| First Author | Shirakawa J | Year | 2006 |
| Journal | Int Immunol | Volume | 18 |
| Issue | 6 | Pages | 951-7 |
| PubMed ID | 16636013 | Mgi Jnum | J:109134 |
| Mgi Id | MGI:3625806 | Doi | 10.1093/intimm/dxl031 |
| Citation | Shirakawa J, et al. (2006) LFA-1-dependent lipid raft recruitment of DNAM-1 (CD226) in CD4+ T cell. Int Immunol 18(6):951-7 |
| abstractText | Upon antigen recognition by the TCR, both the leukocyte adhesion molecules DNAM-1 and leukocyte function-associated antigen-1 (LFA-1) associate with lipid rafts and form peripheral supra-molecular activation clusters that surround central-supra-molecular activation clusters at the immunological synapse. The serine residue in the cytoplasmic tail of DNAM-1 is responsible for this association of DNAM-1 with lipid rafts. The TCR-mediated signal also induces physical association of DNAM-1 with LFA-1, for which the serine phosphorylation of DNAM-1 is also responsible. However, how the serine residue is involved in lipid raft recruitment of DNAM-1 has remained unclear. Here, we show that, although the TCR-mediated signal induced the serine phosphorylation of DNAM-1, DNAM-1 did not associate with lipid rafts in CD4(+) T cells derived from mice deficient in LFA-1 expression, indicating that lipid raft recruitment of DNAM-1 depends on LFA-1 expression. These results suggest that the serine phosphorylation of DNAM-1 primarily induces physical association of DNAM-1 with LFA-1, which then takes DNAM-1 into lipid raft compartment. |
