pubmed-article:9614172 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:9614172 | lifeskim:mentions | umls-concept:C0036025 | lld:lifeskim |
pubmed-article:9614172 | lifeskim:mentions | umls-concept:C0031165 | lld:lifeskim |
pubmed-article:9614172 | lifeskim:mentions | umls-concept:C1519751 | lld:lifeskim |
pubmed-article:9614172 | pubmed:issue | 6 | lld:pubmed |
pubmed-article:9614172 | pubmed:dateCreated | 1998-7-10 | lld:pubmed |
pubmed-article:9614172 | pubmed:abstractText | Addition of ammonium ions to yeast cells growing on proline as the sole nitrogen source induces rapid inactivation and degradation of the general amino acid permease Gap1 through a process requiring the Npi1/Rsp5 ubiquitin (Ub) ligase. In this study, we show that NH4+ induces endocytosis of Gap1, which is then delivered into the vacuole where it is degraded. This down-regulation is accompanied by increased conversion of Gap1 to ubiquitinated forms. Ubiquitination and subsequent degradation of Gap1 are impaired in the npi1 strain. In this mutant, the amount of Npi1/Rsp5 Ub ligase is reduced >10-fold compared with wild-type cells. The C-terminal tail of Gap1 contains sequences, including a di-leucine motif, which are required for NH4+-induced internalization and degradation of the permease. We show here that mutant Gap1 permeases affected in these sequences still bind Ub. Furthermore, we provide evidence that only a small fraction of Gap1 is modified by Ub after addition of NH4+ to mutants defective in endocytosis. | lld:pubmed |
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pubmed-article:9614172 | pubmed:language | eng | lld:pubmed |
pubmed-article:9614172 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:9614172 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:9614172 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:9614172 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:9614172 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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pubmed-article:9614172 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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pubmed-article:9614172 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:9614172 | pubmed:month | Jun | lld:pubmed |
pubmed-article:9614172 | pubmed:issn | 1059-1524 | lld:pubmed |
pubmed-article:9614172 | pubmed:author | pubmed-author:AndréBB | lld:pubmed |
pubmed-article:9614172 | pubmed:author | pubmed-author:SpringaelJ... | lld:pubmed |
pubmed-article:9614172 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:9614172 | pubmed:volume | 9 | lld:pubmed |
pubmed-article:9614172 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:9614172 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:9614172 | pubmed:pagination | 1253-63 | lld:pubmed |
pubmed-article:9614172 | pubmed:dateRevised | 2009-11-19 | lld:pubmed |
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