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

Published

Journal Article

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.

Full Text

Duke Authors

Cited Authors

  • Palaniappan, KK; Hangauer, MJ; Smith, TJ; Smart, BP; Pitcher, AA; Cheng, EH; Bertozzi, CR; Boyce, M

Published Date

  • October 31, 2013

Published In

Volume / Issue

  • 5 / 2

Start / End Page

  • 546 - 552

PubMed ID

  • 24120863

Pubmed Central ID

  • 24120863

Electronic International Standard Serial Number (EISSN)

  • 2211-1247

Digital Object Identifier (DOI)

  • 10.1016/j.celrep.2013.08.048

Language

  • eng

Conference Location

  • United States