A Chemical Glycoproteomics Platform Reveals O-GlcNAcylation of Mitochondrial Voltage-Dependent Anion Channel 2
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-Gl...
| Main Authors: | , , , , , , , |
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| Format: | Article |
| Language: | English |
| Published: |
Elsevier
2013-10-01
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| Series: | Cell Reports |
| Online Access: | http://www.sciencedirect.com/science/article/pii/S2211124713005081 |
| _version_ | 1818066087610155008 |
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| author | Krishnan K. Palaniappan Matthew J. Hangauer Timothy J. Smith Brian P. Smart Austin A. Pitcher Emily H. Cheng Carolyn R. Bertozzi Michael Boyce |
| author_facet | Krishnan K. Palaniappan Matthew J. Hangauer Timothy J. Smith Brian P. Smart Austin A. Pitcher Emily H. Cheng Carolyn R. Bertozzi Michael Boyce |
| author_sort | Krishnan K. Palaniappan |
| collection | DOAJ |
| description | 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. |
| first_indexed | 2024-12-10T15:02:13Z |
| format | Article |
| id | doaj.art-aeec06a4f1d546dfb6232a33d03115b5 |
| institution | Directory Open Access Journal |
| issn | 2211-1247 |
| language | English |
| last_indexed | 2024-12-10T15:02:13Z |
| publishDate | 2013-10-01 |
| publisher | Elsevier |
| record_format | Article |
| series | Cell Reports |
| spelling | doaj.art-aeec06a4f1d546dfb6232a33d03115b52022-12-22T01:44:08ZengElsevierCell Reports2211-12472013-10-015254655210.1016/j.celrep.2013.08.048A Chemical Glycoproteomics Platform Reveals O-GlcNAcylation of Mitochondrial Voltage-Dependent Anion Channel 2Krishnan K. Palaniappan0Matthew J. Hangauer1Timothy J. Smith2Brian P. Smart3Austin A. Pitcher4Emily H. Cheng5Carolyn R. Bertozzi6Michael Boyce7Department of Chemistry, University of California, Berkeley, Berkeley, CA 94720, USADepartment of Chemistry, University of California, Berkeley, Berkeley, CA 94720, USADepartment of Biochemistry, Duke University School of Medicine, Durham, NC 27710, USADepartment of Chemistry, University of California, Berkeley, Berkeley, CA 94720, USADepartment of Chemistry, University of California, Berkeley, Berkeley, CA 94720, USAHuman Oncology and Pathogenesis Program and Department of Pathology, Memorial Sloan-Kettering Cancer Center, New York, NY 10065, USADepartment of Chemistry, University of California, Berkeley, Berkeley, CA 94720, USADepartment of Chemistry, University of California, Berkeley, Berkeley, CA 94720, USAProtein 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.http://www.sciencedirect.com/science/article/pii/S2211124713005081 |
| spellingShingle | Krishnan K. Palaniappan Matthew J. Hangauer Timothy J. Smith Brian P. Smart Austin A. Pitcher Emily H. Cheng Carolyn R. Bertozzi Michael Boyce A Chemical Glycoproteomics Platform Reveals O-GlcNAcylation of Mitochondrial Voltage-Dependent Anion Channel 2 Cell Reports |
| title | A Chemical Glycoproteomics Platform Reveals O-GlcNAcylation of Mitochondrial Voltage-Dependent Anion Channel 2 |
| title_full | A Chemical Glycoproteomics Platform Reveals O-GlcNAcylation of Mitochondrial Voltage-Dependent Anion Channel 2 |
| title_fullStr | A Chemical Glycoproteomics Platform Reveals O-GlcNAcylation of Mitochondrial Voltage-Dependent Anion Channel 2 |
| title_full_unstemmed | A Chemical Glycoproteomics Platform Reveals O-GlcNAcylation of Mitochondrial Voltage-Dependent Anion Channel 2 |
| title_short | A Chemical Glycoproteomics Platform Reveals O-GlcNAcylation of Mitochondrial Voltage-Dependent Anion Channel 2 |
| title_sort | chemical glycoproteomics platform reveals o glcnacylation of mitochondrial voltage dependent anion channel 2 |
| url | http://www.sciencedirect.com/science/article/pii/S2211124713005081 |
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