Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
2004-9-22
pubmed:abstractText
In this paper, a molecular and functional interaction between metabotropic glutamate receptor type 1alpha (mGlu1alpha receptor) and caveolin-1 or caveolin-2beta is described. An overlapping pattern of staining for mGlu1alpha receptor with caveolin-1 and caveolin-2 by confocal laser microscopy in transiently transfected HEK-293 cells is observed. The presence of mGlu1alpha receptor in caveolin-enriched membrane fractions was demonstrated by flotation gradient analysis in the absence of detergents and the interaction between mGlu1alpha receptor with caveolin-1 and with caveolin-2beta was demonstrated by coimmunoprecipitation experiments. In HEK-293 cells, caveolin-2beta accumulates surrounding lipid droplets when single expressed but coexpression with mGlu1alpha receptor changed dramatically the subcellular localization of caveolin-2beta, directing it from lipid droplets to the cell surface. At the membrane level, the interaction between caveolin-1 and mGlu1alpha receptor could abrogate the constitutive activity exhibited by mGlu1alpha receptor. Overall, these results show that mGlu1alpha receptor interacts with caveolins and that this interaction is physiologically relevant for receptor function. Interestingly, we provide evidence that caveolin-1 is not just acting as a scaffolding protein for the mGlu1alpha receptor but that also regulates mGlu1alpha receptor constitutive activity.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Oct
pubmed:issn
0014-4827
pubmed:author
pubmed:issnType
Print
pubmed:day
15
pubmed:volume
300
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
23-34
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed:year
2004
pubmed:articleTitle
Mutual regulation between metabotropic glutamate type 1alpha receptor and caveolin proteins: from traffick to constitutive activity.
pubmed:affiliation
Department of Biochemistry and Molecular Biology. University of Barcelona. Barcelona, Spain.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't