Linked Life Data

11724808

Source:http://linkedlifedata.com/resource/pubmed/id/11724808

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
5
pubmed:dateCreated
2002-1-28
pubmed:abstractText
Caveolae are flask-shaped invaginations at the plasma membrane that constitute a subclass of detergent-resistant membrane domains enriched in cholesterol and sphingolipids and that express caveolin, a caveolar coat protein. Autocrine motility factor receptor (AMF-R) is stably localized to caveolae, and the cholesterol extracting reagent, methyl-beta-cyclodextrin, inhibits its internalization to the endoplasmic reticulum implicating caveolae in this distinct receptor-mediated endocytic pathway. Curiously, the rate of methyl-beta-cyclodextrin-sensitive endocytosis of AMF-R to the endoplasmic reticulum is increased in ras- and abl-transformed NIH-3T3 cells that express significantly reduced levels of caveolin and few caveolae. Overexpression of the dynamin K44A dominant negative mutant via an adenovirus expression system induces caveolar invaginations sensitive to methyl-beta-cyclodextrin extraction in the transformed cells without increasing caveolin expression. Dynamin K44A expression further inhibits AMF-R-mediated endocytosis to the endoplasmic reticulum in untransformed and transformed NIH-3T3 cells. Adenoviral expression of caveolin-1 also induces caveolae in the transformed NIH-3T3 cells and reduces AMF-R-mediated endocytosis to the endoplasmic reticulum to levels observed in untransformed NIH-3T3 cells. Cholesterol-rich detergent-resistant membrane domains or glycolipid rafts therefore invaginate independently of caveolin-1 expression to form endocytosis-competent caveolar vesicles via rapid dynamin-dependent detachment from the plasma membrane. Caveolin-1 stabilizes the plasma membrane association of caveolae and thereby acts as a negative regulator of the caveolae-mediated endocytosis of AMF-R to the endoplasmic reticulum.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Feb
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
1
pubmed:volume
277
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
3371-9
pubmed:dateRevised
2011-11-17
pubmed:meshHeading
pubmed-meshheading:11724808-3T3 Cells, pubmed-meshheading:11724808-Amino Acid Substitution, pubmed-meshheading:11724808-Animals, pubmed-meshheading:11724808-Caveolae, pubmed-meshheading:11724808-Caveolin 1, pubmed-meshheading:11724808-Caveolins, pubmed-meshheading:11724808-Cell Transformation, Neoplastic, pubmed-meshheading:11724808-Dynamins, pubmed-meshheading:11724808-Endocytosis, pubmed-meshheading:11724808-Endoplasmic Reticulum, pubmed-meshheading:11724808-GTP Phosphohydrolases, pubmed-meshheading:11724808-Genes, abl, pubmed-meshheading:11724808-Genes, ras, pubmed-meshheading:11724808-Homeostasis, pubmed-meshheading:11724808-Kinetics, pubmed-meshheading:11724808-Mice, pubmed-meshheading:11724808-Mutagenesis, Site-Directed, pubmed-meshheading:11724808-Receptors, Autocrine Motility Factor, pubmed-meshheading:11724808-Receptors, Cytokine, pubmed-meshheading:11724808-Recombinant Proteins, pubmed-meshheading:11724808-Ubiquitin-Protein Ligases
pubmed:year
2002
pubmed:articleTitle
Caveolin-1 is a negative regulator of caveolae-mediated endocytosis to the endoplasmic reticulum.
pubmed:affiliation
Department of Pathology and Cell Biology, Université de Montréal, Montreal, Quebec H3C 3J7, Canada.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't