Linked Life Data

15466865

Source:http://linkedlifedata.com/resource/pubmed/id/15466865

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
50
pubmed:dateCreated
2004-12-6
pubmed:abstractText
We have recently shown that stimulation of endothelial cells with vascular endothelial growth factor (VEGF) induces dissociation of caveolin-1 from the VEGFR-2 receptor, followed by Src family kinase-dependent tyrosine phosphorylation of the protein (Labrecque, L., Royal, I., Surprenant, D. S., Patterson, C., Gingras, D., and Beliveau, R. (2003) Mol. Biol. Cell 14, 334-347). In this study, we provide evidence that the VEGF-dependent tyrosine phosphorylation of caveolin-1 induces interaction of the protein with the membrane-type 1 matrix metalloproteinase (MT1-MMP). This interaction requires the phosphorylation of caveolin-1 on tyrosine 14 by members of the Src family of protein kinases, such as Src and Fyn, because it is completely abolished by expression of a catalytically inactive Src mutant or by site-directed mutagenesis of tyrosine 14 of caveolin-1. Most interestingly, the association of MT1-MMP with phosphorylated caveolin-1 induced the recruitment of Src and a concomitant inhibition of the kinase activity of the enzyme, suggesting that this complex may be involved in the negative regulation of Src activity. The association of MT1-MMP with phosphorylated caveolin-1 occurs in caveolae membranes and involves the cytoplasmic domain of MT1-MMP because it was markedly reduced by mutation of Cys574 and Val582 residues of the cytoplasmic tail of the enzyme. Most interestingly, the reduction of the interaction between MT1-MMP and caveolin-1 by using these mutants also decreases MT1-MMP-dependent cell locomotion. Overall these results indicate that MT1-MMP associates with tyrosine-phosphorylated caveolin-1 and that this complex may play an important role in MT1-MMP regulation and function.
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
10
pubmed:volume
279
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
52132-40
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed-meshheading:15466865-Amino Acid Sequence, pubmed-meshheading:15466865-Animals, pubmed-meshheading:15466865-COS Cells, pubmed-meshheading:15466865-Cattle, pubmed-meshheading:15466865-Caveolae, pubmed-meshheading:15466865-Caveolin 1, pubmed-meshheading:15466865-Caveolins, pubmed-meshheading:15466865-Cells, Cultured, pubmed-meshheading:15466865-Endothelium, Vascular, pubmed-meshheading:15466865-Humans, pubmed-meshheading:15466865-Matrix Metalloproteinases, Membrane-Associated, pubmed-meshheading:15466865-Metalloendopeptidases, pubmed-meshheading:15466865-Molecular Sequence Data, pubmed-meshheading:15466865-Mutagenesis, Site-Directed, pubmed-meshheading:15466865-Phosphorylation, pubmed-meshheading:15466865-Recombinant Proteins, pubmed-meshheading:15466865-Tyrosine, pubmed-meshheading:15466865-Vascular Endothelial Growth Factor A, pubmed-meshheading:15466865-src-Family Kinases
pubmed:year
2004
pubmed:articleTitle
Src-mediated tyrosine phosphorylation of caveolin-1 induces its association with membrane type 1 matrix metalloproteinase.
pubmed:affiliation
Laboratoire de Médecine Moléculaire, Hôpital Ste-Justine-Université du Québec à Montréal, Centre de Cancérologie Charles-Bruneau, 3175 Chemin Côte-Ste-Catherine, Montréal, Québec H3T 1C5.
pubmed:publicationType
Journal Article, In Vitro, Research Support, Non-U.S. Gov't