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Identifiers and Description
Gene Model Identifier
CDK1 (Cyclin-Dependent protein Kinase)
PreTt21599 | 44.m00266 | 3714.m00112
Cyclin-dependent protein kinase; localizes to domains associated with mature basal bodies of ciliary rows and to both the polykineties and haplokinety of the oral apparatus; partial knockout implicates this CDK in chromatin condensation
Cyclin-dependent kinases (cdks) are a family of serine-threonine kinases that are involved in cell cycle control and cell division in eukaryotes. Cdks are catalytic subunits that are activated by association with proteins called cyclins, forming cyclin-cdk complexes. Cdk kinase activity is regulated by cyclin binding, phosphorylation and dephosphorylation, protein degradation, protein-protein interactions with cdk inhibitors, and subcellular localization.
Tetrahymena thermophila Cdk1p shares homology with cdk homologs from other eukaryotes. It contains 11 catalytic domains characteristic of protein kinases, conserves all of the regulatory phosphorylation sites found in cdks, and has a slightly modified cyclin-binding PSTAIRE motif that is a hallmark of cdks. The Tetrahymena thermophila Cdk1p was also found to bind Saccharomyces cerevisiae p13suc1, a yeast cyclin.
The level of Cdk1p fluctuates over the vegetative cell cycle, correlating with its histone H1 kinase activity. Cdk1p is associated with the basal bodies of the ciliary rows of the cell cortex and the oral apparatus. This localization, along with the phenotype of a partial CDK1 knockout phenotype of bent and buckled ciliary rows, suggests that Cdk1p is involved in cortical morphogenesis.
Ref:16933976: Eisen JA, Coyne RS, Wu M, Wu D, Thiagarajan M, Wortman JR, Badger JH, Ren Q, Amedeo P, Jones KM, Tallon LJ, Delcher AL, Salzberg SL, Silva JC, Haas BJ, Majoros WH, Farzad M, Carlton JM, Smith RK, Garg J, Pearlman RE, Karrer KM, Sun L, Manning G, Elde NC, Turkewitz AP, Asai DJ, Wilkes DE, Wang Y, Cai H, Collins K, Stewart BA, Lee SR, Wilamowska K, Weinberg Z, Ruzzo WL, Wloga D, Gaertig J, Frankel J, Tsao CC, Gorovsky MA, Keeling PJ, Waller RF, Patron NJ, Cherry JM, Stover NA,
Ref:12045216: Doree M and Hunt T (2002) From Cdc2 to Cdk1: when did the cell cycle kinase join its cyclin partner? J Cell Sci 115(Pt 12):2461-4
Ref:12183062: Zhang H, Huang X, Tang L, Zhang QJ, Frankel J, Berger JD (2002) A cyclin-dependent protein kinase homologue associated with the basal body domains in the ciliate Tetrahymena thermophila. Biochimica et biophysica acta 1591(1-3):119-128
Ref:10329641: Mizzen CA, Dou Y, Liu Y, Cook RG, Gorovsky MA, Allis CD (1999) Identification and mutation of phosphorylation sites in a linker histone. Phosphorylation of macronuclear H1 is not essential for viability in tetrahymena. The Journal of biological chemistry 274(21):14533-6
Ref:8995382: Sweet MT, Carlson G, Cook RG, Nelson D, Allis CD (1997) Phosphorylation of linker histones by a protein kinase A-like activity in mitotic nuclei. The Journal of biological chemistry 272(2):916-23
Ref:9442875: Morgan DO (1997) Cyclin-dependent kinases: engines, clocks, and microprocessors. Annu Rev Cell Dev Biol 13:261-91
Ref:7958616: Doree M and Galas S (1994) The cyclin-dependent protein kinases and the control of cell division. FASEB J 8(14):1114-21
Ref:2065655: Roth SY, Collini MP, Draetta G, Beach D, Allis CD (1991) A cdc2-like kinase phosphorylates histone H1 in the amitotic macronucleus of Tetrahymena. The EMBO journal 10(8):2069-75
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