| 15701649 |
Golks A, Brenner D, Fritsch C, Krammer PH, Lavrik IN: c-FLIPR, a new regulator of death receptor-induced apoptosis. J Biol Chem. 2005 Apr 15;280(15):14507-13. Epub 2005 Feb 8.
c-FLIPs (c-FLICE inhibitory proteins) play an essential role in regulation of death receptor-induced apoptosis. Multiple splice variants of c-FLIP have been described on the mRNA level; so far only two of them, c-FLIP (L) and c-FLIP (S,) had been found to be expressed at the protein level. In this report, we reveal the endogenous expression of a third isoform of c-FLIP. We demonstrate its presence in a number of T and B cell lines as well as in primary human T cells. We identified this isoform as c-FLIP (R), a death effector domain-only splice variant previously identified on the mRNA level. Impor-/tantly, c-FLIP (R) is recruited to the CD95 (Fas/APO-1) death-inducing signaling complex upon CD95 stimulation. Several properties of c-FLIP (R) are similar to c-FLIP (S): both isoforms have a short half-life, a similar pattern of expression during activation of primary human T cells, and are strongly induced in T cells upon CD3/CD28 costimulation. Taken together, our data demonstrate endogenous expression of c-FLIP (R) and similar roles of c-FLIP (R) and c-FLIP (S) isoforms in death receptor-mediated apoptosis. |
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