title: Multiple roles of the vesicular-SNARE TI-VAMP in post-Golgi and endosomal trafficking.
abstract: SNARE (Soluble N-ethylmaleimide-sensitive factor attachment protein receptor) proteins are the core machinery of membrane fusion. Vesicular SNAREs (v-SNAREs) interact with their target SNAREs (t-SNAREs) to form SNARE complexes which mediate membrane fusion. Here we review the basic properties and functions of the v-SNARE TI-VAMP/VAMP7 (Tetanus neurotoxin insensitive-vesicle associated membrane protein). TI-VAMP interacts with its t-SNARE partners, particularly plasmalemmal syntaxins, to mediate membrane fusion and with several regulatory proteins especially via its amino-terminal regulatory Longin domain. Partners include AP-3, Hrb/(Human immunodeficiency virus Rev binding) protein, and Varp (Vps9 domain and ankyrin repeats containing protein) and regulate TI-VAMP's function and targeting. TI-VAMP is involved both in secretory and endocytic pathways which mediate neurite outgrowth and synaptic transmission, plasma membrane remodeling and lysosomal secretion.
authors.affiliation: Membrane Traffic in Neuronal and Epithelial Morphogenesis', INSERM U950, Paris F-75013, France.
authors.forename: Mathilde
authors.initials: M
authors.lastname: Chaineau
authors.forename: Lydia
authors.initials: L
authors.lastname: Danglot
authors.forename: Thierry
authors.initials: T
authors.lastname: Galli
mesh_terms: D000818:Animals; D011992:Endosomes / Q000378:metabolism*; D006056:Golgi Apparatus / Q000378:metabolism*; D006801:Humans; D008666:Metalloendopeptidases / Q000378:metabolism*; D021381:Protein Transport; D050600:SNARE Proteins / Q000378:metabolism*; D013744:Tetanus Toxin / Q000378:metabolism*
chemical_list: D050600:SNARE Proteins; D013744:Tetanus Toxin; C035979:tetanospasmin; D008666:Metalloendopeptidases