Transmembrane topology of vesicular glutamate transporter 2

Sun Kyung Jung, Riyo Morimoto, Masato Otsuka, Hiroshi Omote

Research output: Contribution to journalArticlepeer-review

18 Citations (Scopus)

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.

Original languageEnglish
Pages (from-to)547-549
Number of pages3
JournalBiological and Pharmaceutical Bulletin
Volume29
Issue number3
DOIs
Publication statusPublished - Mar 2006

Keywords

  • L-glutamate
  • Secretory vesicle
  • Topology
  • Vesicular glutamate transporter

ASJC Scopus subject areas

  • Pharmacology
  • Pharmaceutical Science

Fingerprint

Dive into the research topics of 'Transmembrane topology of vesicular glutamate transporter 2'. Together they form a unique fingerprint.

Cite this