RGD Reference Report - Vesicular glutamate transporter contains two independent transport machineries. - Rat Genome Database

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Vesicular glutamate transporter contains two independent transport machineries.

Authors: Juge, Narinobu  Yoshida, Yumi  Yatsushiro, Shouki  Omote, Hiroshi  Moriyama, Yoshinori 
Citation: Juge N, etal., J Biol Chem. 2006 Dec 22;281(51):39499-506. doi: 10.1074/jbc.M607670200. Epub 2006 Oct 17.
RGD ID: 151665738
Pubmed: PMID:17046815   (View Abstract at PubMed)
DOI: DOI:10.1074/jbc.M607670200   (Journal Full-text)

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 F(o)F(1)-ATPase (F-ATPase) into liposomes. Upon the addition of ATP, the proteoliposomes facilitated l-glutamate uptake in a membrane potential (DeltaPsi)-dependent fashion. The ATP-dependent l-glutamate uptake exhibited an absolute requirement for approximately 4 mm Cl(-), was sensitive to Evans blue, but was insensitive to d,l-aspartate. VGLUT2s with mutations in the transmembrane-located residues Arg(184), His(128), and Glu(191) showed a dramatic loss in l-glutamate transport activity, whereas Na(+)-dependent inorganic phosphate (P(i)) uptake remained comparable to that of the wild type. Furthermore, P(i) 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 DeltaPsi-dependent l-glutamate uptake and a Na(+)-dependent P(i) uptake.



Gene Ontology Annotations    Click to see Annotation Detail View

Biological Process

  
Object SymbolSpeciesTermQualifierEvidenceWithNotesSourceOriginal Reference(s)
Slc17a6RatL-glutamate transmembrane transport involved_inIDA PMID:17046815UniProt 
Slc17a6Ratsodium-dependent phosphate transport involved_inIDA PMID:17046815UniProt 

Molecular Function

  
Object SymbolSpeciesTermQualifierEvidenceWithNotesSourceOriginal Reference(s)
Slc17a6RatL-glutamate uniporter activity enablesIDA PMID:17046815UniProt 
Slc17a6Ratsodium:phosphate symporter activity enablesIDA PMID:17046815UniProt 

Objects Annotated

Genes (Rattus norvegicus)
Slc17a6  (solute carrier family 17 member 6)


Additional Information