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FLASH GENE
Symbol STX17 contributors: mct - updated : 20-08-2017
HGNC name syntaxin 17
HGNC id 11432
EXPRESSION
Type ubiquitous
   expressed in (based on citations)
organ(s)
SystemOrgan level 1Organ level 2Organ level 3Organ level 4LevelPubmedSpeciesStageRna symbol
Digestiveliver   highly
Reproductivemale systemtestis  highly
Skin/Tegumentskin appendageshairfollicle   Homo sapiens
cell lineage
cell lines
fluid/secretion
at STAGE
PROTEIN
PHYSICAL PROPERTIES
STRUCTURE
motifs/domains
  • 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
  • HOMOLOGY
    interspecies homolog to murine 9030425C21Rik
    homolog to rattus LOC252853
    intraspecies homolog to syntaxin 13, syntaxin 7
    Homologene
    FAMILY syntaxin/epimorphin family
    CATEGORY transport carrier
    SUBCELLULAR LOCALIZATION     intracellular
    intracellular,cytoplasm,organelle,membrane
    intracellular,cytoplasm,organelle,endoplasmic reticulum
    intracellular,cytoplasm,cytosolic
    text
  • 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
    PATHWAY
    metabolism
    signaling
    a component
    INTERACTION
    DNA
    RNA
    small molecule
    protein
  • 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
    REGULATION
    ASSOCIATED DISORDERS
    ANIMAL & CELL MODELS