Title : FAK phosphorylation at Tyr-925 regulates cross-talk between focal adhesion turnover and cell protrusion.

Pub. Date : 2011 Apr

PMID : 21289086






6 Functional Relationships(s)
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1 FAK phosphorylation at Tyr-925 regulates cross-talk between focal adhesion turnover and cell protrusion. Tyrosine PTK2 protein tyrosine kinase 2 Mus musculus
2 Focal adhesion kinase (FAK), a major signaling component of FAs, is involved in the disassembly process of FAs through phosphorylation and dephosphorylation of its tyrosine residues, but the role of such phosphorylations in nascent FA formation and turnover near the cell front and in cell protrusion is less well understood. Tyrosine PTK2 protein tyrosine kinase 2 Mus musculus
3 Focal adhesion kinase (FAK), a major signaling component of FAs, is involved in the disassembly process of FAs through phosphorylation and dephosphorylation of its tyrosine residues, but the role of such phosphorylations in nascent FA formation and turnover near the cell front and in cell protrusion is less well understood. Tyrosine PTK2 protein tyrosine kinase 2 Mus musculus
4 In the present study, we demonstrate that, depending on the phosphorylation status of Tyr-925 residue, FAK modulates cell migration via two specific mechanisms. Tyrosine PTK2 protein tyrosine kinase 2 Mus musculus
5 Together, our results demonstrate that phosphorylation of FAK at Tyr-925 is required for FAK-mediated cell migration and cell protrusion. Tyrosine PTK2 protein tyrosine kinase 2 Mus musculus
6 Together, our results demonstrate that phosphorylation of FAK at Tyr-925 is required for FAK-mediated cell migration and cell protrusion. Tyrosine PTK2 protein tyrosine kinase 2 Mus musculus