Transmembrane topology of vesicular glutamate transporter 2

Biological & Pharmaceutical Bulletin
Sun-Kyung JungHiroshi Omote

Abstract

Vesicular glutamate transporter (VGLUT) plays an essential role in L-glutamate signaling in neurons and some peripheral tissues through vesicular storage of L-glutamate in secretory vesicles. To investigate the topology of VGLUT in membranes, we prepared site-directed antibodies against the amino-terminal (anti-N), 1st putative loop (anti-L), and carboxyl terminal (anti-C) regions. None of the antibodies reacted with VGLUT2 expressed in COS cells because they could not gain access to the antigen. However, both the anti-N and anti-C antibodies recognized VGLUT2 when the cells were permeabilized with digitonin, while the anti-L antibodies did not. Immunological reactivity to anti-L-antibodies appeared when the cells were permeabilized with Triton X-100. These results suggest that both the amino-terminal and carboxyl-terminal regions of VGLUT2 in membranes face the cytoplasm while the 1st loop faces the lumen.

References

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Citations

Aug 3, 2011·Neurobiology of Disease·Andrea C LoboCarlos B Duarte
May 30, 2008·Traffic·Hao FeiDavid E Krantz
Mar 31, 2007·Journal of Neurochemistry·Hao FeiDavid E Krantz
Jul 31, 2007·Protein Science : a Publication of the Protein Society·Jonas AlmqvistSven Hovmöller
Oct 19, 2006·The Journal of Biological Chemistry·Narinobu JugeYoshinori Moriyama
Feb 18, 2020·Brain Structure & Function·Jose L Lanciego, Floris G Wouterlood
Jun 16, 2017·Purinergic Signalling·Yoshinori MoriyamaMasatoshi Nomura
May 4, 2011·Biochemistry·Alexis GonzalezCarlos B Gonzalez

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