| pubmed-article:15794750 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:15794750 | lifeskim:mentions | umls-concept:C0035820 | lld:lifeskim |
| pubmed-article:15794750 | lifeskim:mentions | umls-concept:C0060919 | lld:lifeskim |
| pubmed-article:15794750 | lifeskim:mentions | umls-concept:C0441655 | lld:lifeskim |
| pubmed-article:15794750 | lifeskim:mentions | umls-concept:C0205360 | lld:lifeskim |
| pubmed-article:15794750 | lifeskim:mentions | umls-concept:C0599896 | lld:lifeskim |
| pubmed-article:15794750 | lifeskim:mentions | umls-concept:C0205088 | lld:lifeskim |
| pubmed-article:15794750 | pubmed:issue | 7 | lld:pubmed |
| pubmed-article:15794750 | pubmed:dateCreated | 2005-3-29 | lld:pubmed |
| pubmed-article:15794750 | pubmed:abstractText | Neurotransmitter transporters play a major role in achieving low concentrations of their respective transmitter in the synaptic cleft. The GABA transporter GAT1 belongs to the family of Na(+)- and Cl(-)-coupled transport proteins which possess 12 putative transmembrane domains and three N-glycosylation sites in the extracellular loop between transmembrane domain 3 and 4. To study the significance of N-glycosylation, green fluorescence protein (GFP)-tagged wild type GAT1 (NNN) and N-glycosylation defective mutants (DDQ, DGN, DDN and DDG) were expressed in CHO cells. Compared with the wild type, all N-glycosylation mutants showed strongly reduced protein stability and trafficking to the plasma membrane, which however were not affected by 1-deoxymannojirimycin (dMM). This indicates that N-glycosylation, but not terminal trimming of the N-glycans is involved in the attainment of a correctly folded and stable conformation of GAT1. All N-glycosylation mutants were expressed on the plasma membrane, but they displayed markedly reduced GABA-uptake activity. Also, inhibition of oligosaccharide processing by dMM led to reduction of this activity. Further experiments showed that both N-glycosylation mutations and dMM reduced the V(max) value, while not increasing the K(m) value for GABA uptake. Electrical measurements revealed that the reduced transport activity can be partially attributed to a reduced apparent affinity for extracellular Na+ and slowed kinetics of the transport cycle. This indicates that N-glycans, in particular their terminal trimming, are important for the GABA-uptake activity of GAT1. They play a regulatory role in the GABA translocation by affecting the affinity and the reaction steps associated with the sodium ion binding. | lld:pubmed |
| pubmed-article:15794750 | pubmed:language | eng | lld:pubmed |
| pubmed-article:15794750 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15794750 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:15794750 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15794750 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:15794750 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15794750 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15794750 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15794750 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15794750 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15794750 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15794750 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:15794750 | pubmed:month | Apr | lld:pubmed |
| pubmed-article:15794750 | pubmed:issn | 1742-464X | lld:pubmed |
| pubmed-article:15794750 | pubmed:author | pubmed-author:OhlS ASA | lld:pubmed |
| pubmed-article:15794750 | pubmed:author | pubmed-author:ReutterWerner... | lld:pubmed |
| pubmed-article:15794750 | pubmed:author | pubmed-author:SchüleinRalfR | lld:pubmed |
| pubmed-article:15794750 | pubmed:author | pubmed-author:SchwarzWolfga... | lld:pubmed |
| pubmed-article:15794750 | pubmed:author | pubmed-author:FeiJianJ | lld:pubmed |
| pubmed-article:15794750 | pubmed:author | pubmed-author:CaiGuoqiangG | lld:pubmed |
| pubmed-article:15794750 | pubmed:author | pubmed-author:SalonikidisPe... | lld:pubmed |
| pubmed-article:15794750 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:15794750 | pubmed:volume | 272 | lld:pubmed |
| pubmed-article:15794750 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:15794750 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:15794750 | pubmed:pagination | 1625-38 | lld:pubmed |
| pubmed-article:15794750 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
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| pubmed-article:15794750 | pubmed:meshHeading | pubmed-meshheading:15794750... | lld:pubmed |
| pubmed-article:15794750 | pubmed:meshHeading | pubmed-meshheading:15794750... | lld:pubmed |
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| pubmed-article:15794750 | pubmed:meshHeading | pubmed-meshheading:15794750... | lld:pubmed |
| pubmed-article:15794750 | pubmed:year | 2005 | lld:pubmed |
| pubmed-article:15794750 | pubmed:articleTitle | The role of N-glycosylation in the stability, trafficking and GABA-uptake of GABA-transporter 1. Terminal N-glycans facilitate efficient GABA-uptake activity of the GABA transporter. | lld:pubmed |
| pubmed-article:15794750 | pubmed:affiliation | Institute of Biochemistry and Cell Biology, SIBS, CAS, Shanghai, China. | lld:pubmed |
| pubmed-article:15794750 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:15794750 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:15794750 | lld:pubmed |
