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- Title
O-GlcNAc-modification of SNAP-29 regulates autophagosome maturation.
- Authors
Guo, Bin; Liang, Qianqian; Li, Lin; Hu, Zhe; Wu, Fan; Zhang, Peipei; Ma, Yongfen; Zhao, Bin; Kovács, Attila L.; Zhang, Zhiyuan; Feng, Du; Chen, She; Zhang, Hong
- Abstract
The mechanism by which nutrient status regulates the fusion of autophagosomes with endosomes/lysosomes is poorly understood. Here, we report that O-linked β-N-acetylglucosamine (O-GlcNAc) transferase (OGT) mediates O-GlcNAcylation of the SNARE protein SNAP-29 and regulates autophagy in a nutrient-dependent manner. In mammalian cells, OGT knockdown, or mutating the O-GlcNAc sites in SNAP-29, promotes the formation of a SNAP-29-containing SNARE complex, increases fusion between autophagosomes and endosomes/lysosomes, and promotes autophagic flux. In Caenorhabditis elegans, depletion of ogt-1 has a similar effect on autophagy; moreover, expression of an O-GlcNAc-defective SNAP-29 mutant facilitates autophagic degradation of protein aggregates. O-GlcNAcylated SNAP-29 levels are reduced during starvation in mammalian cells and in C. elegans. Our study reveals a mechanism by which O-GlcNAc-modification integrates nutrient status with autophagosome maturation.
- Subjects
N-acetylglucosamine genetics; AUTOPHAGY; CELLULAR control mechanisms; CAENORHABDITIS elegans; CELL aggregation
- Publication
Nature Cell Biology, 2014, Vol 16, Issue 12, p1215
- ISSN
1465-7392
- Publication type
Article
- DOI
10.1038/ncb3066