Linked Life Data

14992406

Source:http://linkedlifedata.com/resource/pubmed/id/14992406

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:dateCreated
2004-3-2
pubmed:abstractText
Caveolae are small, flask shaped invaginations in the cell membrane. They are thought to play a crucial role in cell signaling, endocytosis and intracellular cholesterol transport. Caveolin-1, 2 and 3 are key proteins, which are important for the formation of the invaginations on the cell surface. Caveolin-1 exists in two isoforms: caveolin-1 alpha (a) and caveolin-1 beta (beta). Little is known about the difference between these two isoforms, and less in known about their role in cell signaling. Bone morphogenetic proteins IBMPs) are a subfamily of the TGF beta superfamily and their response is mediated by serine/threonine kinase receptors. Epidermal growth factor (EGF) is known to signal through tyrosine kinase receptors of the ErbB family. Here we report on the aggregation and association of caveolin-1 isoforms with these receptors and the effect of BMP and EGF activation on caveolin-1 distribution in A431 cells. Our data, obtained by application of a family of image correlation spectroscopy tools, indicate that BMP and EGF stimulation lead to a rearrangement of the caveolin-1 isoforms on the cell surface. BMP as well as EGF stimulation leads to a rearrangement of the caveolin-1 P isoform into domains enriched in the caveolin-1 alpha isoform. We further show that about 20-30% of the caveolin-1 present at the surface of the cells co-localize with the EGF and BMP receptors. Using a reporter gene assay sensitive to the activation of the BMP pathway, we show that overexpression of caveolin-1beta inhibits signaling. Our data suggest that the two isoforms of caveolin-1 play different roles on the cell surface and that caveolae are dynamic structures.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
1359-6640
pubmed:author
pubmed:issnType
Print
pubmed:volume
126
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
185-95; discussion 245-54
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed:year
2004
pubmed:articleTitle
Caveolin-1 isoform reorganization studied by image correlation spectroscopy.
pubmed:affiliation
Department of Chemistry, University of Western Ontario, London, Canada.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't