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Programme in Cell Biology, Hospital for Sick Children, Toronto, Ontario, Canada, and Department of Biochemistry, University of Toronto, Toronto, Ontario, Canada
Coronins are a family of conserved actin-associated proteins that have been implicated in a variety of cellular processes dependent on actin rearrangements. In this study, we show that in primary human neutrophils, coronins-1–4 and -7 are expressed. Coronin-1 accumulates at the leading edge of migrating neutrophils and at the nascent phagosome. Inhibition of coronin function by transduction of a dominant-negative form of the protein leads to inhibition of chemotaxis and a reduction in neutrophil spreading and adhesion. This inhibition appears to correlate with changes in the distribution of F-actin structures within the cell. In addition, phagocytosis is inhibited, but neither secretion nor activation of the NADPH oxidase appears to be affected. Together, these results show that coronins are required for actin-dependent changes in cell morphology that lead to migration and phagocytosis.
The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked advertisement in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.
1 This work was supported by a grant from the Canadian Institutes of Health Research. S.G. is the current holder of the Pitblado Chair in Cell Biology. W.S.T. is a recipient of a Canada Research Chair in Molecular Cell Biology.
2 Current address: Division of Nephrology, Duke University Medical Center, Durham, NC 27708.
3 Address correspondence and reprint requests to Dr. William S. Trimble, Programme in Cell Biology, Hospital for Sick Children, 555 University Avenue, Toronto, Ontario M5G 1X8, Canada. E-mail address: wtrimble{at}sickkids.on.ca
4 Abbreviations used in this paper: FL, full length; fMLF, N-formyl-Met-Leu-Phe; RT, room temperature.
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