| First Author | Banh C | Year | 2009 |
| Journal | Blood | Volume | 114 |
| Issue | 26 | Pages | 5299-306 |
| PubMed ID | 19855082 | Mgi Jnum | J:155699 |
| Mgi Id | MGI:4415109 | Doi | 10.1182/blood-2009-06-228353 |
| Citation | Banh C, et al. (2009) Immunoregulatory functions of KLRG1 cadherin interactions are dependent on forward and reverse signaling. Blood 114(26):5299-306 |
| abstractText | KLRG1 is an inhibitory receptor expressed on a subset of mature T and NK cells. Recently, E-, N-, and R-cadherin have been identified as ligands for KLRG1. Cadherins are a large family of transmembrane or membrane-associated glycoproteins that were thought to only bind specifically to other cadherins to mediate specific cell-to-cell adhesion in a Ca(2+)-dependent manner. The consequences of cadherin KLRG1 molecular interactions are not well characterized. Here, we report that the first 2 extracellular domains of cadherin are sufficient to initiate a KLRG1-dependent signaling. We also demonstrate that KLRG1 engagement inhibits cadherin-dependent cellular adhesion and influences dendritic cell secretion of inflammatory cytokines, thereby exerting immunosuppressive effects. Consistent with this, engagement of cadherin by KLRG1 molecule induces cadherin tyrosine phosphorylation. Therefore, KLRG1/cadherin interaction leads to the generation of a bidirectional signal in which both KLRG1 and cadherin activate downstream signaling cascades simultaneously. Taken together, our results provide novel insights on how KLRG1 and E-cadherin interactions are integrated to differentially regulate not only KLRG1(+) cells, but also E-cadherin-expressing cells, such as dendritic cells. |
