Serine/threonine-protein kinase VRK1 is an enzyme that in humans is encoded by the VRK1gene.[1][2]
This gene encodes a member of the vaccinia-related kinase (VRK) family of serine/threonine protein kinases. This gene is widely expressed in human tissues and has increased expression in actively dividing cells, such as those in testis, thymus, fetal liver, and carcinomas. Its protein localizes to the nucleus and has been shown to promote the stability and nuclear accumulation of a transcriptionally active p53 molecule and, in vitro, to phosphorylate Thr18 of p53 and reduce p53 ubiquitination. This gene, therefore, may regulate cell proliferation. This protein also phosphorylates histone, casein, and the transcription factors ATF2 (activating transcription factor 2) and c-JUN.[2]
References
↑Nezu J, Oku A, Jones MH, Shimane M (Feb 1998). "Identification of two novel human putative serine/threonine kinases, VRK1 and VRK2, with structural similarity to vaccinia virus B1R kinase". Genomics. 45 (2): 327–31. doi:10.1006/geno.1997.4938. PMID9344656.
Sugimoto J, Yamauchi T, Hatakeyama T, Isobe M (1999). "Isolation and mapping of a polymorphic CA repeat sequence at the human VRK1 locus". J. Hum. Genet. 44 (2): 133–4. doi:10.1007/s100380050127. PMID10083742.
Sayed M, Kim SO, Salh BS, et al. (2000). "Stress-induced activation of protein kinase CK2 by direct interaction with p38 mitogen-activated protein kinase". J. Biol. Chem. 275 (22): 16569–73. doi:10.1074/jbc.M000312200. PMID10747897.
Lopez-Borges S, Lazo PA (2000). "The human vaccinia-related kinase 1 (VRK1) phosphorylates threonine-18 within the mdm-2 binding site of the p53 tumour suppressor protein". Oncogene. 19 (32): 3656–64. doi:10.1038/sj.onc.1203709. PMID10951572.
Latonen L, Taya Y, Laiho M (2001). "UV-radiation induces dose-dependent regulation of p53 response and modulates p53-HDM2 interaction in human fibroblasts". Oncogene. 20 (46): 6784–93. doi:10.1038/sj.onc.1204883. PMID11709713.
Barcia R, López-Borges S, Vega FM, Lazo PA (2002). "Kinetic properties of p53 phosphorylation by the human vaccinia-related kinase 1". Arch. Biochem. Biophys. 399 (1): 1–5. doi:10.1006/abbi.2001.2746. PMID11883897.
Nichols RJ, Traktman P (2004). "Characterization of three paralogous members of the Mammalian vaccinia related kinase family". J. Biol. Chem. 279 (9): 7934–46. doi:10.1074/jbc.M310813200. PMID14645249.
Sevilla A, Santos CR, Vega FM, Lazo PA (2004). "Human vaccinia-related kinase 1 (VRK1) activates the ATF2 transcriptional activity by novel phosphorylation on Thr-73 and Ser-62 and cooperates with JNK". J. Biol. Chem. 279 (26): 27458–65. doi:10.1074/jbc.M401009200. PMID15105425.
Sevilla A, Santos CR, Barcia R, et al. (2004). "c-Jun phosphorylation by the human vaccinia-related kinase 1 (VRK1) and its cooperation with the N-terminal kinase of c-Jun (JNK)". Oncogene. 23 (55): 8950–8. doi:10.1038/sj.onc.1208015. PMID15378002.
Santos CR, Rodríguez-Pinilla M, Vega FM, et al. (2006). "VRK1 signaling pathway in the context of the proliferation phenotype in head and neck squamous cell carcinoma". Mol. Cancer Res. 4 (3): 177–85. doi:10.1158/1541-7786.MCR-05-0212. PMID16547155.
Valbuena A, López-Sánchez I, Vega FM, et al. (2007). "Identification of a dominant epitope in human vaccinia-related kinase 1 (VRK1) and detection of different intracellular subpopulations". Arch. Biochem. Biophys. 465 (1): 219–26. doi:10.1016/j.abb.2007.06.005. PMID17617371.