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 α-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.
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22 September 1997
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September 22 1997
Moesin Interacts with the Cytoplasmic Region of Intercellular Adhesion Molecule-3 and Is Redistributed to the Uropod of T Lymphocytes during Cell Polarization
Heinz Furthmayr,
Heinz Furthmayr
Servicio de Inmunología, Hospital de la Princesa, Universidad Autónoma de Madrid, 28006 Madrid, Spain; ‡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
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Reinhard Schwartz-Albiez,
Reinhard Schwartz-Albiez
Servicio de Inmunología, Hospital de la Princesa, Universidad Autónoma de Madrid, 28006 Madrid, Spain; ‡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
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Javier Calvo,
Javier Calvo
Servicio de Inmunología, Hospital de la Princesa, Universidad Autónoma de Madrid, 28006 Madrid, Spain; ‡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
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Francisco Lozano,
Francisco Lozano
Servicio de Inmunología, Hospital de la Princesa, Universidad Autónoma de Madrid, 28006 Madrid, Spain; ‡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
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Juan M. Serrador
José L. Alonso-Lebrero
Miguel A. del Pozo
Heinz Furthmayr
Servicio de Inmunología, Hospital de la Princesa, Universidad Autónoma de Madrid, 28006 Madrid, Spain; ‡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
Reinhard Schwartz-Albiez
Servicio de Inmunología, Hospital de la Princesa, Universidad Autónoma de Madrid, 28006 Madrid, Spain; ‡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
Javier Calvo
Servicio de Inmunología, Hospital de la Princesa, Universidad Autónoma de Madrid, 28006 Madrid, Spain; ‡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
Francisco Lozano
Servicio de Inmunología, Hospital de la Princesa, Universidad Autónoma de Madrid, 28006 Madrid, Spain; ‡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
Francisco Sánchez-Madrid
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/ [email protected]
Received:
February 21 1997
Revision Received:
May 29 1997
Online ISSN: 1540-8140
Print ISSN: 0021-9525
1997
J Cell Biol (1997) 138 (6): 1409–1423.
Article history
Received:
February 21 1997
Revision Received:
May 29 1997
Citation
Juan M. Serrador, José L. Alonso-Lebrero, Miguel A. del Pozo, Heinz Furthmayr, Reinhard Schwartz-Albiez, Javier Calvo, Francisco Lozano, Francisco Sánchez-Madrid; Moesin Interacts with the Cytoplasmic Region of Intercellular Adhesion Molecule-3 and Is Redistributed to the Uropod of T Lymphocytes during Cell Polarization . J Cell Biol 22 September 1997; 138 (6): 1409–1423. doi: https://doi.org/10.1083/jcb.138.6.1409
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