Truncated RIP3 (tRIP3) acts upstream of FADD to induce apoptosis in the human hepatocellular carcinoma cell line QGY-7703

Biochemical and Biophysical Research Communications

Volumn 347, Issue 3, 2006, Pages 558-565

  Feng, Shanshan ^a   Ma, Li ^a   Yang, Yonghui ^a   Wu, Mian ^a  

^a UNIVERSITY OF SCIENCE AND TECHNOLOGY OF CHINA   (China)

Author keywords

Apoptosis; Dominant negative mutant; FADD; RIP3

Indexed keywords

AMINO ACID; CARRIER PROTEINS AND BINDING PROTEINS; FAS ASSOCIATED DEATH DOMAIN PROTEIN; RECEPTOR INTERACTING PROTEIN 3; TUMOR NECROSIS FACTOR RECEPTOR 1; UNCLASSIFIED DRUG;

APOPTOSIS; ARTICLE; CARBOXY TERMINAL SEQUENCE; CARCINOMA CELL; CELL DEATH; HUMAN; HUMAN CELL; LIVER CELL CARCINOMA; MUTATION; PRIORITY JOURNAL; SEQUENCE ALIGNMENT;

ADAPTOR PROTEINS, SIGNAL TRANSDUCING; AMINO ACID SEQUENCE; AMINO ACIDS; APOPTOSIS; CARCINOMA, HEPATOCELLULAR; CELL LINE, TUMOR; FAS-ASSOCIATED DEATH DOMAIN PROTEIN; HUMANS; LEUCINE; MOLECULAR SEQUENCE DATA; PROTEIN KINASES; RECEPTOR-INTERACTING PROTEIN SERINE-THREONINE KINASES; SEQUENCE ALIGNMENT; SEQUENCE HOMOLOGY, AMINO ACID; SIGNAL TRANSDUCTION;

EID: 33746214657     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2006.06.118     Document Type: Article

References (12)

1. Yu P.W., Huang B.C., Shen M., Quast J., Chan E., Xu X., Nolan G.P., Payan D.G., and Luo Y. Identification of RIP3, a RIP-like kinase that activates apoptosis and NF-κB. Curr. Biol. 9 (1999) 539-542
2. Sun X., Lee J., Nayas T., Baldwin D.T., Stewart T.A., and Dixit V.M. RIP3, a novel apoptosis-inducing kinase. J. Biol. Chem. 274 (1999) 16871-16875
3. Meylan E., and Tschopp J. The RIP kinases: crucial integrators of cellular stress. Trends Biochem. Sci. 30 (2005) 151-159
4. Stanger B.Z., Leder P., Lee T.H., Kim E., and Seed B. RIP: a novel protein containing a death domain that interacts with Fas/APO-1 (CD95) in yeast and causes cell death. Cell 81 (1995) 513-523
5. McCarthy J.V., Ni J., and Dixit V.M. RIP2 is a novel NF-κB-activating and cell death-inducing kinase. J. Biol. Chem. 273 (1998) 16968-16975
6. Meylan E., Martinon F., Thome M., Gschwendt M., and Tschopp J. RIP4 (DIK/PKK), a novel member of the RIP kinase family, activates NF-κB and is processed during apoptosis. EMBO Rep. 3 (2002) 1201-1208
7. Kasof G.M., Prosser J.C., Liu D., Lorenzi M.V., and Gomes B.C. The RIP-like kinase, RIP3, induces apoptosis and NF-κB nuclear translocation and localizes to mitochondria. FEBS Lett. 473 (2000) 285-291
8. Pazdernik N.J., Donner D.B., Goebl M.G., and Harrington M.A. Mouse receptor interacting protein 3 does not contain a caspase recruiting or a death domain but induces apoptosis and activates NF-κB. Mol. Cell. Biol. 19 (1999) 6500-6508
9. Sun X., Yin J., Starovasnik M.A., Fairbrother W.J., and Dixit V.M. Identification of a novel homotypic interaction motif required for the phosphorylation of receptor-interacting protein (RIP) by RIP3. J. Biol. Chem. 277 (2002) 9505-9511
10. Newton K., Sun X., and Dixit V.M. Kinase RIP3 is dispensable for normal NF-κBs, signaling by the B-cell and T-cell receptors, tumor necrosis factor receptor 1, and Toll-like receptor 2 and 4. Mol. Cell. Biol. 24 (2004) 1464-1469
11. Strasser A., and Newton K. FADD/MORT1, a signal transducer that can promote cell death or cell growth. Int. J. Biochem. Cell Biol. 31 (1999) 533-537
12. Yang Y., Ma J., Chen Y., and Wu M. Nucleocytoplasmic shuttling of receptor-interacting protein 3 (RIP3): identification of novel nuclear export and import signals in RIP3. J. Biol. Chem. 279 (2004) 38820-38829