{"type": "root", "children": [{"type": "p", "children": [{"type": "t", "text": "\nSyntaxin 17 (STX17) is a key autophagosomal SNARE protein that localizes exclusively on the outer membrane of fully formed autophagosomes to mediate their fusion with endosomes and lysosomes. Its unique structure—including a dual‐spanning C‐terminal hairpin with glycine zipper–like motifs—facilitates specific interactions with partner SNAREs such as SNAP29 and VAMP8, as well as with tethering factors of the HOPS complex. Moreover, STX17’s fusogenic activity is tightly regulated by posttranslational modifications; phosphorylation by kinases (for example, by ULK1 and TBK1) and changes in its acetylation status modulate its recruitment to autophagosomes and promote efficient SNARE complex assembly. Additional regulatory proteins, including IRGM and Pacer, and factors affecting membrane lipid charge further fine‐tune its function in promoting autophagosome–lysosome fusion and even influence related processes such as lipid droplet biogenesis."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "1", "end_ref": "10"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nIn addition to its central role in autophagosome maturation, STX17 functions at endoplasmic reticulum–mitochondria contact sites where it helps regulate mitochondrial dynamics and quality control. Here, STX17 has been shown to influence mitochondrial fission and PINK1/Parkin‐independent mitophagy by modulating the localization and activity of the mitochondrial fission factor Drp1, by interacting with Fis1 to trigger mitophagic removal of damaged mitochondria, and by controlling the dephosphorylation of mitochondrial proteins such as PGAM5. Pathogen‐derived effectors that target or cleave STX17 further underscore its importance in maintaining mitochondrial integrity and the balance between apoptosis and mitophagy."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "11"}, {"type": "fg_f", "ref": "5"}, {"type": "fg_f", "ref": "13"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nBeyond its roles in fundamental membrane fusion and mitochondrial quality control, dysregulation of STX17 has been implicated in diverse pathological settings. In certain cancers—including retinoblastoma and possibly melanoma—as well as in autoimmune disorders, altered expression or posttranslational modification of STX17 has been associated with abnormal autophagic flux that can contribute to chemoresistance or impaired degradation of harmful substrates. Similarly, during viral infections with agents such as hepatitis C virus and coxsackievirus B3, down‐regulation or cleavage of STX17 disrupts autophagosome–lysosome fusion and thereby shifts the balance between intracellular degradation and viral release. Moreover, defective STX17 function is linked to perturbations in additional cellular pathways (for example, via competitive SNARE interactions with isoforms like VAMP7 and regulators such as DIPK2A, noncoding RNAs, CFTR, and even STING), thereby integrating autophagy with innate immune responses and inflammatory processes seen in conditions such as atherosclerosis."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "14", "end_ref": "29"}]}, {"type": "t", "text": "\n"}]}, {"type": "rg", "children": [{"type": "r", "ref": 1, "children": [{"type": "t", "text": "Eisuke Itakura, Chieko Kishi-Itakura, Noboru Mizushima "}, {"type": "b", "children": [{"type": "t", "text": "The hairpin-type tail-anchored SNARE syntaxin 17 targets to autophagosomes for fusion with endosomes/lysosomes."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Cell (2012)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1016/j.cell.2012.11.001"}], "href": "https://doi.org/10.1016/j.cell.2012.11.001"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "23217709"}], "href": "https://pubmed.ncbi.nlm.nih.gov/23217709"}]}, {"type": "r", "ref": 2, "children": [{"type": "t", "text": "Peidu Jiang, Taki Nishimura, Yuriko Sakamaki, et al. 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