Vesicular glutamate transporter contains two independent transport machineries

Narinobu Juge, Yumi Yoshida, Shouki Yatsushiro, Hiroshi Omote, Yoshinori Moriyama


100 被引用数 (Scopus)


Vesicular glutamate transporters (VGLUTs) are responsible for the vesicular storage of L-glutamate and play an essential role in glutamatergic signal transmission in the central nervous system. The molecular mechanism of the transport remains unknown. Here, we established a novel in vitro assay procedure, which includes purification of wild and mutant VGLUT2 and their reconstitution with purified bacterial FoF1-ATPase (F-ATPase) into liposomes. Upon the addition of ATP, the proteoliposomes facilitated L-glutamate uptake in a membrane potential (Δψ)-dependent fashion. The ATP-dependent L-glutamate uptake exhibited an absolute requirement for ∼4 mM Cl-, was sensitive to Evans blue, but was insensitive to D,L-aspartate. VGLUT2s with mutations in the transmembrane-located residues Arg184, His128, and Glu191 showed a dramatic loss in L-glutamate transport activity, whereas Na+-dependent inorganic phosphate (Pi) uptake remained comparable to that of the wild type. Furthermore, Pi transport did not require Cl- and was not inhibited by Evans blue. Thus, VGLUT2 appears to possess two intrinsic transport machineries that are independent of each other: a Δψ-dependent L-glutamate uptake and a Na+-dependent P i uptake.

ジャーナルJournal of Biological Chemistry
出版ステータスPublished - 12月 22 2006

ASJC Scopus subject areas

  • 生化学
  • 分子生物学
  • 細胞生物学


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