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| Content Provider | World Health Organization (WHO)-Global Index Medicus |
|---|---|
| Author | Aschrafi, A. Nicke, A. Betz, H. Gomeza, J. Horiuchi, M. Schmalzing, G. |
| Description | Author Affiliation: Horiuchi M ( Department of Neurochemistry, Max Planck Institute for Brain Research, Deutschordenstrasse 46, D-60528 Frankfurt am Main, Germany.); |
| Abstract | Na(+)/Cl(-)-dependent neurotransmitter transporters form a superfamily of transmembrane proteins that share 12 membrane-spanning regions. To gain information about the quaternary structure of these transporter proteins, we heterologously expressed the glial glycine transporter GlyT1 and its neuronal homolog GlyT2 in Xenopus oocytes. By using metabolic labeling with [(35)S]methionine or surface labeling with a plasma membrane impermeable reagent followed by affinity purification, we separately analyzed the total cellular pools of newly synthesized GlyTs and its functional plasma membrane-bound fractions. Upon blue native gel electrophoresis, the surface-localized transporter proteins were found to exist exclusively in complex-glycosylated monomeric form, whereas a significant fraction of the intracellular GlyT1 and GlyT2 was core-glycosylated and oligomeric. In contrast, even after treatment with the crosslinker glutaraldehyde, surface GlyTs failed to migrate as oligomeric proteins. These results indicate that plasma membrane-bound GlyT1 and GlyT2 are monomeric proteins. Thus, Na(+)/Cl(-)-dependent neurotransmitter transporters do not require oligomerization for substrate translocation. |
| ISSN | 00278424 |
| e-ISSN | 10916490 |
| Journal | Proceedings of the National Academy of Sciences of the United States of America |
| Issue Number | 4 |
| Volume Number | 98 |
| Language | English |
| Publisher | National Academy of Sciences |
| Publisher Date | 2001-02-01 |
| Publisher Place | United States |
| Access Restriction | Open |
| Subject Keyword | Amino Acid Transport Systems, Neutral Carrier Proteins Metabolism Glycine Membrane Proteins Animals Genetics Cell Membrane Glycine Plasma Membrane Transport Proteins Oligopeptides Oocytes Recombinant Fusion Proteins Xenopus Laevis Research Support, Non-U.S. Gov't Multidisciplinary |
| Content Type | Text |
| Resource Type | Article |
| Subject | Multidisciplinary |
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