References
- Henras, A. K., Soudet, J., Gerus, M., Lebaron, S., Caizergues-Ferrer, M., Mougin, A. and Henry, Y. (2008) The post-transcriptional steps of eukaryotic ribosome biogenesis. Cell. Mol. Life Sci. 65, 2334-2359. https://doi.org/10.1007/s00018-008-8027-0
- Yadavilli, S., Hegde, V. and Deutsch, W. A. (2007) Translocation of human ribosomal protein S3 to sites of DNA damage is dependent on ERK-mediated phosphorylation following genotoxic stress. DNA Repair 6, 1453-1462. https://doi.org/10.1016/j.dnarep.2007.04.009
- Kim, T. S., Kim, H. D. and Kim, J. (2009) PKCdelta-dependent functional switch of rpS3 between translation and DNA repair. Biochim. Biophys. Acta. 1793, 395-405. https://doi.org/10.1016/j.bbamcr.2008.10.017
- Lee, S. B., Kwon, I. S., Park, J., Lee, K. H., Ahn, Y., Lee, C., Kim, J., Choi, S. Y., Cho, S. W. and Ahn, J. Y. (2010) Ribosomal protein S3, a new substrate of Akt, serves as a signal mediator between neuronal apoptosis and DNA repair. J. Biol. Chem. 285, 29457-29468. https://doi.org/10.1074/jbc.M110.131367
- Wan, F., Anderson, D. E., Barnitz, R. A., Snow, A., Bidere, N., Zheng, L., Hegde, V., Lam, L. T., Staudt, L. M., Levens, D., Deutsch, W. A. and Lenardo, M. J. (2007) Ribosomal protein S3: a KH domain subunit in NF-kappaB complexes that mediates selective gene regulation. Cell 131, 927-939. https://doi.org/10.1016/j.cell.2007.10.009
- Kim, H. D., Lee, J. Y. and Kim, J. (2005) Erk phosphorylates threonine 42 residue of ribosomal protein S3. Biochem. Biophys. Res. Commun. 333, 110-115. https://doi.org/10.1016/j.bbrc.2005.05.079
- Kim, T. S., Kim, H. D., Shin, H. S. and Kim, J. (2009) Phosphorylation status of nuclear ribosomal protein S3 is reciprocally regulated by protein kinase Cδ and protein phosphatase 2A. J. Biol. Chem. 284, 21201-21208. https://doi.org/10.1074/jbc.M109.018168
- Jang, C. Y., Lee, J. Y. and Kim, J. (2004) RpS3, a DNA repair endonuclease and ribosomal protein, is involved in apoptosis. FEBS Lett. 560, 81-85. https://doi.org/10.1016/S0014-5793(04)00074-2
- Malumbres, M. and Barbacid, M. (2005) Mammalian cyclin- dependent kinases. Trends Biochem. Sci. 30, 630-641. https://doi.org/10.1016/j.tibs.2005.09.005
- Salaun, P., Rannou, Y. and Prigent, C. (2008) Cdk1, Plks, Auroras, and Neks: the mitotic bodyguards. Adv. Exp. Med. Biol. 617, 41-56. https://doi.org/10.1007/978-0-387-69080-3_4
- Holt, L. J., Tuch, B. B., Villen, J., Johnson, A. D., Gygi, S. P. and Morgan, D. O. (2009) Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution. Science 325, 1682-1686. https://doi.org/10.1126/science.1172867
- Bembenek, J. and Yu, H. (2003) Regulation of CDC14: pathways and checkpoints of mitotic exit. Front. Biosci. 8, d1275-d1287. https://doi.org/10.2741/1128
- Macaluso, M., Montanari, M., Cinti, C. and Giordano, A. (2005) Modulation of cell cycle components by epigenetic and genetic events. Semin. Oncol. 32, 452-457. https://doi.org/10.1053/j.seminoncol.2005.07.009
- Bhat, K. P., Itahana, K., Jin, A. and Zhang, Y. (2004) Essential role of ribosomal protein L11 in mediating growth inhibition-induced p53 activation. EMBO J. 23, 2402-2412 https://doi.org/10.1038/sj.emboj.7600247
- Dai, M. S. and Lu, H. (2004) Inhibition of MDM2-mediated p53 ubiquitination and degradation by ribosomal protein L5. J. Biol. Chem. 279, 44475-44482. https://doi.org/10.1074/jbc.M403722200
- Zhang, Y., Wolf, G. W., Bhat, K., Jin, A., Allio, T., Burkhart, W. A. and Xiong, Y. (2003) Ribosomal protein L11 negatively regulates oncoprotein MDM2 and mediates a p53-dependent ribosomal-stress checkpoint pathway. Mol. Cell Biol. 23, 8902-8912. https://doi.org/10.1128/MCB.23.23.8902-8912.2003
- Gou, Y., Shi, Y., Zhang, Y., Nie, Y., Wang, J., Song, J., Jin, H., He, L., Gao, L., Qiao, L., Wu, K. and Fan, D. (2010) Ribosomal protein L6 promotes growth and cell cycle progression through upregulating cyclin E in gastric cancer cells. Biochem. Biophys. Res. Commun. 393, 788-793. https://doi.org/10.1016/j.bbrc.2010.02.083
- Chen, Y. C., Chang, M. Y., Shiau, A. L., Yo, Y. T. and Wu, C. L. (2007) Mitochondrial ribosomal protein S36 delays cell cycle progression in association with p53 modification and p21(WAF1/CIP1) expression. J. Cell. Biochem. 100, 981-990. https://doi.org/10.1002/jcb.21079
- Ventimiglia, F. A. and Wool, I. G. (1974) A kinase that transfers the gamma-phosphoryl group of GTP to proteins of eukaryotic 40S ribosomal subunits. Proc. Natl. Acad. Sci. U. S. A. 71, 350-354. https://doi.org/10.1073/pnas.71.2.350
- Francis, T. A. and Roberts, S. (1982) Influence of the state of ribosome association on the phosphorylation of ribosomal proteins in isolated ribosome-protein kinase systems from rat cerebral cortex. Biochem. J. 208, 289-300. https://doi.org/10.1042/bj2080289
- Naranda, T. and Ballesta, J. P. (1991) Phosphorylation controls binding of acidic proteins to the ribosome. Proc. Natl. Acad. Sci. U. S. A. 88, 10563-10567. https://doi.org/10.1073/pnas.88.23.10563
- Moreno, S. and Nurse, P. (1990) Substrates for p34cdc2: in vivo veritas? Cell 61, 549-551. https://doi.org/10.1016/0092-8674(90)90463-O
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