dc.contributor |
Universitat de Barcelona |
dc.contributor.author |
Serrador, Juan M. |
dc.contributor.author |
Alonso Lebrero, José L. |
dc.contributor.author |
Pozo, Miguel A. del |
dc.contributor.author |
Furthmayr, Heinz |
dc.contributor.author |
Schwartz-Albiez, Reinhard |
dc.contributor.author |
Calvo, Javier |
dc.contributor.author |
Lozano Soto, Francisco |
dc.contributor.author |
Sánchez-Madrid, Francisco |
dc.date |
2012-05-09T10:01:15Z |
dc.date |
2012-05-09T10:01:15Z |
dc.date |
1997-09-22 |
dc.identifier.citation |
0021-9525 |
dc.identifier.citation |
530389 |
dc.identifier.uri |
http://hdl.handle.net/2445/25214 |
dc.format |
15 p. |
dc.format |
application/pdf |
dc.language.iso |
eng |
dc.publisher |
Rockefeller University Press |
dc.relation |
Reproducció digital del document publicat a: http://dx.doi.org/10.1083/jcb.138.6.1409 |
dc.relation |
Journal of Cell Biology, 1997, vol. 138, núm. 6, p. 1409-1423 |
dc.relation |
http://dx.doi.org/10.1083/jcb.138.6.1409 |
dc.rights |
(c) Rockefeller University Press, 1997 |
dc.rights |
info:eu-repo/semantics/openAccess |
dc.subject |
Interacció cel·lular |
dc.subject |
Cèl·lules T |
dc.subject |
Cell interaction |
dc.title |
Moesin interacts with the cytoplasmic region of intercellular adhesion molecule-3 and is redistributed to the uropod of T Lymphocytes during cell polarization |
dc.type |
info:eu-repo/semantics/article |
dc.type |
info:eu-repo/semantics/publishedVersion |
dc.description.abstract |
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, ß-actin and ¿-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. |