A chemical glycoproteomics platform reveals O-GlcNAcylation of mitochondrial voltage-dependent anion channel 2.
Abstract
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.
Type
Journal articleSubject
AcetylglucosamineAnimals
Cell Line
Electrophoresis, Gel, Pulsed-Field
Fluorescent Dyes
Glycoproteins
Glycosylation
HEK293 Cells
Humans
Jurkat Cells
Mice
Mitochondria
Proteomics
Substrate Specificity
Voltage-Dependent Anion Channel 2
Permalink
https://hdl.handle.net/10161/15370Published Version (Please cite this version)
10.1016/j.celrep.2013.08.048Publication Info
Palaniappan, K; Hangauer, M; Smith, T; Smart, B; Pitcher, A; Cheng, E; ... Boyce,
M (2013). A chemical glycoproteomics platform reveals O-GlcNAcylation of mitochondrial voltage-dependent
anion channel 2. Cell Rep, 5(2). pp. 546-552. 10.1016/j.celrep.2013.08.048. Retrieved from https://hdl.handle.net/10161/15370.This is constructed from limited available data and may be imprecise. To cite this
article, please review & use the official citation provided by the journal.
Collections
More Info
Show full item recordScholars@Duke
Tim Smith
Student

Articles written by Duke faculty are made available through the campus open access policy. For more information see: Duke Open Access Policy
Rights for Collection: Scholarly Articles
Works are deposited here by their authors, and represent their research and opinions, not that of Duke University. Some materials and descriptions may include offensive content. More info