| pubmed-article:18167356 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:18167356 | lifeskim:mentions | umls-concept:C0024660 | lld:lifeskim |
| pubmed-article:18167356 | lifeskim:mentions | umls-concept:C0014239 | lld:lifeskim |
| pubmed-article:18167356 | lifeskim:mentions | umls-concept:C0033684 | lld:lifeskim |
| pubmed-article:18167356 | lifeskim:mentions | umls-concept:C1538931 | lld:lifeskim |
| pubmed-article:18167356 | lifeskim:mentions | umls-concept:C1854053 | lld:lifeskim |
| pubmed-article:18167356 | lifeskim:mentions | umls-concept:C0061467 | lld:lifeskim |
| pubmed-article:18167356 | lifeskim:mentions | umls-concept:C0851285 | lld:lifeskim |
| pubmed-article:18167356 | lifeskim:mentions | umls-concept:C0205263 | lld:lifeskim |
| pubmed-article:18167356 | lifeskim:mentions | umls-concept:C0337094 | lld:lifeskim |
| pubmed-article:18167356 | pubmed:issue | 10 | lld:pubmed |
| pubmed-article:18167356 | pubmed:dateCreated | 2008-3-3 | lld:pubmed |
| pubmed-article:18167356 | pubmed:abstractText | GTRAP3-18 interacts with and reduces the activity of the neuronal specific Na(+)/K(+) glutamate transporter, EAAC1 both in vitro and in vivo. GTRAP3-18 and the related isoform, JM4, are distant relatives of the Rab GTPase-interacting factor PRA1, and share a topology of four transmembrane domains and cytosolic termini. GTRAP3-18 and JM4 are resident endoplasmic reticulum (ER) proteins. The physiological role of GTRAP3-18 is poorly understood. We demonstrate for the first time that GTRAP3-18 is a regulator of ER protein trafficking. Expression of GTRAP3-18 delays the ER exit of EAAC1, as well as other members of the excitatory amino acid transporter family. GTRAP3-18 uses hydrophobic domain interactions in the ER membrane to self-associate and cytoplasmic interactions at the C terminus to regulate trafficking. The features of GTRAP3-18 activity are consistent with recent phylogenic sequence analyses suggesting GTRAP3-18 and JM4 be reclassified as mammalian isoforms of the yeast protein family Yip, Yip6b, and Yip6a, respectively. | lld:pubmed |
| pubmed-article:18167356 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:18167356 | pubmed:language | eng | lld:pubmed |
| pubmed-article:18167356 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:18167356 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:18167356 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:18167356 | pubmed:month | Mar | lld:pubmed |
| pubmed-article:18167356 | pubmed:issn | 0021-9258 | lld:pubmed |
| pubmed-article:18167356 | pubmed:author | pubmed-author:RothsteinJeff... | lld:pubmed |
| pubmed-article:18167356 | pubmed:author | pubmed-author:RobinsonMicha... | lld:pubmed |
| pubmed-article:18167356 | pubmed:author | pubmed-author:SitteHarald... | lld:pubmed |
| pubmed-article:18167356 | pubmed:author | pubmed-author:LiuYitingY | lld:pubmed |
| pubmed-article:18167356 | pubmed:author | pubmed-author:FarhanHessoH | lld:pubmed |
| pubmed-article:18167356 | pubmed:author | pubmed-author:VidenskySvetl... | lld:pubmed |
| pubmed-article:18167356 | pubmed:author | pubmed-author:MaierSusanneS | lld:pubmed |
| pubmed-article:18167356 | pubmed:author | pubmed-author:JungElizabeth... | lld:pubmed |
| pubmed-article:18167356 | pubmed:author | pubmed-author:RuggieroAlici... | lld:pubmed |
| pubmed-article:18167356 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:18167356 | pubmed:day | 7 | lld:pubmed |
| pubmed-article:18167356 | pubmed:volume | 283 | lld:pubmed |
| pubmed-article:18167356 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:18167356 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:18167356 | pubmed:pagination | 6175-83 | lld:pubmed |
| pubmed-article:18167356 | pubmed:dateRevised | 2011-4-6 | lld:pubmed |
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| pubmed-article:18167356 | pubmed:year | 2008 | lld:pubmed |
| pubmed-article:18167356 | pubmed:articleTitle | The endoplasmic reticulum exit of glutamate transporter is regulated by the inducible mammalian Yip6b/GTRAP3-18 protein. | lld:pubmed |
| pubmed-article:18167356 | pubmed:affiliation | Department of Neuroscience, Johns Hopkins University, 625 N. Wolfe Street, Baltimore, MD 21287, USA. | lld:pubmed |
| pubmed-article:18167356 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:18167356 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| pubmed-article:18167356 | pubmed:publicationType | Research Support, N.I.H., Extramural | lld:pubmed |
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