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Full-Text Articles in Biochemistry, Biophysics, and Structural Biology
Distinct Phospho-Forms Of Cortactin Differentially Regulate Actin Polymerization And Focal Adhesions, Anne E. Kruchten, Eugene W. Krueger, Yu Wang, Mark A. Mcniven
Distinct Phospho-Forms Of Cortactin Differentially Regulate Actin Polymerization And Focal Adhesions, Anne E. Kruchten, Eugene W. Krueger, Yu Wang, Mark A. Mcniven
Faculty Publications
Cortactin is an actin-binding protein that is overexpressed in many cancers and is a substrate for both tyrosine and serine/threonine kinases. Tyrosine phosphorylation of cortactin has been observed to increase cell motility and invasion in vivo, although it has been reported to have both positive and negative effects on actin polymerization in vitro. In contrast, serine phosphorylation of cortactin has been shown to stimulate actin assembly in vitro. Currently, the effects of cortactin serine phosphorylation on cell migration are unclear, and furthermore, how the distinct phospho-forms of cortactin may differentially contribute to cell migration has not been directly compared. Therefore, …