c-FLIPR, a new regulator of death receptor-induced apoptosis

Alexander Golks, Dirk Brenner, Cornelius Fritsch, Peter H. Krammer*, Inna N. Lavrik

*Corresponding author for this work

Research output: Contribution to journalArticleResearchpeer-review

229 Citations (Scopus)

Abstract

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-FLIPL and c-FLIPS, 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-FLIPR, a death effector domain-only splice variant previously identified on the mRNA level. Importantly, c-FLIPR is recruited to the CD95 (Fas/APO-1) death-inducing signaling complex upon CD95 stimulation. Several properties of c-FLIPR are similar to C-FLIPS: 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-FLIPR and similar roles of c-FLIPR and C-FLIPS isofonns in death receptor-mediated apoptosis.

Original languageEnglish
Pages (from-to)14507-14513
Number of pages7
JournalJournal of Biological Chemistry
Volume280
Issue number15
DOIs
Publication statusPublished - 15 Apr 2005
Externally publishedYes

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