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A chemical glycoproteomics platform reveals O-GlcNAcylation of mitochondrial voltage-dependent anion channel 2.

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Date
2013-10-31
Authors
Palaniappan, K
Hangauer, M
Smith, T
Smart, B
Pitcher, A
Cheng, E
Bertozzi, C
Boyce, M
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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 article
Subject
Acetylglucosamine
Animals
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/10161/15370
Published Version (Please cite this version)
10.1016/j.celrep.2013.08.048
Publication 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.
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Smith

Tim Smith

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