A chemical glycoproteomics platform reveals O-GlcNAcylation of mitochondrial voltage-dependent anion channel 2.
Repository Usage Stats
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.
Electrophoresis, Gel, Pulsed-Field
Voltage-Dependent Anion Channel 2
Published Version (Please cite this version)10.1016/j.celrep.2013.08.048
Publication InfoPalaniappan, KK; Hangauer, MJ; Smith, TJ; Smart, BP; Pitcher, AA; Cheng, EH; ... Boyce, Michael Scott (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.
More InfoShow full item record
Assistant Professor of Biochemistry
The Boyce Lab studies mammalian cell signaling through protein glycosylation. For the latest news, project information and publications from our group, please visit our web site at http://www.boycelab.org.