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

Jacqueline Vinatier, Etienne Herzog, Marie-Aude Plamont, Sonja M. Wojcik, Anne Schmidt, Nils Brose, Laurent Daviet, Salah El Mestikawy, Bruno Giros
J Neurochem. 2006-05-01; 97(4): 1111-1125
DOI: 10.1111/j.1471-4159.2006.03821.x

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1. J Neurochem. 2006 May;97(4):1111-25. Epub 2006 Apr 5.

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

Vinatier J(1), Herzog E, Plamont MA, Wojcik SM, Schmidt A, Brose N, Daviet L, El
Mestikawy S, Giros B.

Author information:
(1)INSERM U513, Neurobiology and Psychiatry, Faculté de Médecine, Créteil,
France.

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.

DOI: 10.1111/j.1471-4159.2006.03821.x
PMID: 16606361 [Indexed for MEDLINE]

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