| pubmed-article:11950838 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:11950838 | lifeskim:mentions | umls-concept:C0043393 | lld:lifeskim |
| pubmed-article:11950838 | lifeskim:mentions | umls-concept:C0014239 | lld:lifeskim |
| pubmed-article:11950838 | lifeskim:mentions | umls-concept:C0001473 | lld:lifeskim |
| pubmed-article:11950838 | lifeskim:mentions | umls-concept:C1157399 | lld:lifeskim |
| pubmed-article:11950838 | lifeskim:mentions | umls-concept:C1546857 | lld:lifeskim |
| pubmed-article:11950838 | lifeskim:mentions | umls-concept:C1522492 | lld:lifeskim |
| pubmed-article:11950838 | lifeskim:mentions | umls-concept:C1556066 | lld:lifeskim |
| pubmed-article:11950838 | lifeskim:mentions | umls-concept:C1619636 | lld:lifeskim |
| pubmed-article:11950838 | lifeskim:mentions | umls-concept:C1514873 | lld:lifeskim |
| pubmed-article:11950838 | pubmed:issue | 25 | lld:pubmed |
| pubmed-article:11950838 | pubmed:dateCreated | 2002-6-17 | lld:pubmed |
| pubmed-article:11950838 | pubmed:abstractText | The yeast plasma membrane H(+)-ATPase Pma1p is one of the most abundant proteins to traverse the secretory pathway. Newly synthesized Pma1p exits the endoplasmic reticulum (ER) via COPII-coated vesicles bound for the Golgi. Unlike most secreted proteins, efficient incorporation of Pma1p into COPII vesicles requires the Sec24p homolog Lst1p, suggesting a unique role for Lst1p in ER export. Vesicles formed with mixed Sec24p-Lst1p coats are larger than those with Sec24p alone. Here, we examined the relationship between Pma1p biosynthesis and the requirement for this novel coat subunit. We show that Pma1p forms a large oligomeric complex of >1 MDa in the ER, which is packaged into COPII vesicles. Furthermore, oligomerization of Pma1p is linked to membrane lipid composition; Pma1p is rendered monomeric in cells depleted of ceramide, suggesting that association with lipid rafts may influence oligomerization. Surprisingly, monomeric Pma1p present in ceramide-deficient membranes can be exported from the ER in COPII vesicles in a reaction that is stimulated by Lst1p. We suggest that Lst1p directly conveys Pma1p into a COPII vesicle and that the larger size of mixed Sec24pLst1p COPII vesicles is not essential to the packaging of large oligomeric complexes. | lld:pubmed |
| pubmed-article:11950838 | pubmed:language | eng | lld:pubmed |
| pubmed-article:11950838 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11950838 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:11950838 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11950838 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:11950838 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11950838 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:11950838 | pubmed:month | Jun | lld:pubmed |
| pubmed-article:11950838 | pubmed:issn | 0021-9258 | lld:pubmed |
| pubmed-article:11950838 | pubmed:author | pubmed-author:SchekmanRandy... | lld:pubmed |
| pubmed-article:11950838 | pubmed:author | pubmed-author:LeeMarcus C... | lld:pubmed |
| pubmed-article:11950838 | pubmed:author | pubmed-author:HamamotoSusan... | lld:pubmed |
| pubmed-article:11950838 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:11950838 | pubmed:day | 21 | lld:pubmed |
| pubmed-article:11950838 | pubmed:volume | 277 | lld:pubmed |
| pubmed-article:11950838 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:11950838 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:11950838 | pubmed:pagination | 22395-401 | lld:pubmed |
| pubmed-article:11950838 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
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| pubmed-article:11950838 | pubmed:meshHeading | pubmed-meshheading:11950838... | lld:pubmed |
| pubmed-article:11950838 | pubmed:year | 2002 | lld:pubmed |
| pubmed-article:11950838 | pubmed:articleTitle | Ceramide biosynthesis is required for the formation of the oligomeric H+-ATPase Pma1p in the yeast endoplasmic reticulum. | lld:pubmed |
| pubmed-article:11950838 | pubmed:affiliation | Department of Molecular and Cell Biology, Howard Hughes Medical Institute, University of California, Berkeley, California 94720, USA. | lld:pubmed |
| pubmed-article:11950838 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:11950838 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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