| First Author | Peled M | Year | 2018 |
| Journal | J Immunol | Volume | 201 |
| Issue | 9 | Pages | 2824-2831 |
| PubMed ID | 30275048 | Mgi Jnum | J:267225 |
| Mgi Id | MGI:6258208 | Doi | 10.4049/jimmunol.1800839 |
| Citation | Peled M, et al. (2018) EF Hand Domain Family Member D2 Is Required for T Cell Cytotoxicity. J Immunol 201(9):2824-2831 |
| abstractText | Programmed cell death 1 (PD-1) is a major coinhibitory receptor and a member of the immunological synapse (IS). To uncover proteins that regulate PD-1 recruitment to the IS, we searched for cytoskeleton-related proteins that also interact with PD-1 using affinity purification mass spectrometry. Among these proteins, EF hand domain family member D2 (EFHD2), a calcium binding adaptor protein, was functionally and mechanistically analyzed for its contribution to PD-1 signaling. EFHD2 was required for PD-1 to inhibit cytokine secretion, proliferation, and adhesion of human T cells. Interestingly, EFHD2 was also required for human T cell-mediated cytotoxicity and for mounting an antitumor immune response in a syngeneic murine tumor model. Mechanistically, EFHD2 contributed to IS stability, lytic vesicles trafficking, and granzyme B secretion. Altogether, EFHD2 is an important regulator of T cell cytotoxicity and further studies should evaluate its role in T cell-mediated inflammation. |
