Glycine transporter dimers: Evidence for occurrence in the plasma membrane

Bartholomaus, Ingo, Milan-Lobo, Laura, Nicke, Annette, Dutertre, Sebastien, Hastrup, Hanne, Jha, Alok, Gether, Ulrik, Sitte, Harald H., Betz, Heinrich and Eulenburg, Volker (2008) Glycine transporter dimers: Evidence for occurrence in the plasma membrane. Journal of Biological Chemistry, 283 16: 10978-10991. doi:10.1074/jbc.M800622200

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Author Bartholomaus, Ingo
Milan-Lobo, Laura
Nicke, Annette
Dutertre, Sebastien
Hastrup, Hanne
Jha, Alok
Gether, Ulrik
Sitte, Harald H.
Betz, Heinrich
Eulenburg, Volker
Title Glycine transporter dimers: Evidence for occurrence in the plasma membrane
Journal name Journal of Biological Chemistry   Check publisher's open access policy
ISSN 0021-9258
Publication date 2008-04-18
Sub-type Article (original research)
DOI 10.1074/jbc.M800622200
Open Access Status File (Publisher version)
Volume 283
Issue 16
Start page 10978
End page 10991
Total pages 14
Place of publication Bethesda, MD, United States
Publisher American Society for Biochemistry and Molecular Biology
Language eng
Formatted abstract
Different Na+/Cl--dependent neurotransmitter transporters of the SLC6a family have been shown to form dimers or oligomers in both intracellular compartments and at the cell surface. In contrast, the glycine transporters (GlyTs) GlyT1 and -2 have been reported to exist as monomers in the plasma membrane based on hydrodynamic and native gel electrophoretic studies. Here, we used cysteine substitution and oxidative cross-linking to show that of GlyT1 and GlyT2 also form dimeric complexes within the plasma membrane. GlyT oligomerization at the cell surface was confirmed for both GlyT1 and GlyT2 by fluorescence resonance energy transfer microscopy. Endoglycosidase treatment and surface biotinylation further revealed that complex-glycosylated GlyTs form dimers located at the cell surface. Furthermore, substitution of tryptophan 469 of GlyT2 by an arginine generated a transporter deficient in dimerization that was retained intracellulary. Based on these results and GlyT structures modeled by using the crystal structure of the bacterial homolog LeuTAa, as a template, residues located within the extracellular loop 3 and at the beginning of transmembrane domain 6 are proposed to contribute to the dimerization interface of GlyTs.
Q-Index Code C1
Q-Index Status Provisional Code
Institutional Status Non-UQ

Document type: Journal Article
Sub-type: Article (original research)
Collections: ERA 2012 Admin Only
Institute for Molecular Bioscience - Publications
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Citation counts: TR Web of Science Citation Count  Cited 32 times in Thomson Reuters Web of Science Article | Citations
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Created: Thu, 13 Oct 2011, 13:57:55 EST by Mr Sebastien Dutertre on behalf of Institute for Molecular Bioscience