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CD43 Interacts With Moesin and Ezrin and Regulates Its
Redistribution to the Uropods of T Lymphocytes at the Cell-Cell
Contacts
Juan M. Serrador,
Marta Nieto,
José L. Alonso-Lebrero,
Miguel A. del Pozo,
Javier Calvo,
Heinz Furthmayr,
Reinhard Schwartz-Albiez,
Francisco Lozano,
Roberto González-Amaro,
Paloma Sánchez-Mateos, and
Francisco Sánchez-Madrid
From the Servicio de Inmunología, Hospital de la Princesa,
Universidad Autónoma de Madrid, Madrid, Spain; the Department of
Pathology, Stanford University, Stanford, CA; the School of Medicine,
University of San Luis Potosí, San Luis Potosí, Mexico;
the Servicio de Inmunología, Hospital General Universitario
Gregorio Marañón, Madrid, Spain; the Servei d'Immunologia,
Hospital Clinic, Barcelona, Spain; and the Tumor Immunology Program,
German Cancer Research Center, Heidelberg, Germany.
Chemokines as well as the signaling through the adhesion molecules
intercellular adhesion molecule (ICAM)-3 and CD43 are
able to induce in T lymphocytes their switching from a spherical to a
polarized motile morphology, with the formation of a uropod at the rear
of the cell. We investigated here the role of CD43 in the regulation of
T-cell polarity, CD43-cytoskeletal interactions, and lymphocyte
aggregation. Pro-activatory anti-CD43 monoclonal antibody (MoAb)
induced polarization of T lymphocytes with redistribution of CD43 to
the uropod and the CCR2 chemokine receptor to the leading edge of the
cell. Immunofluorescence analysis showed that all three
ezrin-radixin-moesin (ERM) actin-binding proteins
localized in the uropod of both human T lymphoblasts stimulated with
anti-CD43 MoAb and tumor-infiltrating T lymphocytes. Radixin localized
at the uropod neck, whereas ezrin and moesin colocalized with CD43 in
the uropod. Biochemical analyses showed that ezrin and moesin coimmunoprecipitated with CD43 in T lymphoblasts. Furthermore, in these
cells, the CD43-associated moesin increased after stimulation through
CD43. The interaction of moesin and ezrin with CD43 was specifically
mediated by the cytoplasmic domain of CD43, as shown by precipitation
of both ERM proteins with a GST-fusion protein containing the CD43
cytoplasmic tail. Videomicroscopy analysis of homotypic cell
aggregation induced through CD43 showed that cellular uropods mediate
cell-cell contacts and lymphocyte recruitment. Immunofluorescence
microscopy performed in parallel showed that uropods enriched in CD43
and moesin localized at the cell-cell contact areas of cell aggregates.
The polarization and homotypic cell aggregation induced through CD43
was prevented by butanedione monoxime, indicating the involvement of
myosin cytoskeleton in these phenomena. Altogether, these data indicate
that CD43 plays an important regulatory role in remodeling T-cell
morphology, likely through its interaction with actin-binding proteins
ezrin and moesin. In addition, the redistribution of CD43 to the uropod region of migrating lymphocytes and during the formation of cell aggregates together with the enhancing effect of anti-CD43 antibodies on lymphocyte cell recruitment suggest that CD43 plays a key role in
the regulation of cell-cell interactions during lymphocyte traffic.
Blood, Vol. 91 No. 12 (June 15), 1998:
pp. 4632-4644
© 1998 by The American Society of Hematology.
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