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First published online 6 March 2007
doi: 10.1242/jcs.03408

Journal of Cell Science 120, 1157-1167 (2007)
Published by The Company of Biologists 2007
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Research Article

Phosphorylation of adducin by protein kinase C{delta} promotes cell motility

Chien-Lin Chen1, Yeun-Ting Hsieh1,2 and Hong-Chen Chen1,*

1 Department of Life Science and the Graduate Institute of Biomedical Sciences, National Chung Hsing University, Taichung 40227, Taiwan
2 Department of Obstetrics and Gynecology, Taichung Veterans General Hospital, Taichung 40705, Taiwan

* Author for correspondence (e-mail: hcchen{at}nchu.edu.tw)

Accepted 15 January 2007

Protein kinase C{delta} (PKC{delta}) has been implicated to play a crucial role in cell proliferation, differentiation and apoptosis. In this study, we have investigated the role of PKC{delta} in cell motility using Madin-Darby canine kidney cells. Overexpression of PKC{delta} promoted membrane protrusions, concomitant with increased cell motility. By contrast, suppression of PKC{delta} expression by RNA interference inhibited cell motility. Moreover, a fraction of PKC{delta} was detected at the edge of membrane protrusions in which it colocalized with adducin, a membrane skeletal protein whose phosphorylation state is important for remodeling of the cortical actin cytoskeleton. Elevated expression of PKC{delta} correlated with increased phosphorylation of adducin at Ser726 in intact cells. In vitro, PKC{delta}, but not PKC{alpha}, directly phosphorylated the Ser726 of adducin. Finally, we demonstrated that overexpression of both adducin and PKC{delta} could generate a synergistic effect on promoting cell spreading and cell migration. Our results support a positive role for PKC{delta} in cell motility and strongly suggest a link between PKC{delta} activity, adducin phosphorylation and cell motility.

Key words: PKC{delta}, Adducin, Motility, Phosphorylation






© The Company of Biologists Ltd 2007