pubmed-article:20943949 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:20943949 | lifeskim:mentions | umls-concept:C0033684 | lld:lifeskim |
pubmed-article:20943949 | lifeskim:mentions | umls-concept:C0001479 | lld:lifeskim |
pubmed-article:20943949 | lifeskim:mentions | umls-concept:C0001443 | lld:lifeskim |
pubmed-article:20943949 | lifeskim:mentions | umls-concept:C0001473 | lld:lifeskim |
pubmed-article:20943949 | lifeskim:mentions | umls-concept:C0332281 | lld:lifeskim |
pubmed-article:20943949 | lifeskim:mentions | umls-concept:C0017262 | lld:lifeskim |
pubmed-article:20943949 | lifeskim:mentions | umls-concept:C1426056 | lld:lifeskim |
pubmed-article:20943949 | lifeskim:mentions | umls-concept:C0205148 | lld:lifeskim |
pubmed-article:20943949 | lifeskim:mentions | umls-concept:C0851285 | lld:lifeskim |
pubmed-article:20943949 | lifeskim:mentions | umls-concept:C0086597 | lld:lifeskim |
pubmed-article:20943949 | lifeskim:mentions | umls-concept:C0597484 | lld:lifeskim |
pubmed-article:20943949 | lifeskim:mentions | umls-concept:C2911684 | lld:lifeskim |
pubmed-article:20943949 | lifeskim:mentions | umls-concept:C0185117 | lld:lifeskim |
pubmed-article:20943949 | pubmed:issue | 24 | lld:pubmed |
pubmed-article:20943949 | pubmed:dateCreated | 2010-12-16 | lld:pubmed |
pubmed-article:20943949 | pubmed:abstractText | The Na(+),K(+)-ATPase is the major active transport protein found in the plasma membranes of most epithelial cell types. The regulation of Na(+),K(+)-ATPase activity involves a variety of mechanisms, including regulated endocytosis and recycling. Our efforts to identify novel Na(+),K(+)-ATPase binding partners revealed a direct association between the Na(+),K(+)-ATPase and AS160, a Rab-GTPase-activating protein. In COS cells, coexpression of AS160 and Na(+),K(+)-ATPase led to the intracellular retention of the sodium pump. We find that AS160 interacts with the large cytoplasmic NP domain of the ?-subunit of the Na(+),K(+)-ATPase. Inhibition of the activity of the adenosine monophosphate-stimulated protein kinase (AMPK) in Madin-Darby canine kidney cells through treatment with Compound C induces Na(+),K(+)-ATPase endocytosis. This effect of Compound C is prevented through the short hairpin RNA-mediated knockdown of AS160, demonstrating that AMPK and AS160 participate in a common pathway to modulate the cell surface expression of the Na(+),K(+)-ATPase. | lld:pubmed |
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pubmed-article:20943949 | pubmed:language | eng | lld:pubmed |
pubmed-article:20943949 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:20943949 | pubmed:citationSubset | IM | lld:pubmed |
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pubmed-article:20943949 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:20943949 | pubmed:month | Dec | lld:pubmed |
pubmed-article:20943949 | pubmed:issn | 1939-4586 | lld:pubmed |
pubmed-article:20943949 | pubmed:author | pubmed-author:CaplanMichael... | lld:pubmed |
pubmed-article:20943949 | pubmed:author | pubmed-author:FarrGlen AGA | lld:pubmed |
pubmed-article:20943949 | pubmed:author | pubmed-author:AlvesDaiane... | lld:pubmed |
pubmed-article:20943949 | pubmed:author | pubmed-author:Seo-MayerPatr... | lld:pubmed |
pubmed-article:20943949 | pubmed:issnType | Electronic | lld:pubmed |
pubmed-article:20943949 | pubmed:volume | 21 | lld:pubmed |
pubmed-article:20943949 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:20943949 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:20943949 | pubmed:pagination | 4400-8 | lld:pubmed |
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