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pubmed-article:9358037pubmed:abstractTextThe movement of hydrolases and other proteins to lysosomes is accomplished by vesicle trafficking. Specific vesicles are targeted from the trans-Golgi network via a prelysosomal compartment to lysosomes. The specificity of vesicle transport is thought to occur through the interaction of vesicle proteins with receptors on a particular target membrane. The syntaxins are a family of transmembrane proteins that have been implicated as vesicle receptors involved in vesicle docking and fusion. Syntaxins 1-4 are localized to the plasma membrane, and in particular, syntaxin 1a mediates synaptic vesicle docking in the nerve terminal. Syntaxins 5 and 6 have been localized to cis-Golgi and trans-Golgi network compartments, respectively. We now report the identification of syntaxin 7 from a human brain cDNA library. The syntaxin 7 gene is localized to human chromosome 6. By Northern analysis, the syntaxin RNA was found to be broadly distributed. Based on its homology to yeast and plant vacuolar syntaxins, we propose that syntaxin 7 has a role in vesicle trafficking between the Golgi complex and lysosomes. In vitro binding studies reveal that syntaxin 7 binds alphaSNAP, a key regulator of transport vesicle fusion at multiple stages of the secretory pathway.lld:pubmed
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pubmed-article:9358037pubmed:articleTitleHuman syntaxin 7: a Pep12p/Vps6p homologue implicated in vesicle trafficking to lysosomes.lld:pubmed
pubmed-article:9358037pubmed:affiliationDepartment of Molecular Neurobiology, Kennedy Krieger Institute, The Johns Hopkins University School of Medicine, Baltimore, MD 21205, USA.lld:pubmed
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