Syntaxin-8 is a protein that in humans is encoded by the STX8 gene. [5][6][7] Syntaxin 8 directly interacts with HECTd3 and has similar subcellular localization. [8] . The protein has been shown to form the SNARE complex with syntaxin 7, vti1b and endobrevin. These function as the machinery for the homotypic fusion of late endosomes. [9]

Mar 30, 2025 · STX8 (Syntaxin 8) is a Protein Coding gene. Diseases associated with STX8 include Prostate Cancer and Ceroid Lipofuscinosis, Neuronal, 8. Among its related pathways are wtCFTR and delta508-CFTR traffic / Generic schema (norm and CF) and Nicotine Pathway (Dopaminergic Neuron), Pharmacodynamics.

Stx8 localizes at the trans -Golgi network (TGN) and the prevacuolar endosome (PVE), and its recycling depends on the retromer component Vps35, and on the sorting nexins Vps5, Vps17, and Snx3. Several experimental approaches demonstrate that Stx8 is a cargo of the Snx3-retromer.

Vesicle trafficking protein that functions in the early secretory pathway, possibly by mediating retrograde transport from cis-Golgi membranes to the ER. Gene Ontology (GO) annotations organized by slimming set. Note: Preferentially associated with the early endosome.

STX8 silencing reduced the binding of quality control protein, Hsp 27, a protein that targets ΔF508-CFTR for sumoylation and subsequent degradation, to ΔF508-CFTR. STX8 silencing increased the levels of Hsp 60 a protein involving in early events in protein folding.

STX8 silencing restores the function ofDeltaF508-CFTR. Stx8 is required for proper and timely sorting and trafficking of cytotoxic molecules to functional lytic granules through the endosomal pathway in human cytotoxic t-lymphocytes.

Syntaxin 8 (STX8) is another SNARE protein that binds to CFTR [9, 10]. STX8 operates together with several other proteins, including vesicle associated protein 8 (VAMP8), STX7, and Vti1b, to support intracellular membrane fusion processes at the early endosome [9, 11].

Syntaxin 8 (Stx8) is expressed in LG and colocalizes with the T cell receptor (TCR) upon IS formation. Here, we report the significance of Stx8 for human CTL cytotoxicity. We found that Stx8 mostly localized in late, recycling endosomal and lysosomal compartments with little expression in early endosomal compartments.

Results: ATP secretion, aggregation, and thrombus stability are defective in Stx8−/− mouse platelets. Conclusion: STX8 is involved in platelet dense granule secretion, and the STX8-mediated pathway contributes to thrombus stabilization.

Stx8 is required for proper and timely sorting and trafficking of cytotoxic molecules to functional lytic granules through the endosomal pathway in human cytotoxic t-lymphocytes.