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  Interaction between the vesicular glutamate transporter type 1 and endophilin A1, a protein essential for endocytosis

Vinatier, J., Herzog, E., Plamont, M.-A., Wojcik, S. M., Schmidt, A., Brose, N., et al. (2006). Interaction between the vesicular glutamate transporter type 1 and endophilin A1, a protein essential for endocytosis. Journal of Neurochemistry, 97(4), 1111-1125. doi:10.1111/j.1471-4159.2006.0381.x.

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 Creators:
Vinatier, Jacqueline, Author
Herzog, Etienne1, Author              
Plamont, Marie-Aude, Author
Wojcik, Sonja M.1, Author              
Schmidt, Anne, Author
Brose, Nils1, Author              
Daviet, Laurent, Author
El Mestikawy, Salah, Author
Giros, Bruno, Author
Affiliations:
1Molecular neurobiology, Max Planck Institute of Experimental Medicine, Max Planck Society, ou_2173659              

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Free keywords: endophilin; interaction; synaptic vesicle recycling; vesicular glutamate transporter CENTRAL-NERVOUS-SYSTEM; INORGANIC-PHOSPHATE COTRANSPORTER; SYNAPTIC VESICLE ENDOCYTOSIS; DOMAIN-CONTAINING PROTEINS; ACETYLCHOLINE TRANSPORTER; BINDING PARTNERS; SH3 DOMAIN; MONOAMINE TRANSPORTER-2; EXCITATORY NEURONS; MEMBRANE CURVATURE
 Abstract: In the nerve terminal, neurotransmitter is actively packaged into synaptic vesicles before its release by Ca2+-dependent exocytosis. The three vesicular glutamate transporters (VGLUT1, -2 and -3) are highly conserved proteins that display similar bioenergetic and pharmacological properties but are expressed in different brain areas. We used the divergent C-terminus of VGLUT1 as a bait in a yeast two-hybrid screen to identify and map the interaction between a proline-rich domain of VGLUT1 and the Src homology domain 3 (SH3) domain of endophilin. We further confirmed this interaction by using different glutathione-S-transferase-endophilin fusion proteins to pull down VGLUT1 from rat brain extracts. The expression profiles of the two genes and proteins were compared on rat brain sections, showing that endophilin is most highly expressed in regions and cells expressing VGLUT1. Double immunofluorescence in the rat cerebellum shows that most VGLUT1-positive terminals co-express endophilin, whereas VGLUT2-expressing terminals are often devoid of endophilin. However, neither VGLUT1 transport activity, endophilin enzymatic activity nor VGLUT1 synaptic targeting were altered by this interaction. Overall, the discovery of endophilin as a partner for VGLUT1 in nerve terminals strongly suggests the existence of functional differences between VGLUT1 and -2 terminals in their abilities to replenish vesicle pools.

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Language(s): eng - English
 Dates: 2006-05
 Publication Status: Published in print
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 Rev. Type: Peer
 Identifiers: eDoc: 292185
ISI: 000237063200020
ISI: 000237063200020
DOI: 10.1111/j.1471-4159.2006.0381.x
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Title: Journal of Neurochemistry
  Alternative Title : J. Neurochem.
Source Genre: Journal
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Pages: - Volume / Issue: 97 (4) Sequence Number: - Start / End Page: 1111 - 1125 Identifier: ISSN: 0022-3042