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Prepublished online as a Blood First Edition Paper on August 7, 2003; DOI 10.1182/blood-2002-12-3807. This Article Full Text (PDF) All Versions of this Article: 2002-12-3807v1 102/12/3890    most recent Alert me when this article is cited Alert me if a correction is posted Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Rights and Permissions Citing Articles Citing Articles via HighWire Citing Articles via CrossRef Citing Articles via Google Scholar Google Scholar Articles by Brown, M. J Articles by Shaw, S. Search for Related Content PubMed PubMed Citation Articles by Brown, M. J Articles by Shaw, S. Social Bookmarking                   What's this? Submitted December 17, 2002 Accepted July 21, 2003 Chemokine stimulation of human peripheral blood T lymphocytes induces rapid dephosphorylation of ERMs which facilitates loss of microvilli and polarization Martin J Brown, Ruchika Nijhara, John A Hallam, Michelle Gignac, Kenneth M Yamada, Stanley L Erlandsen, Jerome Delon, Michael Kruhlak, and Stephen Shaw* Experimental Immunology Branch, National Cancer Institute, Bethesda, MD, USA Image Analysis Laboratory, SAIC-Frederick, Frederick, MD, USA Craniofacial Developmental Biology and Regeneration Branch, National Institute of Dental and Craniofacial Research, Bethesda, MD, USA Department of Genetics, Cell Biology & Development, University of Minnesota Medical School, Minneapolis, MN, USA Departement de Biologie Cellulaire, INSERM U567 / CNRS UMR 8104, Institut COCHIN, Paris, France * Corresponding author; email: sshaw{at}nih.gov. 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 cells (PBT) is sufficient to induce rapid resorption of microvilli. Microvilli in other cells are regulated by ERM proteins (ezrin/radixin/moesin), 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-ERMs (cpERM) in resting PBT show a punctate peripheral distribution consistent with localization to microvilli. cpERM dephosphorylation begins within seconds of stimulation by chemokines (SDF-1 or SLC), and ERMs lose their punctate distribution with kinetics paralleling the loss of microvilli. cpERMs 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, while 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 cpERMs which may in turn facilitate two aspects of cytoskeletal reorganization involved in lymphocyte recruitment: loss of microvilli and polarization. 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