A chemical glycoproteomics platform reveals O-GlcNAcylation of mitochondrial voltage-dependent anion channel 2.
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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 http://hdl.handle.net/10161/15370.
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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.