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Sphingosine‐1‐phosphate induces the association of membrane‐type 1 matrix metalloproteinase with p130Cas in endothelial cells
Author(s) -
Gingras Denis,
Michaud Marisol,
Di Tomasso Geneviève,
Béliveau Eric,
Nyalendo Carine,
Béliveau Richard
Publication year - 2008
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2007.12.029
Subject(s) - microbiology and biotechnology , phosphorylation , sphingosine 1 phosphate , signal transducing adaptor protein , matrix metalloproteinase , sphingosine , actin , immunoprecipitation , chemistry , tyrosine phosphorylation , cytoplasm , biology , biochemistry , receptor , gene
Membrane‐type 1 matrix metalloproteinase (MT1‐MMP) plays an important role in sphingosine‐1‐phosphate(S1P)‐dependent migration of endothelial cells but the underlying mechanisms remain largely unknown. Herein, we show that S1P promotes the relocalization of MT1‐MMP to peripheral actin‐rich membrane ruffles that is coincident with its association with the adaptor protein p130Cas at the leading edge of migrating cells. Immunoprecipitation and confocal microscopy analyses suggest that this interaction required the tyrosine phosphorylation of p130Cas and also involves S1P‐dependent phosphorylation of MT1‐MMP within its cytoplasmic sequence. The interaction of MT1‐MMP with p130Cas at the cell periphery suggests the existence of a close interplay between pericellular proteolysis and signaling pathways involved in EC migration.