Accès gratuit
Numéro
Med Sci (Paris)
Volume 18, Numéro 5, Mai 2002
Page(s) 540 - 542
Section Le Magazine : Nouvelles
DOI https://doi.org/10.1051/medsci/2002185540
Publié en ligne 15 mai 2002
  1. Delon J, Kaibuchi K, Germain RN. Exclusion of CD43 from the immunological synapse is mediated by phosphorylation-regulated relocation of the cytoskeletal adaptor moesin. Immunity 2001; 15 : 691–701.
  2. Roumier A, Olivo-Marin JC, Arpin M, et al. The membrane-microfilament linker ezrin is involved in the formation of the immunological synapse and in T cell activation. Immunity 2001; 15 : 715–28.
  3. Allenspach EJ, Cullinan P, Tong J, et al. ERM-dependent movement of CD43 defines a novel protein complex distal to the immunological synapse. Immunity 2001; 15 : 739–50.
  4. Delon J, Germain RN. Information transfer at the immunological synapse. Curr Biol 2000; 10 : R923–33.
  5. Bretscher A, Chambers D, Nguyen R, et al. ERM-merlin and EBP50 protein families in plasma membrane organization and function. Annu Rev Cell Dev Biol 2000; 16 : 113–43.
  6. Gautreau A, Louvard D, Arpin M. ERM proteins and NF2 tumor suppressor: the Yin and Yang of cortical actin organization and cell growth signaling. Curr Opin Cell Biol 2002; 14 : 104–9.
  7. Pearson MA, Recezk D, Bretscher A, et al. Structure of the ERM protein moesin reveals the FERM domain fold masked by an extended actin binding tail domain. Cell 2000; 101 : 259–70.
  8. Serrador JM, Nieto M, Alonso-Lebrero JL, et al. CD43 interacts with moesin and ezrin and regulates its redistribution to the uropods of T lymphocytes at the cell-cell contacts. Blood 1998; 91 : 4632–44.
  9. Cyster JG, Shotton DM, Williams AF. The dimensions of the T lymphocyte glycoprotein leukosialin and identification of linear protein epitopes that can be modified by glycosylation. EMBO J 1991; 10 : 893–902.
  10. Manjunath N, Correa M, Ardman M, et al. Negative regulation of T-cell adhesion and activation by CD43. Nature 1995; 377 : 535–8.

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