pubmed-article:12393888 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:12393888 | lifeskim:mentions | umls-concept:C0043393 | lld:lifeskim |
pubmed-article:12393888 | lifeskim:mentions | umls-concept:C0596901 | lld:lifeskim |
pubmed-article:12393888 | lifeskim:mentions | umls-concept:C0033684 | lld:lifeskim |
pubmed-article:12393888 | lifeskim:mentions | umls-concept:C0037900 | lld:lifeskim |
pubmed-article:12393888 | lifeskim:mentions | umls-concept:C0004083 | lld:lifeskim |
pubmed-article:12393888 | lifeskim:mentions | umls-concept:C0205360 | lld:lifeskim |
pubmed-article:12393888 | lifeskim:mentions | umls-concept:C1546857 | lld:lifeskim |
pubmed-article:12393888 | lifeskim:mentions | umls-concept:C1556066 | lld:lifeskim |
pubmed-article:12393888 | lifeskim:mentions | umls-concept:C1619636 | lld:lifeskim |
pubmed-article:12393888 | lifeskim:mentions | umls-concept:C1514873 | lld:lifeskim |
pubmed-article:12393888 | pubmed:issue | 51 | lld:pubmed |
pubmed-article:12393888 | pubmed:dateCreated | 2002-12-16 | lld:pubmed |
pubmed-article:12393888 | pubmed:abstractText | Ongoing sphingolipid synthesis is specifically required in vivo for the endoplasmic reticulum (ER) to Golgi transport of glycosylphosphatidylinositol (GPI)-anchored proteins. However, the sphingolipid intermediates that are required for transport nor their role(s) have been identified. Using stereoisomers of dihydrosphingosine, together with specific inhibitors and a mutant defective for sphingolipid synthesis, we now show that ceramides and/or inositol sphingolipids are indispensable for GPI-anchored protein transport. Furthermore, in the absence of sphingolipid synthesis, a significant fraction of GPI-anchored proteins is no longer associated tightly with the ER membrane. The loose membrane association is neither because of the lack of a GPI-anchor nor because of prolonged ER retention of GPI-anchored proteins. These results indicate that ceramides and/or inositol sphingolipids are required to stabilize the association of GPI-anchored proteins with membranes. They could act either by direct involvement as membrane components or as substrates for the remodeling of GPI lipid moieties. | lld:pubmed |
pubmed-article:12393888 | pubmed:language | eng | lld:pubmed |
pubmed-article:12393888 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:12393888 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:12393888 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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pubmed-article:12393888 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:12393888 | pubmed:month | Dec | lld:pubmed |
pubmed-article:12393888 | pubmed:issn | 0021-9258 | lld:pubmed |
pubmed-article:12393888 | pubmed:author | pubmed-author:FutermanAntho... | lld:pubmed |
pubmed-article:12393888 | pubmed:author | pubmed-author:VenkataramanK... | lld:pubmed |
pubmed-article:12393888 | pubmed:author | pubmed-author:RiezmanHoward... | lld:pubmed |
pubmed-article:12393888 | pubmed:author | pubmed-author:FunatoKouichi... | lld:pubmed |
pubmed-article:12393888 | pubmed:author | pubmed-author:WatanabeReika... | lld:pubmed |
pubmed-article:12393888 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:12393888 | pubmed:day | 20 | lld:pubmed |
pubmed-article:12393888 | pubmed:volume | 277 | lld:pubmed |
pubmed-article:12393888 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:12393888 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:12393888 | pubmed:pagination | 49538-44 | lld:pubmed |
pubmed-article:12393888 | pubmed:dateRevised | 2010-11-18 | lld:pubmed |
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pubmed-article:12393888 | pubmed:year | 2002 | lld:pubmed |
pubmed-article:12393888 | pubmed:articleTitle | Sphingolipids are required for the stable membrane association of glycosylphosphatidylinositol-anchored proteins in yeast. | lld:pubmed |
pubmed-article:12393888 | pubmed:affiliation | Biozentrum of the University of Basel, Klingelbergstrasse 70, Basel 4056, Switzerland. | lld:pubmed |
pubmed-article:12393888 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:12393888 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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