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Symbol STX17 contributors: mct - updated : 20-08-2017
HGNC name syntaxin 17
HGNC id 11432
  • one t-SNARE coiled coil homology domain
  • two transmembrane domains, each containing glycine zipper motifs
  • tyrosine-based motif which is required for its incorporation into COPII (coatomer protein II) vesicles, exit from the ER and localization to the ERGIC
  • 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
    interspecies homolog to murine 9030425C21Rik
    homolog to rattus LOC252853
    intraspecies homolog to syntaxin 13, syntaxin 7
    FAMILY syntaxin/epimorphin family
    CATEGORY transport carrier
    SUBCELLULAR LOCALIZATION     intracellular
    intracellular,cytoplasm,organelle,endoplasmic reticulum
  • type IV membrane protein
  • 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 (pMID: 23217709)
  • present on raft-like structures of ER-mitochondria contact sites and promotes mitochondrial fission by determining DNM1L localization and activity
  • basic FUNCTION
  • involved in vesicular trafficking to lysosomes
  • is essential for maintaining the architecture of ERGIC and Golgi
  • autophagosomal SNARE required for fusion with the endosome/lysosome
  • has a hairpin-type structure mediated by two transmembrane domains, each containing glycine zipper motifs, contributing to its specific localization to completed autophagosomes but not to phagophores
  • late recruitment of STX17 to completed autophagosomes could prevent premature fusion of the lysosome with unclosed phagophores
  • might contribute to proper phagophore assembly
  • acts as a switch that responds to nutrient conditions and integrates functions for the ER and autophagosomes with mitochondrial dynamics
  • upon autophagy induction STX17 is strictly required for ATG14 recruitment to the ER-mitochondria contact sites, a critical step for the assembly of the phagophore and therefore for autophagosome formation
  • plays a role in the early events of autophagy by interacting with the phosphatidylinositol 3-kinase complex component ATG14
  • STX17, SNAP29, and VAMP8, are potentially essential for the fusion between autophagosomes and lysosomes
  • CELLULAR PROCESS cell cycle, division
    PHYSIOLOGICAL PROCESS cellular trafficking transport
    a component
    small molecule
  • interacting with syntaxin 3
  • ER-resident SNARE protein syntaxin 17 (STX17) binds ATG14 and recruits it to the ER-mitochondria contact site
  • interacts with SNAP29 and the lysosomal SNARE VAMP8, and all of these proteins are required for autophagosome-lysosome fusion
  • HOPS complex mediates autophagosome-lysosome fusion through interaction with syntaxin 17
  • promotes mitochondrial fission by determining DNM1L localization and activity
  • ATG14 binds to the SNARE core domain of STX17 through its coiled-coil domain, and stabilizes the STX17-SNAP29 binary t-SNARE complex on autophagosomes
  • ATG14-STX17-SNAP29 interaction mediates autophagosome-lysosome tethering and fusion events, thus revealing a novel function of ATG14 in the later steps of the autophagy pathway
  • ATG14 directly binds to the STX17-SNAP29 binary complex on autophagosomes and promotes STX17-SNAP29-VAMP8-mediated autophagosome fusion with lysosomes
  • is dispensable for lysosome acidification, but promotes the completion of autophagy via promotion of autophagosome-lysosome fusion through its interaction with STX17 and VAMP8
  • DIPK2A, a late endosome- and lysosome-localized protein, binds to VAMP7B, which inhibits the interaction of VAMP7B with STX17 and enhances the binding of STX17 to VAMP7A, thus enhancing autophagosome-lysosome fusion
  • cell & other