| pubmed-article:16446503 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:16446503 | lifeskim:mentions | umls-concept:C0086418 | lld:lifeskim |
| pubmed-article:16446503 | lifeskim:mentions | umls-concept:C0032098 | lld:lifeskim |
| pubmed-article:16446503 | lifeskim:mentions | umls-concept:C0005528 | lld:lifeskim |
| pubmed-article:16446503 | lifeskim:mentions | umls-concept:C0596902 | lld:lifeskim |
| pubmed-article:16446503 | lifeskim:mentions | umls-concept:C1412390 | lld:lifeskim |
| pubmed-article:16446503 | lifeskim:mentions | umls-concept:C0002611 | lld:lifeskim |
| pubmed-article:16446503 | lifeskim:mentions | umls-concept:C0441712 | lld:lifeskim |
| pubmed-article:16446503 | pubmed:issue | 2 | lld:pubmed |
| pubmed-article:16446503 | pubmed:dateCreated | 2006-1-31 | lld:pubmed |
| pubmed-article:16446503 | pubmed:abstractText | The conserved family of AMT/Rh proteins facilitates ammonium transport across animal, plant, and microbial membranes. A bacterial homologue, AmtB, forms a channel-like structure and appears to function as an NH3 gas channel. To evaluate the function of eukaryotic homologues, the human RhCG glycoprotein and the tomato plant ammonium transporter LeAMT1;2 were expressed and compared in Xenopus oocytes and yeast. RhCG mediated the electroneutral transport of methylammonium (MeA), which saturated with Km = 3.8 mM at pHo 7.5. Uptake was strongly favored by increasing the pHo and was inhibited by ammonium. Ammonium induced rapid cytosolic alkalinization in RhCG-expressing oocytes. Additionally, RhCG expression was associated with an alkali-cation conductance, which was not significantly permeable to NH4+ and was apparently uncoupled from the ammonium transport. In contrast, expression of the homologous LeAMT1;2 induced pHo-independent MeA+ uptake and specific NH4+ and MeA+ currents that were distinct from endogenous currents. The different mechanisms of transport, including the RhCG-associated alkali-cation conductance, were verified by heterologous expression in appropriate yeast strains. Thus, homologous AMT/Rh-type proteins function in a distinct manner; while LeAMT1;2 carries specifically NH4+, or cotransports NH3/H+, RhCG mediates electroneutral NH3 transport. | lld:pubmed |
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| pubmed-article:16446503 | pubmed:language | eng | lld:pubmed |
| pubmed-article:16446503 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16446503 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:16446503 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:16446503 | pubmed:month | Feb | lld:pubmed |
| pubmed-article:16446503 | pubmed:issn | 0022-1295 | lld:pubmed |
| pubmed-article:16446503 | pubmed:author | pubmed-author:MoeP WPW | lld:pubmed |
| pubmed-article:16446503 | pubmed:author | pubmed-author:CartronJean-P... | lld:pubmed |
| pubmed-article:16446503 | pubmed:author | pubmed-author:LudewigUweU | lld:pubmed |
| pubmed-article:16446503 | pubmed:author | pubmed-author:MouroIsabelle... | lld:pubmed |
| pubmed-article:16446503 | pubmed:author | pubmed-author:ColinYvesY | lld:pubmed |
| pubmed-article:16446503 | pubmed:author | pubmed-author:LopezClaudeC | lld:pubmed |
| pubmed-article:16446503 | pubmed:author | pubmed-author:SchaafGabriel... | lld:pubmed |
| pubmed-article:16446503 | pubmed:author | pubmed-author:NeumannPetraP | lld:pubmed |
| pubmed-article:16446503 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:16446503 | pubmed:volume | 127 | lld:pubmed |
| pubmed-article:16446503 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:16446503 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:16446503 | pubmed:pagination | 133-44 | lld:pubmed |
| pubmed-article:16446503 | pubmed:dateRevised | 2010-9-20 | lld:pubmed |
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| pubmed-article:16446503 | pubmed:meshHeading | pubmed-meshheading:16446503... | lld:pubmed |
| pubmed-article:16446503 | pubmed:year | 2006 | lld:pubmed |
| pubmed-article:16446503 | pubmed:articleTitle | Different transport mechanisms in plant and human AMT/Rh-type ammonium transporters. | lld:pubmed |
| pubmed-article:16446503 | pubmed:affiliation | Zentrum für Molekularbiologie der Pflanzen, Pflanzenphysiologie, Universität Tübingen, Tübingen, Germany. | lld:pubmed |
| pubmed-article:16446503 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:16446503 | pubmed:publicationType | Comparative Study | lld:pubmed |
| pubmed-article:16446503 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
