| pubmed-article:10758001 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:10758001 | lifeskim:mentions | umls-concept:C0036024 | lld:lifeskim |
| pubmed-article:10758001 | lifeskim:mentions | umls-concept:C0005528 | lld:lifeskim |
| pubmed-article:10758001 | lifeskim:mentions | umls-concept:C1511625 | lld:lifeskim |
| pubmed-article:10758001 | lifeskim:mentions | umls-concept:C0441655 | lld:lifeskim |
| pubmed-article:10758001 | lifeskim:mentions | umls-concept:C0597304 | lld:lifeskim |
| pubmed-article:10758001 | lifeskim:mentions | umls-concept:C1519249 | lld:lifeskim |
| pubmed-article:10758001 | lifeskim:mentions | umls-concept:C0065608 | lld:lifeskim |
| pubmed-article:10758001 | lifeskim:mentions | umls-concept:C1546857 | lld:lifeskim |
| pubmed-article:10758001 | lifeskim:mentions | umls-concept:C0439831 | lld:lifeskim |
| pubmed-article:10758001 | lifeskim:mentions | umls-concept:C1556066 | lld:lifeskim |
| pubmed-article:10758001 | lifeskim:mentions | umls-concept:C1619636 | lld:lifeskim |
| pubmed-article:10758001 | lifeskim:mentions | umls-concept:C1514873 | lld:lifeskim |
| pubmed-article:10758001 | pubmed:issue | 15 | lld:pubmed |
| pubmed-article:10758001 | pubmed:dateCreated | 2000-6-16 | lld:pubmed |
| pubmed-article:10758001 | pubmed:abstractText | Maltose permease is required for maltose transport into Saccharomyces cells. Glucose addition to maltose-fermenting cells causes selective delivery of this integral plasma membrane protein to the yeast vacuole via endocytosis for degradation by resident proteases. This glucose-induced degradation is independent of the proteasome but requires ubiquitin and certain ubiquitin conjugating enzymes. We used mutation analysis to identify target sequences in Mal61/HA maltose permease involved in its selective glucose-induced degradation. A nonsense mutation was introduced at codon 581, creating a truncated functional maltose permease. Additional missense mutations were introduced into the mal61/HA-581NS allele, altering potential phosphorylation and ubiquitination sites. No significant effect was seen on the rate of glucose-induced degradation of these mutant proteins. Deletion mutations were constructed, removing residues 2-30, 31-60, 61-90, and 49-78 of the N-terminal cytoplasmic domain, as well as a missense mutation of a dileucine motif. Results indicate that the proline-, glutamate-, aspartate-, serine-, and threonine-rich (PEST) sequence found in the N-terminal cytoplasmic domain, particularly residues 49-78, is required for glucose-induced degradation of Mal61/HAp and for the rapid glucose-induced inactivation of maltose transport activity. The decreased rate of glucose-induced degradation correlates with a decrease in the level of glucose-induced ubiquitination of the DeltaPEST mutant permease. In addition, newly synthesized mutant permease proteins lacking residues 49-78 or carrying an alteration in the dileucine motif, residues 69 and 70, are resistant to glucose-induced inactivation of maltose transport activity. This N-terminal PEST-like sequence is the target of both the Rgt2p-dependent and the Glc7p-Reg1p-dependent glucose signaling pathways. | lld:pubmed |
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| pubmed-article:10758001 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10758001 | pubmed:language | eng | lld:pubmed |
| pubmed-article:10758001 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10758001 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:10758001 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:10758001 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:10758001 | pubmed:month | Apr | lld:pubmed |
| pubmed-article:10758001 | pubmed:issn | 0006-2960 | lld:pubmed |
| pubmed-article:10758001 | pubmed:author | pubmed-author:MichelsC ACA | lld:pubmed |
| pubmed-article:10758001 | pubmed:author | pubmed-author:WangXX | lld:pubmed |
| pubmed-article:10758001 | pubmed:author | pubmed-author:MedintzII | lld:pubmed |
| pubmed-article:10758001 | pubmed:author | pubmed-author:HradekTT | lld:pubmed |
| pubmed-article:10758001 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:10758001 | pubmed:day | 18 | lld:pubmed |
| pubmed-article:10758001 | pubmed:volume | 39 | lld:pubmed |
| pubmed-article:10758001 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:10758001 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:10758001 | pubmed:pagination | 4518-26 | lld:pubmed |
| pubmed-article:10758001 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
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| pubmed-article:10758001 | pubmed:year | 2000 | lld:pubmed |
| pubmed-article:10758001 | pubmed:articleTitle | A PEST-like sequence in the N-terminal cytoplasmic domain of Saccharomyces maltose permease is required for glucose-induced proteolysis and rapid inactivation of transport activity. | lld:pubmed |
| pubmed-article:10758001 | pubmed:affiliation | Biology Department, Queens College and the Graduate School of the City University of New York, 65-30 Kissena Boulevard, Flushing, New York 11367, USA. | lld:pubmed |
| pubmed-article:10758001 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:10758001 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:10758001 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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