Циклинзависимая киназа 3
Функции
CDK3 восстанавливает нормальный рост и деление у дрожжевых мутантов Saccharomyces cerevisiae с неактивным геном cdc28, что позволяет предположить его возможную вовлечённость в контроль клеточного цикла. CDK3 способна фосфорилировать гистон H1 и взаимодействует с циклином неизвестного типа[2].
Примечания
Литература
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- Gyuris J, Golemis E, Chertkov H, Brent R (1993). “Cdi1, a human G1 and S phase protein phosphatase that associates with Cdk2”. Cell. 75 (4): 791—803. DOI:10.1016/0092-8674(93)90498-F. PMID 8242750.
- Sasaguri T, Ishida A, Kosaka C, et al. (1996). “Phorbol ester inhibits the phosphorylation of the retinoblastoma protein without suppressing cyclin D-associated kinase in vascular smooth muscle cells”. J. Biol. Chem. 271 (14): 8345—51. DOI:10.1074/jbc.271.14.8345. PMID 8626531.
- Meikrantz W, Schlegel R (1996). “Suppression of apoptosis by dominant negative mutants of cyclin-dependent protein kinases”. J. Biol. Chem. 271 (17): 10205—9. DOI:10.1074/jbc.271.17.10205. PMID 8626584.
- Hofmann F, Livingston DM (1996). “Differential effects of cdk2 and cdk3 on the control of pRb and E2F function during G1 exit”. Genes Dev. 10 (7): 851—61. DOI:10.1101/gad.10.7.851. PMID 8846921.
- Lamphere L, Fiore F, Xu X, et al. (1997). “Interaction between Cdc37 and Cdk4 in human cells”. Oncogene. 14 (16): 1999—2004. DOI:10.1038/sj.onc.1201036. PMID 9150368. S2CID 25236893.
- Braun K, Hölzl G, Soucek T, et al. (1998). “Investigation of the cell cycle regulation of cdk3-associated kinase activity and the role of cdk3 in proliferation and transformation”. Oncogene. 17 (17): 2259—69. DOI:10.1038/sj.onc.1202145. PMID 9811456. S2CID 12470182.
- Yamochi T, Semba K, Tsuji K, et al. (2002). “ik3-1/Cables is a substrate for cyclin-dependent kinase 3 (cdk 3)”. Eur. J. Biochem. 268 (23): 6076—82. DOI:10.1046/j.0014-2956.2001.02555.x. PMID 11733001.
- Sato H, Nishimoto I, Matsuoka M (2002). “ik3-2, a relative to ik3-1/cables, is associated with cdk3, cdk5, and c-abl”. Biochim. Biophys. Acta. 1574 (2): 157—63. DOI:10.1016/S0167-4781(01)00367-0. PMID 11955625.
- Schang LM, Bantly A, Schaffer PA (2002). “Explant-induced reactivation of herpes simplex virus occurs in neurons expressing nuclear cdk2 and cdk4”. J. Virol. 76 (15): 7724—35. DOI:10.1128/JVI.76.15.7724-7735.2002. PMC 136347. PMID 12097586.
- Ota T, Suzuki Y, Nishikawa T, et al. (2004). “Complete sequencing and characterization of 21,243 full-length human cDNAs”. Nat. Genet. 36 (1): 40—5. DOI:10.1038/ng1285. PMID 14702039.
- Ren S, Rollins BJ (2004). “Cyclin C/cdk3 promotes Rb-dependent G0 exit”. Cell. 117 (2): 239—51. DOI:10.1016/S0092-8674(04)00300-9. PMID 15084261. S2CID 890866.
- Zhang Y, Wolf-Yadlin A, Ross PL, et al. (2005). “Time-resolved mass spectrometry of tyrosine phosphorylation sites in the epidermal growth factor receptor signaling network reveals dynamic modules”. Mol. Cell. Proteomics. 4 (9): 1240—50. DOI:10.1074/mcp.M500089-MCP200. PMID 15951569.
- Beausoleil SA, Villén J, Gerber SA, et al. (2006). “A probability-based approach for high-throughput protein phosphorylation analysis and site localization”. Nat. Biotechnol. 24 (10): 1285—92. DOI:10.1038/nbt1240. PMID 16964243. S2CID 14294292.
- Olsen JV, Blagoev B, Gnad F, et al. (2006). “Global, in vivo, and site-specific phosphorylation dynamics in signaling networks”. Cell. 127 (3): 635—48. DOI:10.1016/j.cell.2006.09.026. PMID 17081983. S2CID 7827573.
- Wissing J, Jänsch L, Nimtz M, et al. (2007). “Proteomics analysis of protein kinases by target class-selective prefractionation and tandem mass spectrometry” (PDF). Mol. Cell. Proteomics. 6 (3): 537—47. DOI:10.1074/mcp.T600062-MCP200. PMID 17192257. S2CID 40974821.
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