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Papers In Press, published online ahead of print January 27, 2004
Pathology, University of Pittsburgh, Pittsburgh, PA 15261
Corresponding Author: wellsa{at}msx.upmc.edu
Myosin-based cell contractile force is considered to be a critical process in cell motility. However, for EGF-induced fibroblast migration, molecular links between EGF receptor (EGFR) activation and force generation have not been clarified. Herein, we demonstrate that EGF stimulation increases myosin light chain (MLC) phosphorylation, a marker for contractile force, concomitant with PKC activity in mouse fibroblasts expressing human EGFR constructs. Interestingly, PKCd is most strongly phosphorylated isoform, and the preferential PKCd inhibitor rottlerin largely prevented EGF-induced phosphorylation of PKC substrates and MARCKS. The pathway through which EGFR activates PKCd is suggested by the fact that the MEK-1 inhibitor U0126 and the PI3 kinase inhibitor LY294002 had no effect on PKCd activation, whereas lack of PLCg signaling resulted in delayed PKCd activation. EGF-enhanced MLC phosphorylation was prevented by a specific MLC kinase inhibitor ML-7, and the PKC inhibitors chelerythrine chloride and rottlerin. Further indicating that PKCd is required, a dominant negative PKCd construct or RNAi-mediated PKCd depletion also prevented MLC phosphorylation. In the absence of PLC signaling, MLC phosphorylation and cell force generation was delayed similarly to PKCd activation. All of the interventions that blocked PKCd activation or MLC phosphorylation abrogated EGF-induced cell contractile force generation and motility. Our results suggest that PKCd activation is responsible for a major part of EGF-induced fibroblast contractile force generation. Hence, we identify here a new pathway helping to govern cell motility, with PLC signaling playing a role in activation of PKCd to promote the acute phase of EGF-induced MLC activation.
J. Biol. Chem, 10.1074/jbc.M311981200
Submitted on October 31, 2003
Revised on January 26, 2004
Accepted on January 27, 2004
EGF induces fibroblast contractility and motility via a PKC
-dependent pathway
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