Receptor-interacting serine/threonine-protein kinase 3 is an enzyme that in humans is encoded by the RIPK3gene.[1][2][3][4]
The product of this gene is a member of the receptor-interacting protein (RIP) family of serine/threonine protein kinases, and contains a C-terminal domain unique from other RIP family members. The encoded protein is predominantly localized to the cytoplasm, and can undergo nucleocytoplasmic shuttling dependent on novel nuclear localization and export signals. It is a component of the tumor necrosis factor (TNF) receptor-I signaling complex, and can induce apoptosis and weakly activate the NF-kappaB transcription factor.[3]
↑ 1.01.1Yu PW, Huang BC, Shen M, Quast J, Chan E, Xu X, Nolan GP, Payan DG, Luo Y (Jun 1999). "Identification of RIP3, a RIP-like kinase that activates apoptosis and NFkappaB". Curr Biol. 9 (10): 539–42. doi:10.1016/S0960-9822(99)80239-5. PMID10339433.
↑Sun X, Lee J, Navas T, Baldwin DT, Stewart TA, Dixit VM (Jul 1999). "RIP3, a novel apoptosis-inducing kinase". J Biol Chem. 274 (24): 16871–5. doi:10.1074/jbc.274.24.16871. PMID10358032.
↑ 4.04.1Li J, McQuade T, Siemer AB, Napetschnig J, Moriwaki K, Hsiao YS, Damko E, Moquin D, Walz T, McDermott A, Chan FK, Wu H. (July 2012) The RIP1/RIP3 necrosome forms a functional amyloid signaling complex required for programmed necrosis. Cell150 (2):339-50. doi:10.1016/j.cell.2012.06.019. PMID22817896
Further reading
Kasof GM, Prosser JC, Liu D, et al. (2000). "The RIP-like kinase, RIP3, induces apoptosis and NF-kappaB nuclear translocation and localizes to mitochondria". FEBS Lett. 473 (3): 285–91. doi:10.1016/S0014-5793(00)01473-3. PMID10818227.
Sun X, Yin J, Starovasnik MA, et al. (2002). "Identification of a novel homotypic interaction motif required for the phosphorylation of receptor-interacting protein (RIP) by RIP3". J. Biol. Chem. 277 (11): 9505–11. doi:10.1074/jbc.M109488200. PMID11734559.
Bouwmeester T, Bauch A, Ruffner H, et al. (2004). "A physical and functional map of the human TNF-alPha/NF-kappa B signal transduction pathway". Nat. Cell Biol. 6 (2): 97–105. doi:10.1038/ncb1086. PMID14743216.
Meylan E, Burns K, Hofmann K, et al. (2004). "RIP1 is an essential mediator of Toll-like receptor 3-induced NF-kappa B activation". Nat. Immunol. 5 (5): 503–7. doi:10.1038/ni1061. PMID15064760.
Yang Y, Ma J, Chen Y, Wu M (2004). "Nucleocytoplasmic shuttling of receptor-interacting protein 3 (RIP3): identification of novel nuclear export and import signals in RIP3". J. Biol. Chem. 279 (37): 38820–9. doi:10.1074/jbc.M401663200. PMID15208320.
Yang Y, Hu W, Feng S, et al. (2005). "RIP3 beta and RIP3 gamma, two novel splice variants of receptor-interacting protein 3 (RIP3), downregulate RIP3-induced apoptosis". Biochem. Biophys. Res. Commun. 332 (1): 181–7. doi:10.1016/j.bbrc.2005.04.114. PMID15896315.
Zhao L, Wang G, Lu D, et al. (2006). "Homocysteine, hRIP3 and congenital cardiovascular malformations". Anat. Embryol. 211 (3): 203–12. doi:10.1007/s00429-005-0074-9. PMID16429275.
Feng S, Ma L, Yang Y, Wu M (2006). "Truncated RIP3 (tRIP3) acts upstream of FADD to induce apoptosis in the human hepatocellular carcinoma cell line QGY-7703". Biochem. Biophys. Res. Commun. 347 (3): 558–65. doi:10.1016/j.bbrc.2006.06.118. PMID16844082.
Ahn KS, Sethi G, Krishnan K, Aggarwal BB (2007). "Gamma-tocotrienol inhibits nuclear factor-kappaB signaling pathway through inhibition of receptor-interacting protein and TAK1 leading to suppression of antiapoptotic gene products and potentiation of apoptosis". J. Biol. Chem. 282 (1): 809–20. doi:10.1074/jbc.M610028200. PMID17114179.