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O-GlcNAc-modification of SNAP-29 regulates autophagosome maturation
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Journal Article
O-GlcNAc-modification of SNAP-29 regulates autophagosome maturation
2014
Overview
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.
Zhang and colleagues report that starvation reduces
O
-GlcNAcylation of the SNARE protein SNAP-29. This promotes formation of a competent SNARE complex that increases autophagosome–lysosome fusion, increasing autophagosome maturation and flux.
Publisher
Nature Publishing Group UK,Nature Publishing Group
Subject
/ 13/106
/ 14/19
/ 14/28
/ 14/35
/ 38/77
/ Acetylglucosamine - metabolism
/ Animals
/ Caenorhabditis elegans - metabolism
/ Caenorhabditis elegans Proteins - genetics
/ Caenorhabditis elegans Proteins - metabolism
/ Green Fluorescent Proteins - genetics
/ Humans
/ Kinases
/ Mammals
/ Mutation
/ N-Acetylglucosaminyltransferases - genetics
/ N-Acetylglucosaminyltransferases - metabolism
/ Proteins
/ Q-SNARE Proteins - metabolism
/ Qa-SNARE Proteins - genetics
/ Qb-SNARE Proteins - genetics
/ Qb-SNARE Proteins - metabolism
/ Qc-SNARE Proteins - genetics
/ Qc-SNARE Proteins - metabolism
