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• W2077691322 endingPage "3826" @default.
• W2077691322 startingPage "3817" @default.
• W2077691322 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." @default.
• W2077691322 created "2016-06-24" @default.
• W2077691322 creator A5021877231 @default.
• W2077691322 creator A5059402356 @default.
• W2077691322 creator A5084725578 @default.
• W2077691322 date "2009-10-16" @default.
• W2077691322 modified "2023-10-18" @default.
• W2077691322 title "Multiple roles of the vesicular‐SNARE TI‐VAMP in post‐Golgi and endosomal trafficking" @default.
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