use it to identify the mitochondrial voltage-dependent anion channel 2 (VDAC2) as an O-GlcNAc substrate. VDAC2(-/-) cells resist the mitochondrial dysfunction and apoptosis caused by global O-GlcNAc perturbation, demonstrating a functional connection between O-GlcNAc signaling and mitochondrial physiology through VDAC2. More broadly, our method will enable the discovery of signal-specific O-GlcNAcylation events in a wide array of experimental contexts.
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- Voltage-Dependent Anion Channel 2
- Substrate Specificity
- Proteomics
- Mitochondria
- Mice
- Jurkat Cells
- Humans
- HEK293 Cells
- Glycosylation
- Glycoproteins
Citation
Published In
DOI
EISSN
Publication Date
Volume
Issue
Start / End Page
Location
Related Subject Headings
- Voltage-Dependent Anion Channel 2
- Substrate Specificity
- Proteomics
- Mitochondria
- Mice
- Jurkat Cells
- Humans
- HEK293 Cells
- Glycosylation
- Glycoproteins