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Blood, 1 December 2003, Vol. 102, No. 12, pp. 3890-3899.
Prepublished online as a Blood First Edition Paper on August 7, 2003; DOI 10.1182/blood-2002-12-3807.
 Previous Article | Table of Contents | Next Article 
CHEMOKINES
Chemokine stimulation of human peripheral blood T lymphocytes induces rapid dephosphorylation of ERM proteins, which facilitates loss of microvilli and polarization
Martin J. Brown,
Ruchika Nijhara,
John A. Hallam,
Michelle Gignac,
Kenneth M. Yamada,
Stanley L. Erlandsen,
Jérôme Delon,
Michael Kruhlak, and
Stephen Shaw
From the National Cancer Institute, Experimental Immunology Branch, Bethesda, MD; SAIC-Frederick, Image Analysis Laboratory, Frederick, MD; National Institute of Dental and Craniofacial Research, Craniofacial Developmental Biology and Regeneration Branch, Bethesda, MD; University of Minnesota Medical School, Department of Genetics, Cell Biology, and Development, Minneapolis; and Institut COCHIN, Departement de Biologie Cellulaire, INSERM U567/CNRS UMR 8104, Paris, France.
Lymphocyte microvilli mediate initial rolling-adhesion along endothelium but are lost during transmigration from circulation to tissue. However, the mechanism for resorption of lymphocyte microvilli remains unexplored. We show that chemokine stimulation of human peripheral blood T (PBT) cells is sufficient to induce rapid resorption of microvilli. Microvilli in other cells are regulated by ezrin/radixin/moesin (ERM) proteins, which link the plasma membrane to the cortical F-actin cytoskeleton; maintenance of these linkages requires ERM activation, reflected by phosphorylation at a specific carboxy-terminal threonine residue. Carboxyphosphorylated-ERM (cpERM) proteins in resting PBT cells show a punctate peripheral distribution consistent with localization to microvilli. cpERM dephosphorylation begins within seconds of stimulation by chemokines (stromal derived factor 1 [SDF-1] or secondary lymphoid tissue cytokine), and ERM proteins lose their punctate distribution with kinetics paralleling the loss of microvilli. The cpERM proteins are preferentially associated with the cytoskeleton at rest and this association is lost with chemokine-induced dephosphorylation. Transfection studies show that a dominant-negative ERM construct destroys microvilli, whereas a construct mimicking cpERM facilitates formation of microvilli, retards chemokine-induced loss of microvilli, and markedly impairs chemokine-induced polarization. Thus, chemokine induces rapid dephosphorylation and inactivation of cpERM, which may in turn facilitate 2 aspects of cytoskeletal reorganization involved in lymphocyte recruitment: loss of microvilli and polarization.
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