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Sept8 controls the binding of vesicle-associated membrane protein 2 to synaptophysin
- Source :
- Journal of Neurochemistry. 108:867-880
- Publication Year :
- 2009
- Publisher :
- Wiley, 2009.
-
Abstract
- Septins, a conserved family of GTP/GDP-binding proteins, are present in organisms as diverse as yeast and mammals. We analyzed the distribution of five septins, Sept6, Sept7, Sept8, Sept9 and Sept11, in various rat tissues by western blot analyses and found all septins to be expressed in brain. We also examined the developmental changes of expression of these septins in the rat brain and found that the level of Sept8 increased during post-natal development. Morphological analyses revealed that Sept8 is enriched at pre-synapses. Using yeast two-hybrid screening, we identified vesicle-associated membrane protein 2 (VAMP2), a soluble N-ethylmaleimide-sensitive factor attachment protein receptor (SNARE), as an interacting protein for Sept8. Synaptophysin is reported to associate with and recruit VAMP2 to synaptic vesicles and dissociate prior to forming the SNARE complex consisting of VAMP2, syntaxin and synaptosome-associated protein of 25 kDa. We showed that Sept8 suppresses the interaction between VAMP2 and synaptophysin through binding to VAMP2. In addition, we found that Sept8 forms a complex with syntaxin1A, and the Sept8-VAMP2 interaction is disrupted by synaptosome-associated protein of 25 kDa. These results suggest that Sept8 may participate in the process of the SNARE complex formation and subsequent neurotransmitter release.
- Subjects :
- Male
Synaptosomal-Associated Protein 25
Vesicle-Associated Membrane Protein 2
Presynaptic Terminals
Synaptic Membranes
Synaptophysin
Syntaxin 1
Septin
Membrane Fusion
Synaptic Transmission
Biochemistry
Exocytosis
Cell Line
GTP Phosphohydrolases
Cellular and Molecular Neuroscience
GTP-Binding Proteins
Animals
Syntaxin
biology
VAMP2
Binding protein
Brain
Membrane Proteins
Rats
Cell biology
Membrane protein
biology.protein
Female
Synaptic Vesicles
sense organs
biological phenomena, cell phenomena, and immunity
SNARE Proteins
SNARE complex
Septins
Protein Binding
Subcellular Fractions
Subjects
Details
- ISSN :
- 14714159 and 00223042
- Volume :
- 108
- Database :
- OpenAIRE
- Journal :
- Journal of Neurochemistry
- Accession number :
- edsair.doi.dedup.....01b3941d081a6106200e6058d0849d7a