Source:http://linkedlifedata.com/resource/pubmed/id/11950838
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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
25
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| pubmed:dateCreated |
2002-6-17
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| 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.
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| pubmed:language |
eng
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| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Ceramides,
http://linkedlifedata.com/resource/pubmed/chemical/Detergents,
http://linkedlifedata.com/resource/pubmed/chemical/PMA1 protein, S cerevisiae,
http://linkedlifedata.com/resource/pubmed/chemical/Proton-Translocating ATPases,
http://linkedlifedata.com/resource/pubmed/chemical/Saccharomyces cerevisiae Proteins
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| pubmed:status |
MEDLINE
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| pubmed:month |
Jun
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| pubmed:issn |
0021-9258
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| pubmed:author | |
| pubmed:issnType |
Print
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| pubmed:day |
21
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| pubmed:volume |
277
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| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
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| pubmed:pagination |
22395-401
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| pubmed:dateRevised |
2006-11-15
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| pubmed:meshHeading |
pubmed-meshheading:11950838-COP-Coated Vesicles,
pubmed-meshheading:11950838-Cell Membrane,
pubmed-meshheading:11950838-Ceramides,
pubmed-meshheading:11950838-Detergents,
pubmed-meshheading:11950838-Dose-Response Relationship, Drug,
pubmed-meshheading:11950838-Endoplasmic Reticulum,
pubmed-meshheading:11950838-Golgi Apparatus,
pubmed-meshheading:11950838-Kinetics,
pubmed-meshheading:11950838-Lipid Metabolism,
pubmed-meshheading:11950838-Microscopy, Electron,
pubmed-meshheading:11950838-Microsomes,
pubmed-meshheading:11950838-Plasmids,
pubmed-meshheading:11950838-Protein Binding,
pubmed-meshheading:11950838-Protein Transport,
pubmed-meshheading:11950838-Proton-Translocating ATPases,
pubmed-meshheading:11950838-Saccharomyces cerevisiae Proteins,
pubmed-meshheading:11950838-Temperature,
pubmed-meshheading:11950838-Time Factors,
pubmed-meshheading:11950838-Yeasts
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| pubmed:year |
2002
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| pubmed:articleTitle |
Ceramide biosynthesis is required for the formation of the oligomeric H+-ATPase Pma1p in the yeast endoplasmic reticulum.
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| pubmed:affiliation |
Department of Molecular and Cell Biology, Howard Hughes Medical Institute, University of California, Berkeley, California 94720, USA.
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| pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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