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RIPK3  -  receptor-interacting serine-threonine...

Homo sapiens

Synonyms: RIP-3, RIP-like protein kinase 3, RIP3, Receptor-interacting protein 3, Receptor-interacting serine/threonine-protein kinase 3
 
 
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Disease relevance of RIPK3

  • In this study, we showed that a truncated form of RIP3 (tRIP3) containing only the unique C-terminal region (aa 224-518) induced significant apoptosis in human hepatocellular carcinoma cells QGY-7703 [1].
  • Importantly, real-time PCR analysis reveals that the ratio of RIP3 gamma to RIP3 is significantly increased in colon and lung cancers relative to their matched normal tissues, indicating that RIP3 gamma might be a major splice form associated with tumorigenesis [2].
 

High impact information on RIPK3

 

Biological context of RIPK3

 

Anatomical context of RIPK3

  • RIP3 was localized by immunofluorescence to the mitochondrion and may play a key role in the mitochondrial disruptions often associated with apoptosis [5].
  • Northern blots indicate that rip3 mRNA displays a restricted pattern of expression including regions of the adult central nervous system [5].
  • A double-knockout mutant (rip3/aleA null cells) exhibits a further reduction in receptor activation of guanylyl cyclase, and these cells display almost no cell polarization or movement in cAMP gradients [6].
  • Using normal and abnormal human fetal hearts and cultured normal human fetal cardiomyocytes, we show that congenital cardiovascular malformations are associated with the overexpression of hRIP3, and evidence is found for a certain association between overexpression of hRIP3 and homocysteine-induced congenital cardiovascular malformations [7].
 

Associations of RIPK3 with chemical compounds

 

Regulatory relationships of RIPK3

  • In contrast, the RIP3 dominant negative (RIP3-DN) was found unable to block FADD-induced apoptosis [1].
 

Other interactions of RIPK3

  • RIP3-mediated apoptosis was inhibited by Bcl-2, Bcl-x(L), dominant-negative FADD, as well as the general caspase inhibitor Z-VAD [5].
  • RIP3, however, attenuates both RIP and TNF receptor-1-induced NF-kappaB activation [8].
  • As with RIP and RIP2, the kinase domain of RIP3 was not required for either NFkappaB activation or apoptosis induction [10].
 

Analytical, diagnostic and therapeutic context of RIPK3

  • Further dissection of caspase involvement in RIP3-induced apoptosis indicated inhibition by the more specific inhibitors Z-DEVD (caspase-3, -6, -7, -8, and -10) and Z-VDVAD (caspase-2) [5].

References

  1. Truncated RIP3 (tRIP3) acts upstream of FADD to induce apoptosis in the human hepatocellular carcinoma cell line QGY-7703. Feng, S., Ma, L., Yang, Y., Wu, M. Biochem. Biophys. Res. Commun. (2006) [Pubmed]
  2. RIP3 beta and RIP3 gamma, two novel splice variants of receptor-interacting protein 3 (RIP3), downregulate RIP3-induced apoptosis. Yang, Y., Hu, W., Feng, S., Ma, J., Wu, M. Biochem. Biophys. Res. Commun. (2005) [Pubmed]
  3. Nucleocytoplasmic shuttling of receptor-interacting protein 3 (RIP3): identification of novel nuclear export and import signals in RIP3. Yang, Y., Ma, J., Chen, Y., Wu, M. J. Biol. Chem. (2004) [Pubmed]
  4. Identification of a novel homotypic interaction motif required for the phosphorylation of receptor-interacting protein (RIP) by RIP3. Sun, X., Yin, J., Starovasnik, M.A., Fairbrother, W.J., Dixit, V.M. J. Biol. Chem. (2002) [Pubmed]
  5. The RIP-like kinase, RIP3, induces apoptosis and NF-kappaB nuclear translocation and localizes to mitochondria. Kasof, G.M., Prosser, J.C., Liu, D., Lorenzi, M.V., Gomes, B.C. FEBS Lett. (2000) [Pubmed]
  6. A novel Ras-interacting protein required for chemotaxis and cyclic adenosine monophosphate signal relay in Dictyostelium. Lee, S., Parent, C.A., Insall, R., Firtel, R.A. Mol. Biol. Cell (1999) [Pubmed]
  7. Homocysteine, hRIP3 and congenital cardiovascular malformations. Zhao, L., Wang, G., Lu, D., Wu, J., Song, F., Dong, J., Bi, Z., Li, Y. Anat. Embryol. (2006) [Pubmed]
  8. RIP3, a novel apoptosis-inducing kinase. Sun, X., Lee, J., Navas, T., Baldwin, D.T., Stewart, T.A., Dixit, V.M. J. Biol. Chem. (1999) [Pubmed]
  9. A single amino acid change (Asp 53 --> Ala53) converts Survivin from anti-apoptotic to pro-apoptotic. Song, Z., Liu, S., He, H., Hoti, N., Wang, Y., Feng, S., Wu, M. Mol. Biol. Cell (2004) [Pubmed]
  10. Identification of RIP3, a RIP-like kinase that activates apoptosis and NFkappaB. Yu, P.W., Huang, B.C., Shen, M., Quast, J., Chan, E., Xu, X., Nolan, G.P., Payan, D.G., Luo, Y. Curr. Biol. (1999) [Pubmed]
 
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