Multiple roles of the vesicular-SNARE TI-VAMP in post-Golgi and endosomal trafficking - PubMed (original) (raw)
Review
. 2009 Dec 3;583(23):3817-26.
doi: 10.1016/j.febslet.2009.10.026. Epub 2009 Oct 20.
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- PMID: 19837067
- DOI: 10.1016/j.febslet.2009.10.026
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Review
Multiple roles of the vesicular-SNARE TI-VAMP in post-Golgi and endosomal trafficking
Mathilde Chaineau et al. FEBS Lett. 2009.
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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.
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