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Molecular and Cellular Biology, September 2000, p. 6638-6645, Vol. 20, No. 18
0270-7306/00/$04.00+0

The Death Domain Kinase RIP Is Essential for TRAIL (Apo2L)-Induced Activation of Ikappa B Kinase and c-Jun N-Terminal Kinase

Yong Lin,1 Anne Devin,1 Amy Cook,1 Maccon M. Keane,2,dagger Michelle Kelliher,3 Stanley Lipkowitz,2 and Zheng-gang Liu1,*

Department of Cell and Cancer Biology1 and Department of Genetics,2 Medicine Branch, Division of Clinical Sciences, National Cancer Institute, National Institutes of Health, Bethesda, Maryland 20892, and University of Massachusetts Medical Center, Worcester, Massachusetts 016053

Received 13 March 2000/Returned for modification 17 April 2000/Accepted 16 June 2000

Tumor necrosis factor (TNF)-related apoptosis-inducing ligand (TRAIL) (Apo2 ligand [Apo2L]) is a member of the TNF superfamily and has been shown to have selective antitumor activity. Although it is known that TRAIL (Apo2L) induces apoptosis and activates NF-kappa B and Jun N-terminal kinase (JNK) through receptors such as TRAIL-R1 (DR4) and TRAIL-R2 (DR5), the components of its signaling cascade have not been well defined. In this report, we demonstrated that the death domain kinase RIP is essential for TRAIL-induced Ikappa B kinase (IKK) and JNK activation. We found that ectopic expression of the dominant negative mutant RIP, RIP(559-671), blocks TRAIL-induced IKK and JNK activation. In the RIP null fibroblasts, TRAIL failed to activate IKK and only partially activated JNK. The endogenous RIP protein was detected by immunoprecipitation in the TRAIL-R1 complex after TRAIL treatment. More importantly, we found that RIP is not involved in TRAIL-induced apoptosis. In addition, we also demonstrated that the TNF receptor-associated factor 2 (TRAF2) plays little role in TRAIL-induced IKK activation although it is required for TRAIL-mediated JNK activation. These results indicated that the death domain kinase RIP, a key factor in TNF signaling, also plays a pivotal role in TRAIL-induced IKK and JNK activation.

* Corresponding author. Mailing address: Medicine Branch, NCI, NIH, Bldg. 10, Rm. 6N105, 9000 Rockville Pike, Bethesda, MD 20892. Phone: (301) 435-6351. Fax: (301) 402-1997. E-mail: zgliu{at}helix.nih.gov.

dagger Present address: Department of Medical Oncology, University Hospital of Galway, Galway, Republic of Ireland.

Molecular and Cellular Biology, September 2000, p. 6638-6645, Vol. 20, No. 18
0270-7306/00/$04.00+0


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