Multiple roles of the vesicular-SNARE TI-VAMP in post-Golgi and endosomal trafficking.
FEBS Lett
; 583(23): 3817-26, 2009 Dec 03.
Article
in En
| MEDLINE
| ID: mdl-19837067
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.
Full text:
1
Collection:
01-internacional
Database:
MEDLINE
Main subject:
Endosomes
/
Tetanus Toxin
/
Metalloendopeptidases
/
SNARE Proteins
/
Golgi Apparatus
Limits:
Animals
/
Humans
Language:
En
Journal:
FEBS Lett
Year:
2009
Document type:
Article
Affiliation country:
France