Serine phosphorylation of a 67-kDa protein in human T lymphocytes represents an accessory receptor-mediated signaling event
| Autor: | S W Henning, S C Meuer, Y Samstag |
|---|---|
| Rok vydání: | 1994 |
| Předmět: | |
| Zdroj: | The Journal of Immunology. 152:4808-4815 |
| ISSN: | 1550-6606 0022-1767 |
| DOI: | 10.4049/jimmunol.152.10.4808 |
| Popis: | Phosphorylation on serine residues of a 67-kDa cytoplasmic protein (p67) occurs as an early signaling event after stimulation of resting human T cells via CD2 but not via TCR/CD3. Phosphorylation of p67 is, however, not restricted to CD2 stimulation because it can also be induced by costimulation through CD4 and CD8 coreceptors when approximated to the TCR-CD3 complex, suggesting a common signaling mechanism for these accessory receptors of the Ig superfamily. Because late functional responses of T cell activation like IL-2 production and DNA synthesis correlate with phosphorylation of p67, this intracellular event may represent an accessory receptor-mediated costimulatory second signal for human T cell activation. The biochemical characteristics (m.w. and isoelectric point) of p67 are identical with those of the actin binding protein L-plastin (Fimbrin), a cytoplasmic protein that contains two Ca2+ binding sites and a calmodulin binding domain. Moreover, p67 reacts specifically with an L-Plastin (Fimbrin) antiserum. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|