Linked Life Data

10598578

Source:http://linkedlifedata.com/resource/pubmed/id/10598578

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
12
pubmed:dateCreated
2000-1-10
pubmed:abstractText
Caveolae may function as microdomains for signaling that help to determine specific biological actions mediated by the insulin receptor (IR). Caveolin-1, a major component of caveolae, contains a scaffolding domain (SD) that binds to a caveolin-1 binding motif in the kinase domain of the IR in vitro. To investigate the potential role of caveolin-1 in insulin signaling we overexpressed wild-type (Cav-WT) or mutant (Cav-Mut; F92A/V94A in SD) caveolin-1 in either Cos-7 cells cotransfected with IR or rat adipose cells (low and high levels of endogenous caveolin-1, respectively). Cav-WT coimmunoprecipitated with the IR to a much greater extent than Cav-Mut, suggesting that the SD is important for interactions between caveolin-1 and the IR in intact cells. We also constructed several IR mutants with a disrupted caveolin-1 binding motif and found that these mutants were poorly expressed and did not undergo autophosphorylation. Interestingly, overexpression of Cav-WT in Cos-7 cells significantly enhanced insulin-stimulated phosphorylation of Elk-1 (a mitogen-activated protein kinase-dependent pathway) while overexpression of Cav-Mut was without effect. In contrast, in adipose cells, overexpression of either Cav-WT or Cav-Mut did not affect insulin-stimulated phosphorylation of a cotransfected ERK2 (but did significantly inhibit basal phosphorylation of ERK2). Furthermore, we also observed a small inhibition of insulin-stimulated translocation of GLUT4 when either Cav-WT or Cav-Mut was overexpressed in adipose cells. Thus, interaction of caveolin-1 with IRs may differentially modulate insulin signaling to enhance insulin action in Cos-7 cells but inhibit insulin's effects in adipose cells.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Dec
pubmed:issn
0888-8809
pubmed:author
pubmed:issnType
Print
pubmed:volume
13
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
2013-24
pubmed:dateRevised
2011-11-17
pubmed:meshHeading
pubmed-meshheading:10598578-Adipocytes, pubmed-meshheading:10598578-Animals, pubmed-meshheading:10598578-COS Cells, pubmed-meshheading:10598578-Caveolin 1, pubmed-meshheading:10598578-Caveolins, pubmed-meshheading:10598578-Gene Expression, pubmed-meshheading:10598578-Glucose Transporter Type 4, pubmed-meshheading:10598578-Immunosorbent Techniques, pubmed-meshheading:10598578-Insulin, pubmed-meshheading:10598578-Male, pubmed-meshheading:10598578-Membrane Proteins, pubmed-meshheading:10598578-Monosaccharide Transport Proteins, pubmed-meshheading:10598578-Muscle Proteins, pubmed-meshheading:10598578-Mutagenesis, Site-Directed, pubmed-meshheading:10598578-Phosphorylation, pubmed-meshheading:10598578-Rats, pubmed-meshheading:10598578-Receptor, Insulin, pubmed-meshheading:10598578-Recombinant Proteins, pubmed-meshheading:10598578-Signal Transduction, pubmed-meshheading:10598578-Transfection
pubmed:year
1999
pubmed:articleTitle
Caveolin-1 interacts with the insulin receptor and can differentially modulate insulin signaling in transfected Cos-7 cells and rat adipose cells.
pubmed:affiliation
Hypertension-Endocrine Branch, National Heart, Lung, and Blood Institute, National Institutes of Health, Bethesda, Maryland 20892, USA.
pubmed:publicationType
Journal Article