Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
51
pubmed:dateCreated
2002-12-16
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.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Dec
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
20
pubmed:volume
277
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
49538-44
pubmed:dateRevised
2010-11-18
pubmed:meshHeading
pubmed-meshheading:12393888-Cell Cycle Proteins, pubmed-meshheading:12393888-Cell Membrane, pubmed-meshheading:12393888-Ceramides, pubmed-meshheading:12393888-Endoplasmic Reticulum, pubmed-meshheading:12393888-GPI-Linked Proteins, pubmed-meshheading:12393888-Glycosylphosphatidylinositols, pubmed-meshheading:12393888-Golgi Apparatus, pubmed-meshheading:12393888-Lipid Metabolism, pubmed-meshheading:12393888-Membrane Proteins, pubmed-meshheading:12393888-Mutation, pubmed-meshheading:12393888-Plasmids, pubmed-meshheading:12393888-Protein Binding, pubmed-meshheading:12393888-Protein Structure, Tertiary, pubmed-meshheading:12393888-Protein Transport, pubmed-meshheading:12393888-Sphingolipids, pubmed-meshheading:12393888-Stereoisomerism, pubmed-meshheading:12393888-Substrate Specificity, pubmed-meshheading:12393888-Yeasts
pubmed:year
2002
pubmed:articleTitle
Sphingolipids are required for the stable membrane association of glycosylphosphatidylinositol-anchored proteins in yeast.
pubmed:affiliation
Biozentrum of the University of Basel, Klingelbergstrasse 70, Basel 4056, Switzerland.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't