http://www.cnr.it/ontology/cnr/individuo/prodotto/ID10395
HD-PTP inhibits endothelial migration through its interaction with Src. (Articolo in rivista)
- Type
- Label
- HD-PTP inhibits endothelial migration through its interaction with Src. (Articolo in rivista) (literal)
- Anno
- 2009-01-01T00:00:00+01:00 (literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi
- 10.1016/j.bioce1.2008.08.005 (literal)
- Alternative label
Mariotti M. 1, Castiglioni S. 1, Garcia-Manteiga J.M. 2, Beguinot L. 2,3, Maier J.A. 1 (2009)
HD-PTP inhibits endothelial migration through its interaction with Src.
in International journal of biochemistry & cell biology
(literal)
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- Mariotti M. 1, Castiglioni S. 1, Garcia-Manteiga J.M. 2, Beguinot L. 2,3, Maier J.A. 1 (literal)
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- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#note
- Pubblicato on-line: 9 Agosto 2008
Corresponding author: J. Maier (jeanette.maier@unimi.it)
IF 2009: 4.887 (literal)
- Note
- ISI Web of Science (WOS) (literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni
- 1. Department of Preclinical Sciences, University of Milan Medical School, Milano
b. Laboratory of Molecular Oncology, DIBIT, San Raffaele Scientific Institute, Milano
3. CNR Institute of Bioimaging and Molecular Physiology, LITA, Segrate (MI) (literal)
- Titolo
- HD-PTP inhibits endothelial migration through its interaction with Src. (literal)
- Abstract
- Endothelial migration, early step in angiogenesis, is tightly regulated by the coordinated action of tyrosine kinases and tyrosine phosphatases. HD-PTP contributes to endothelial motility, since endothelial cells silencing HD-PTP after transfection with iRNA acquire a scattered and spindle-shaped phenotype and migrate faster than controls. Since (i) the proto-oncogene Src contributes to the regulation of cell motility and (ii) HD-PTP has a potential binding site for Src, we investigated whether an interplay exists between these two proteins. We found that Src binds HD-PTP and this interaction is enhanced after exposure to basic fibroblast growth factor. While HD-PTP does not modulate the levels of Src phosphorylation both in vitro and in vivo, we found that Src phosphorylates HD-PTP on tyrosine residues. Here we show for the first time that (i) HD-PTP has a tyrosine phosphatase activity; (ii) HD-PTP phosphorylation by Src inhibits its enzymatic activity. Interestingly, pharmacological and genetic inhibition of Src abrogates the migratory phenotype of endothelial cells silencing HD-PTP. On these bases, and because we have previously demonstrated that HD-PTP binds and dephosphorylates focal adhesion kinase (FAK), another crucial regulator of cell migration, we hypothesize that HD-PTP participates to the regulation of endothelial motility through its interactions with Src and FAK. (literal)
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