PITSLRE serine/threonine-protein kinase CDC2L1 is an enzyme that in humans is encoded by the CDC2L1gene.
This gene encodes a member of the p34Cdc2 protein kinase family. p34Cdc2 kinase family members are known to be essential for eukaryotic cell cycle control. This gene is in close proximity to CDC2L2, a nearly identical gene in the same chromosomal region. The gene loci including this gene, CDC2L2, as well as metalloprotease MMP21/22, consist of two identical, tandemly linked genomic regions which are thought to be a part of the larger region that has been duplicated. This gene and CDC2L2 were shown to be deleted or altered frequently in neuroblastoma with amplified MYCN genes. The protein kinase encoded by this gene could be cleaved by caspases and was demonstrated to play roles in cell apoptosis. Several alternatively spliced variants of this gene have been reported.
↑Eipers PG, Barnoski BL, Han J, Carroll AJ, Kidd VJ (Mar 1992). "Localization of the expressed human p58 protein kinase chromosomal gene to chromosome 1p36 and a highly related sequence to chromosome 15". Genomics. 11 (3): 621–9. doi:10.1016/0888-7543(91)90069-Q. PMID1774066.
↑Mikolajczyk M, Shi J, Vaillancourt RR, Sachs NA, Nelson M (Sep 2003). "The cyclin-dependent kinase 11(p46) isoform interacts with RanBPM". Biochem. Biophys. Res. Commun. 310 (1): 14–8. doi:10.1016/j.bbrc.2003.08.116. PMID14511641.
Lahti JM, Valentine M, Xiang J, et al. (1994). "Alterations in the PITSLRE protein kinase gene complex on chromosome 1p36 in childhood neuroblastoma". Nat. Genet. 7 (3): 370–5. doi:10.1038/ng0794-370. PMID7920654.
Xiang J, Lahti JM, Grenet J, et al. (1994). "Molecular cloning and expression of alternatively spliced PITSLRE protein kinase isoforms". J. Biol. Chem. 269 (22): 15786–94. PMID8195233.
Beyaert R, Kidd VJ, Cornelis S, et al. (1997). "Cleavage of PITSLRE kinases by ICE/CASP-1 and CPP32/CASP-3 during apoptosis induced by tumor necrosis factor". J. Biol. Chem. 272 (18): 11694–7. doi:10.1074/jbc.272.18.11694. PMID9115219.
Loyer P, Trembley JH, Lahti JM, Kidd VJ (1998). "The RNP protein, RNPS1, associates with specific isoforms of the p34cdc2-related PITSLRE protein kinase in vivo". J. Cell Sci. 111 (11): 1495–506. PMID9580558.
Tang D, Gururajan R, Kidd VJ (1998). "Phosphorylation of PITSLRE p110 isoforms accompanies their processing by caspases during Fas-mediated cell death". J. Biol. Chem. 273 (26): 16601–7. doi:10.1074/jbc.273.26.16601. PMID9632733.
Cornelis S, Bruynooghe Y, Denecker G, et al. (2000). "Identification and characterization of a novel cell cycle-regulated internal ribosome entry site". Mol. Cell. 5 (4): 597–605. doi:10.1016/S1097-2765(00)80239-7. PMID10882096.
Trembley JH, Hu D, Hsu LC, et al. (2002). "PITSLRE p110 protein kinases associate with transcription complexes and affect their activity". J. Biol. Chem. 277 (4): 2589–96. doi:10.1074/jbc.M109755200. PMID11709559.
Zhang S, Cai M, Zhang S, et al. (2002). "Interaction of p58(PITSLRE), a G2/M-specific protein kinase, with cyclin D3". J. Biol. Chem. 277 (38): 35314–22. doi:10.1074/jbc.M202179200. PMID12082095.
Chen S, Yin X, Zhu X, et al. (2003). "The C-terminal kinase domain of the p34cdc2-related PITSLRE protein kinase (p110C) associates with p21-activated kinase 1 and inhibits its activity during anoikis". J. Biol. Chem. 278 (22): 20029–36. doi:10.1074/jbc.M300818200. PMID12624090.
de Graaf K, Hekerman P, Spelten O, et al. (2004). "Characterization of cyclin L2, a novel cyclin with an arginine/serine-rich domain: phosphorylation by DYRK1A and colocalization with splicing factors". J. Biol. Chem. 279 (6): 4612–24. doi:10.1074/jbc.M310794200. PMID14623875.
Sachs NA, Vaillancourt RR (2004). "Cyclin-dependent kinase 11p110 and casein kinase 2 (CK2) inhibit the interaction between tyrosine hydroxylase and 14-3-3". J. Neurochem. 88 (1): 51–62. doi:10.1046/j.1471-4159.2003.02119.x. PMID14675149.
Yang L, Li N, Wang C, et al. (2004). "Cyclin L2, a novel RNA polymerase II-associated cyclin, is involved in pre-mRNA splicing and induces apoptosis of human hepatocellular carcinoma cells". J. Biol. Chem. 279 (12): 11639–48. doi:10.1074/jbc.M312895200. PMID14684736.