A chemical glycoproteomics platform reveals O-GlcNAcylation of mitochondrial voltage-dependent anion channel 2.
| Autor: | Palaniappan KK; Department of Chemistry, University of California, Berkeley, Berkeley, CA 94720, USA., Hangauer MJ, Smith TJ, Smart BP, Pitcher AA, Cheng EH, Bertozzi CR, Boyce M |
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| Jazyk: | angličtina |
| Zdroj: | Cell reports [Cell Rep] 2013 Oct 31; Vol. 5 (2), pp. 546-52. Date of Electronic Publication: 2013 Oct 10. |
| DOI: | 10.1016/j.celrep.2013.08.048 |
| Abstrakt: | 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. (Copyright © 2013 The Authors. Published by Elsevier Inc. All rights reserved.) |
| Databáze: | MEDLINE |
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