Vesicular GABA transporter (VGAT) transports β-alanine

Narinobu Juge, Hiroshi Omote, Yoshinori Moriyama

Research output: Contribution to journalArticle

8 Citations (Scopus)

Abstract

Vesicular GABA transporter (VGAT) is expressed in GABAergic and glycinergic neurons, and is responsible for vesicular storage and subsequent exocytosis of these inhibitory amino acids. In this study, we show that VGAT recognizes β-alanine as a substrate. Proteoliposomes containing purified VGAT transport β-alanine using Δψ but not ΔpH as a driving force. The Δψ-driven β-alanine uptake requires Cl-. VGAT also facilitates Cl- uptake in the presence of β-alanine. A previously described VGAT mutant (Glu213Ala) that disrupts GABA and glycine transport similarly abrogates β-alanine uptake. These findings indicated that VGAT transports β-alanine through a mechanism similar to those for GABA and glycine, and functions as a vesicular β-alanine transporter. Vesicular GABA transporter (VGAT) is expressed in GABAergic and glycinergic neurons, and is responsible for vesicular storage and subsequent exocytosis of these inhibitory amino acids. In the present study, we showed that proteoliposomes containing purified VGAT transport β-alanine using Δψ as a driving force. VGAT also facilitates Cl- uptake. Our findings indicated that VGAT functions as a vesicular β-alanine transporter. Vesicular GABA transporter (VGAT) is expressed in GABAergic and glycinergic neurons, and is responsible for vesicular storage and subsequent exocytosis of these inhibitory amino acids. In the present study, we showed that proteoliposomes containing purified VGAT transport β-alanine using Δψ as a driving force. VGAT also facilitates Cl- uptake. Our findings indicated that VGAT functions as a vesicular β-alanine transporter.

Original languageEnglish
Pages (from-to)482-486
Number of pages5
JournalJournal of Neurochemistry
Volume127
Issue number4
DOIs
Publication statusPublished - Nov 2013

Fingerprint

Alanine
GABAergic Neurons
Exocytosis
Neurons
vesicular GABA transporter
Amino Acids
Glycine
gamma-Aminobutyric Acid

Keywords

  • β-alanine
  • taurine
  • vesicular GABA transporter

ASJC Scopus subject areas

  • Biochemistry
  • Cellular and Molecular Neuroscience

Cite this

Vesicular GABA transporter (VGAT) transports β-alanine. / Juge, Narinobu; Omote, Hiroshi; Moriyama, Yoshinori.

In: Journal of Neurochemistry, Vol. 127, No. 4, 11.2013, p. 482-486.

Research output: Contribution to journalArticle

@article{7a412bddf05e4f70a7ffb674b14fd424,
title = "Vesicular GABA transporter (VGAT) transports β-alanine",
abstract = "Vesicular GABA transporter (VGAT) is expressed in GABAergic and glycinergic neurons, and is responsible for vesicular storage and subsequent exocytosis of these inhibitory amino acids. In this study, we show that VGAT recognizes β-alanine as a substrate. Proteoliposomes containing purified VGAT transport β-alanine using Δψ but not ΔpH as a driving force. The Δψ-driven β-alanine uptake requires Cl-. VGAT also facilitates Cl- uptake in the presence of β-alanine. A previously described VGAT mutant (Glu213Ala) that disrupts GABA and glycine transport similarly abrogates β-alanine uptake. These findings indicated that VGAT transports β-alanine through a mechanism similar to those for GABA and glycine, and functions as a vesicular β-alanine transporter. Vesicular GABA transporter (VGAT) is expressed in GABAergic and glycinergic neurons, and is responsible for vesicular storage and subsequent exocytosis of these inhibitory amino acids. In the present study, we showed that proteoliposomes containing purified VGAT transport β-alanine using Δψ as a driving force. VGAT also facilitates Cl- uptake. Our findings indicated that VGAT functions as a vesicular β-alanine transporter. Vesicular GABA transporter (VGAT) is expressed in GABAergic and glycinergic neurons, and is responsible for vesicular storage and subsequent exocytosis of these inhibitory amino acids. In the present study, we showed that proteoliposomes containing purified VGAT transport β-alanine using Δψ as a driving force. VGAT also facilitates Cl- uptake. Our findings indicated that VGAT functions as a vesicular β-alanine transporter.",
keywords = "β-alanine, taurine, vesicular GABA transporter",
author = "Narinobu Juge and Hiroshi Omote and Yoshinori Moriyama",
year = "2013",
month = "11",
doi = "10.1111/jnc.12393",
language = "English",
volume = "127",
pages = "482--486",
journal = "Journal of Neurochemistry",
issn = "0022-3042",
publisher = "Wiley-Blackwell",
number = "4",

}

TY - JOUR

T1 - Vesicular GABA transporter (VGAT) transports β-alanine

AU - Juge, Narinobu

AU - Omote, Hiroshi

AU - Moriyama, Yoshinori

PY - 2013/11

Y1 - 2013/11

N2 - Vesicular GABA transporter (VGAT) is expressed in GABAergic and glycinergic neurons, and is responsible for vesicular storage and subsequent exocytosis of these inhibitory amino acids. In this study, we show that VGAT recognizes β-alanine as a substrate. Proteoliposomes containing purified VGAT transport β-alanine using Δψ but not ΔpH as a driving force. The Δψ-driven β-alanine uptake requires Cl-. VGAT also facilitates Cl- uptake in the presence of β-alanine. A previously described VGAT mutant (Glu213Ala) that disrupts GABA and glycine transport similarly abrogates β-alanine uptake. These findings indicated that VGAT transports β-alanine through a mechanism similar to those for GABA and glycine, and functions as a vesicular β-alanine transporter. Vesicular GABA transporter (VGAT) is expressed in GABAergic and glycinergic neurons, and is responsible for vesicular storage and subsequent exocytosis of these inhibitory amino acids. In the present study, we showed that proteoliposomes containing purified VGAT transport β-alanine using Δψ as a driving force. VGAT also facilitates Cl- uptake. Our findings indicated that VGAT functions as a vesicular β-alanine transporter. Vesicular GABA transporter (VGAT) is expressed in GABAergic and glycinergic neurons, and is responsible for vesicular storage and subsequent exocytosis of these inhibitory amino acids. In the present study, we showed that proteoliposomes containing purified VGAT transport β-alanine using Δψ as a driving force. VGAT also facilitates Cl- uptake. Our findings indicated that VGAT functions as a vesicular β-alanine transporter.

AB - Vesicular GABA transporter (VGAT) is expressed in GABAergic and glycinergic neurons, and is responsible for vesicular storage and subsequent exocytosis of these inhibitory amino acids. In this study, we show that VGAT recognizes β-alanine as a substrate. Proteoliposomes containing purified VGAT transport β-alanine using Δψ but not ΔpH as a driving force. The Δψ-driven β-alanine uptake requires Cl-. VGAT also facilitates Cl- uptake in the presence of β-alanine. A previously described VGAT mutant (Glu213Ala) that disrupts GABA and glycine transport similarly abrogates β-alanine uptake. These findings indicated that VGAT transports β-alanine through a mechanism similar to those for GABA and glycine, and functions as a vesicular β-alanine transporter. Vesicular GABA transporter (VGAT) is expressed in GABAergic and glycinergic neurons, and is responsible for vesicular storage and subsequent exocytosis of these inhibitory amino acids. In the present study, we showed that proteoliposomes containing purified VGAT transport β-alanine using Δψ as a driving force. VGAT also facilitates Cl- uptake. Our findings indicated that VGAT functions as a vesicular β-alanine transporter. Vesicular GABA transporter (VGAT) is expressed in GABAergic and glycinergic neurons, and is responsible for vesicular storage and subsequent exocytosis of these inhibitory amino acids. In the present study, we showed that proteoliposomes containing purified VGAT transport β-alanine using Δψ as a driving force. VGAT also facilitates Cl- uptake. Our findings indicated that VGAT functions as a vesicular β-alanine transporter.

KW - β-alanine

KW - taurine

KW - vesicular GABA transporter

UR - http://www.scopus.com/inward/record.url?scp=84887079473&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=84887079473&partnerID=8YFLogxK

U2 - 10.1111/jnc.12393

DO - 10.1111/jnc.12393

M3 - Article

C2 - 23919636

AN - SCOPUS:84887079473

VL - 127

SP - 482

EP - 486

JO - Journal of Neurochemistry

JF - Journal of Neurochemistry

SN - 0022-3042

IS - 4

ER -