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Am J Physiol Cell Physiol 295: C1113-C1122, 2008. First published September 3, 2008; doi:10.1152/ajpcell.00238.2008
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PROTEIN AND VESICLE TRAFFICKING, CYTOSKELETON

Distinct phospho-forms of cortactin differentially regulate actin polymerization and focal adhesions

Anne E. Kruchten,* Eugene W. Krueger,* Yu Wang, and Mark A. McNiven

Department of Biochemistry and Molecular Biology and the Miles and Shirley Fiterman Center for Digestive Diseases, Mayo Clinic, Rochester, Minnesota

Submitted 1 May 2008 ; accepted in final form 28 August 2008

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, we tested the effects of different tyrosine and serine phospho-mutants of cortactin on lamellipodial protrusion, actin assembly within cells, and focal adhesion dynamics. Interestingly, while expression of either tyrosine or serine phospho-mimetic cortactin mutants resulted in increased lamellipodial protrusion and cell migration, these effects appeared to be via distinct processes. Cortactin mutants mimicking serine phosphorylation appeared to predominantly affect actin polymerization, whereas mutation of cortactin tyrosine residues resulted in alterations in focal adhesion turnover. Thus these findings provide novel insights into how distinct phospho-forms of cortactin may differentially contribute to actin and focal adhesion dynamics to control cell migration.

cell migration; phosphorylation


Address for reprint requests and other correspondence: M. A. McNiven, Dept. of Biochemistry and Molecular Biology, Mayo Clinic, 200 First St. SW, Guggenheim 1637, Rochester, MN 55905 (e-mail: mcniven.mark{at}mayo.edu)




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[Abstract] [Full Text] [PDF]


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