Casper/c-FLIP is physically and functionally associated with NF-κB1 p105

Biochemical and Biophysical Research Communications

Volumn 309, Issue 4, 2003, Pages 980-985

  Li, Zhiqin ^a   Zhang, Jingbo ^a   Chen, Danying ^b   Shu, Hong Bing ^b,c  

^a INSTITUTE OF BASIC MEDICAL SCIENCES   (China)

^b PEKING UNIVERSITY   (China)

^c NATIONAL JEWISH MEDICAL AND RESEARCH CENTER   (United States)

Author keywords

Caspase; Casper c FLIP; NF B; p105

Indexed keywords

CASPASE 8; CASPER; IMMUNOGLOBULIN ENHANCER BINDING PROTEIN; PROTEIN P105; PROTEIN P50; UNCLASSIFIED DRUG;

APOPTOSIS; ARTICLE; CARBOXY TERMINAL SEQUENCE; CONTROLLED STUDY; EMBRYO; ENZYME ACTIVITY; ENZYME STRUCTURE; GENETIC TRANSFECTION; HUMAN; HUMAN CELL; IMMUNOPRECIPITATION; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN EXPRESSION; PROTEIN FUNCTION; PROTEIN PROCESSING; PROTEIN PROTEIN INTERACTION; REGULATORY MECHANISM;

EID: 0141453242     PISSN: 0006291X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbrc.2003.08.104     Document Type: Article

References (36)

1. Baker S.J., Reddy E.P. Modulation of life and death by the TNF receptor superfamily. Oncogene. 17:1998;3261-3270.
2. Ashkenazi A., Dixit V.M. Apoptosis control by death and decay receptors. Curr. Opin. Cell Biol. 11:1999;255-260.
3. Baud V., Karin M. Signal transduction by tumor necrosis factor and its relatives. Trends Cell Biol. 11:2001;372-377.
4. Locksley R.M., Killeen N., Lenardo M.J. The TNF and TNF receptor superfamilies: integrating mammalian biology. Cell. 104:2001;487-501.
5. Chen G., Goeddel D.V. TNF-R1 signaling: a beautiful pathway. Science. 296:2002;1634-1635.
6. Wajant H., Pfizenmaier K., Scheurich P. Tumor necrosis factor signaling. Cell Death Differ. 10:2003;45-65.
7. Shu H.B., Halpin D.R., Goeddel D.V. Casper is a FADD- and caspase-related inducer of apoptosis. Immunity. 6:1997;751-763.
8. Irmler M., Thome M., Hahne M., Schneider P., Hofmann K., Steiner V., Bodmer J.L., Schroter M., Burns K., Mattmann C., Rimoldi D., French L.E., Tschopp J. Inhibition of death receptor signals by cellular FLIP. Nature. 388:1997;190-195.
9. Hu S., Vincenz C., Ni J., Gentz R., Dixit V.M. I-FLICE, a novel inhibitor of tumor necrosis factor receptor-1- and CD-95-induced apoptosis. J. Biol. Chem. 272:1997;17255-17257.
10. Goltsev Y.V., Kovalenko A.V., Arnold E., Varfolomeev E.E., Brodianskii V.M., Wallach D. CASH, a novel caspase homologue with death effector domains. J. Biol. Chem. 272:1997;19641-19644.
11. Srinivasula S.M., Ahmad M., Ottilie S., Bullrich F., Banks S., Wang Y., Fernandes-Alnemri T., Croce C.M., Litwack G., Tomaselli K.J., Armstrong R.C., Alnemri E.S. FLAME-1, a novel FADD-like anti-apoptotic molecule that regulates Fas/TNFR1-induced apoptosis. J. Biol. Chem. 272:1997;18542-18545.
12. Han D.K., Chaudhary P.M., Wright M.E., Friedman C., Trask B.J., Riedel R.T., Baskin D.G., Schwartz S.M., Hood L. MRIT, a novel death-effector domain-containing protein, interacts with caspases and BclXL and initiates cell death. Proc. Natl. Acad. Sci. USA. 94:1997;11333-11338.
13. Inohara N., Koseki T., Hu Y., Chen S., Nunez G. CLARP, a death effector domain-containing protein interacts with caspase-8 and regulates apoptosis. Proc. Natl. Acad. Sci. USA. 94:1997;10717-10722.
14. Rasper D.M., Vaillancourt J.P., Hadano S., Houtzager V.M., Seiden I., Keen S.L., Tawa P., Xanthoudakis S., Nasir J., Martindale D., Koop B.F., Peterson E.P., Thornberry N.A., Huang J., MacPherson D.P., Black S.C., Hornung F., Lenardo M.J., Hayden M.R., Roy S., Nicholson D.W. Cell death attenuation by 'Usurpin,' a mammalian DED-caspase homologue that precludes caspase-8 recruitment and activation by the CD-95 (Fas, APO-1) receptor complex. Cell Death Differ. 5:1998;271-288.
15. Thome M., Tschopp J. Regulation of lymphocyte proliferation and death by FLIP. Nat. Rev. Immunol. 1:2001;50-58.
16. Bin L., Li X., Xu L.G., Shu H.B. The short splice form of Casper/c-FLIP is a major cellular inhibitor of TRAIL-induced apoptosis. FEBS Lett. 510:2002;37-40.
17. Burns T.F., El-Deiry W.S. Identification of inhibitors of TRAIL-induced death (ITIDs) in the TRAIL-sensitive colon carcinoma cell line SW480 using a genetic approach. J. Biol. Chem. 276:2001;37879-37886.
18. Thome M., Schneider P., Hofmann K., Fickenscher H., Meinl E., Neipel F., Mattmann C., Burns K., Bodmer J.L., Schroter M., Scaffidi C., Krammer P.H., Peter M.E., Tschopp J. Viral FLICE-inhibitory proteins (FLIPs) prevent apoptosis induced by death receptors. Nature. 386:1997;517-521.
19. Krueger A., Baumann S., Krammer P.H., Kirchhoff S. FLICE-inhibitory proteins: regulators of death receptor-mediated apoptosis. Mol. Cell. Biol. 21:2001;8247-8254.
20. Yeh W.C., Itie A., Elia A.J., Ng M., Shu H.B., Wakeham A., Mirtsos C., Suzuki N., Bonnard M., Goeddel D.V., Mak T.W. Requirement for Casper (c-FLIP) in regulation of death receptor-induced apoptosis and embryonic development. Immunity. 12:2000;633-642.
21. Scaffidi C., Schmitz I., Krammer P.H., Peter M.E. The role of c-FLIP in modulation of CD95-induced apoptosis. J. Biol. Chem. 274:1999;1541-1548.
22. Chang D.W., Xing Z., Pan Y., Algeciras-Schimnich A., Barnhart B.C., Yaish-Ohad S., Peter M.E., Yang X. c-FLIP(L) is a dual function regulator for caspase-8 activation and CD95-mediated apoptosis. EMBO J. 21:2002;3704-3714.
23. Micheau O., Thome M., Schneider P., Holler N., Tschopp J., Nicholson D.W., Briand C., Grutter M.G. The long form of FLIP is an activator of caspase-8 at the Fas death-inducing signaling complex. J. Biol. Chem. 277:2002;45162-45171.
24. Hu W.H., Johnson H., Shu H.B. Activation of NF-kappaB by FADD, Casper, and caspase-8. J. Biol. Chem. 275:2000;10838-10844.
25. Kataoka T., Budd R.C., Holler N., Thome M., Martinon F., Irmler M., Burns K., Hahne M., Kennedy N., Kovacsovics M., Tschopp J. The caspase-8 inhibitor FLIP promotes activation of NF-kappaB and Erk signaling pathways. Curr. Biol. 10:2000;640-648.
26. Chaudhary P.M., Eby M.T., Jasmin A., Kumar A., Liu L., Hood L. Activation of the NF-kappaB pathway by caspase-8 and its homologs. Oncogene. 19:2000;4451-4460.
27. Chen D., Li X., Zhai Z., Shu H.B. ZIN is a RIP-interacting Zinc finger protein that inhibits TNF- and IL-1-induced NF-κB activation. J. Biol. Chem. 277:2003;15985-15991.
28. Sambrook J., Fritch E.F., Maniatis T. Molecular Cloning: a Laboratory Manual. second ed. 1994;Cold Spring Harbor Laboratory Press, Cold Spring Harbor, New York.
29. Hsu H., Xiong J., Goeddel D.V. The TNF receptor 1-associated protein TRADD signals cell death and NF-kappa B activation. Cell. 81:1995;495-504.
30. Rice N.R., MacKichan M.L., Israel A. The precursor of NF-kappa B p50 has I kappaB-like functions. Cell. 71:1992;243-253.
31. Liou H.C., Nolan G.P., Ghosh S., Fujita T., Baltimore D. The NF-kappa B p50 precursor, p105, contains an internal I kappa B-like inhibitor that preferentially inhibits p50. EMBO J. 11:1992;3003-3009.
32. Karin M., Lin A. NF-kappaB at the crossroads of life and death. Nat. Immunol. 3:2002;221-227.
33. Orlowski R.Z., Baldwin A.S. Jr. NF-kappaB as a therapeutic target in cancer. Trends Mol. Med. 8:2002;385-389.
34. Salmeron A., Janzen J., Soneji Y., Bump N., Kamens J., Allen H., Ley S.C. Direct phosphorylation of NF-κB1 p105 by the IκB kinase complex on serine 927 is essential for signal-induced p105 proteolysis. J. Biol. Chem. 276:2001;22215-22222.
35. Orian A., Gonen H., Bercovich B., Fajerman I., Eytan E., Israel A., Mercurio F., Iwai K., Schwartz A.L., Ciechanover A. SCF(beta)(-TrCP) ubiquitin ligase-mediated processing of NF-kappaB p105 requires phosphorylation of its C-terminus by IkappaB kinase. EMBO J. 19:2000;2580-2591.
36. Liu L., Eby M.T., Rathore N., Sinha S.K., Kumar A., Chaudhary P.M. The human herpes virus 8-encoded viral FLICE inhibitory protein physically associates with and persistently activates the Ikappa B kinase complex. J. Biol. Chem. 277:2002;13745-13751.