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

• Verfasst von: Golks, Alexander [VerfasserIn]
• Verfasst von: Krammer, Peter H. [VerfasserIn]
• Verfasst von: Lavrik, Inna N. [VerfasserIn]
• Titel: C-FLIPR, a new regulator of death receptor-induced apoptosis
• Verf.angabe: Alexander Golks, Dirk Brenner, Cornelius Fritsch, Peter H. Krammer, and Inna N. Lavrik
• Jahr: 2005
• Umfang: 7 S.
• Fussnoten: Available online 4 January 2021 ; Elektronische Reproduktion der Druck-Ausgabe ; Im Titel ist das "R" bei c-FLIP tiefgestellt ; Gesehen am 04.03.2021
• Titel Quelle: Enthalten in: The journal of biological chemistry
• Ort Quelle: Bethesda, Md. : ASBMB Publications, 1905
• Jahr Quelle: 2005
• Band/Heft Quelle: 280(2005), 15 vom: 15. Apr., Seite 14507-14513
• ISSN Quelle: 1083-351X
• DOI: doi:10.1074/jbc.M414425200
• Datenträger: Online-Ressource
• Sprache: eng
• K10plus-PPN: 1750422352

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. Impor-/tantly, 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 isoforms in death receptor-mediated apoptosis.