The hairpin-type tail-anchored SNARE syntaxin 17 targets to autophagosomes for fusion with endosomes/lysosomes

Cell. 2012 Dec 7;151(6):1256-69. doi: 10.1016/j.cell.2012.11.001.

Abstract

The lysosome is a degradative organelle, and its fusion with other organelles is strictly regulated. In contrast to fusion with the late endosome, the mechanisms underlying autophagosome-lysosome fusion remain unknown. Here, we identify syntaxin 17 (Stx17) as the autophagosomal SNARE required for fusion with the endosome/lysosome. Stx17 localizes to the outer membrane of completed autophagosomes but not to the isolation membrane (unclosed intermediate structures); for this reason, the lysosome does not fuse with the isolation membrane. Stx17 interacts with SNAP-29 and the endosomal/lysosomal SNARE VAMP8. Depletion of Stx17 causes accumulation of autophagosomes without degradation. Stx17 has a unique C-terminal hairpin structure mediated by two tandem transmembrane domains containing glycine zipper-like motifs, which is essential for its association with the autophagosomal membrane. These findings reveal a mechanism by which the SNARE protein is available to the completed autophagosome.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Motifs
  • Amino Acid Sequence
  • Animals
  • Autophagy
  • Cell Line
  • Cytosol / metabolism
  • Endosomes / metabolism*
  • Fibroblasts / metabolism
  • HEK293 Cells
  • HeLa Cells
  • Humans
  • Lysosomes / metabolism*
  • Mice
  • Molecular Sequence Data
  • Phagosomes / metabolism*
  • Protein Structure, Tertiary
  • Qa-SNARE Proteins / chemistry
  • Qa-SNARE Proteins / metabolism*
  • Sequence Alignment

Substances

  • Qa-SNARE Proteins
  • STX17 protein, human
  • Stx17 protein, mouse