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© The Rockefeller University Press, 0021-9525/1997//1409 $5.00
The Journal of Cell Biology, Volume 138, Number 6, , 1997 1409-1423

Article

Moesin Interacts with the Cytoplasmic Region of Intercellular Adhesion Molecule-3 and Is Redistributed to the Uropod of T Lymphocytes during Cell Polarization



Juan M. Serrador, José L. Alonso-Lebrero, Miguel A. del Pozo, Heinz Furthmayr{ddagger}, Reinhard Schwartz-Albiez§, Javier Calvo||, Francisco Lozano||, and Francisco Sánchez-Madrid

Servicio de Inmunología, Hospital de la Princesa, Universidad Autónoma de Madrid, 28006 Madrid, Spain; {ddagger} Department of Pathology, Stanford University, Stanford, California 94305-5324; § Tumor Immunology Program, German Cancer Research Center, Heidelberg, Germany D-69120; and || Servei Inmunología, Hospital Clinic, 08036 Barcelona, Spain

During activation, T lymphocytes become motile cells, switching from a spherical to a polarized shape. Chemokines and other chemotactic cytokines induce lymphocyte polarization with the formation of a uropod in the rear pole, where the adhesion receptors intercellular adhesion molecule-1 (ICAM-1), ICAM-3, and CD44 redistribute. We have investigated membrane–cytoskeleton interactions that play a key role in the redistribution of adhesion receptors to the uropod. Immunofluorescence analysis showed that the ERM proteins radixin and moesin localized to the uropod of human T lymphoblasts treated with the chemokine RANTES (regulated on activation, normal T cell expressed, and secreted), a polarization-inducing agent; radixin colocalized with arrays of myosin II at the neck of the uropods, whereas moesin decorated the most distal part of the uropod and colocalized with ICAM-1, ICAM-3, and CD44 molecules. Two other cytoskeletal proteins, β-actin and {alpha}-tubulin, clustered at the cell leading edge and uropod, respectively, of polarized lymphocytes. Biochemical analysis showed that moesin coimmunoprecipitates with ICAM-3 in T lymphoblasts stimulated with either RANTES or the polarization- inducing anti–ICAM-3 HP2/19 mAb, as well as in the constitutively polarized T cell line HSB-2. In addition, moesin is associated with CD44, but not with ICAM-1, in polarized T lymphocytes. A correlation between the degree of moesin–ICAM-3 interaction and cell polarization was found as determined by immunofluorescence and immunoprecipitation analysis done in parallel. The moesin–ICAM-3 interaction was specifically mediated by the cytoplasmic domain of ICAM-3 as revealed by precipitation of moesin with a GST fusion protein containing the ICAM-3 cytoplasmic tail from metabolically labeled Jurkat T cell lysates. The interaction of moesin with ICAM-3 was greatly diminished when RANTES-stimulated T lymphoblasts were pretreated with the myosin-disrupting drug butanedione monoxime, which prevents lymphocyte polarization. Altogether, these data indicate that moesin interacts with ICAM-3 and CD44 adhesion molecules in uropods of polarized T cells; these data also suggest that these interactions participate in the formation of links between membrane receptors and the cytoskeleton, thereby regulating morphological changes during cell locomotion.

Abbreviations used in this paper: ERM, ezrin, radixin, and moesin; FN80, 80-kD fibronectin fragment; ICAM, intercellular adhesion molecule; IL, interleukin; MCP-1, monocyte chemotactic protein; RANTES, regulated on activation, normal T cell expressed, and secreted.

Address all correspondence to F. Sánchez-Madrid, Servicio de Immunología, Hospital de la Princesa, universidad Autónoma de Madrid, 28006 Madrid, Spain. Tel.: 34-1-4023347. Fax: 34-1-3092496. E-mail: fsmadrid/ princesa{at}hup.es


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