Title : PDGF and FGF induce focal adhesion kinase (FAK) phosphorylation at Ser-910: dissociation from Tyr-397 phosphorylation and requirement for ERK activation.

Pub. Date : 2004 Aug

PMID : 15174091






6 Functional Relationships(s)
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1 PDGF and FGF induce focal adhesion kinase (FAK) phosphorylation at Ser-910: dissociation from Tyr-397 phosphorylation and requirement for ERK activation. Tyrosine PTK2 protein tyrosine kinase 2 Mus musculus
2 PDGF and FGF induce focal adhesion kinase (FAK) phosphorylation at Ser-910: dissociation from Tyr-397 phosphorylation and requirement for ERK activation. Tyrosine PTK2 protein tyrosine kinase 2 Mus musculus
3 A rapid increase in the tyrosine phosphorylation of focal adhesion kinase (FAK) has been extensively documented in cells stimulated by multiple signaling molecules, but very little is known about the regulation of FAK phosphorylation at serine residues. Tyrosine PTK2 protein tyrosine kinase 2 Mus musculus
4 A rapid increase in the tyrosine phosphorylation of focal adhesion kinase (FAK) has been extensively documented in cells stimulated by multiple signaling molecules, but very little is known about the regulation of FAK phosphorylation at serine residues. Tyrosine PTK2 protein tyrosine kinase 2 Mus musculus
5 Furthermore, the selective phosphoinositide 3-kinase (PI 3-kinase) inhibitors wortmannin and LY 294002 abrogated FAK phosphorylation at Tyr-397 but did not interfere with PDGF-induced FAK phosphorylation at Ser-910. Tyrosine PTK2 protein tyrosine kinase 2 Mus musculus
6 Our results indicate that FAK phosphorylation at Tyr-397 and FAK phosphorylation at Ser-910 are induced in response to PDGF stimulation through different signaling pathways, namely PI 3-kinase and ERK, respectively. Tyrosine PTK2 protein tyrosine kinase 2 Mus musculus