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Human CDK1 Protein expressed in Wheat germ - ABIN1348775
Ovejero-Benito, Frade: Brain-derived neurotrophic factor-dependent cdk1 inhibition prevents G2/M progression in differentiating tetraploid neurons. in PLoS ONE 2013
The expression levels of RNASEH2A (show RNASEH2A Proteins), CDK1, and CD151 (show CD151 Proteins) and their combination could predict the survival of renal cell carcinoma (show MOK Proteins) patients.
A CDK1-dependent regulation of the WRN-DNA2-mediated resection and identify a new function of WRN as a DSB repair pathway switch are reported.
High CDK1 expression is associated with HIV-1 infection.
the miR (show MLXIP Proteins)-181a was down-regulated in NSCLC and miR (show MLXIP Proteins)-181a inhibited the cell proliferation by regulating CDK1 expression.
Thus, Cyclin A/Cdk1 phosphorylation primes MYPT1 for Plk1 binding. These data demonstrate cross-regulation between Cyclin A/Cdk1-dependent and Plk1-dependent phosphorylation of substrates during mitosis to ensure efficient correction of kinetochore microtubule attachment errors necessary for high mitotic fidelity.
It has been suggested that through interaction with miR (show MLXIP Proteins)-490-3p DLEU1 may influence the expression of CDK1, CCND1 (show CCND1 Proteins) and SMARCD1 (show SMARCD1 Proteins) protein, subsequently promoting the development and progression of ovarian carcinoma.
The present study suggested that abnormal activation of CDK1 was implicated in the proliferation and apoptosis regulation of ovarian cancer cells, which might due to the aberrant regulations of the upstream Chk1 (show CHEK1 Proteins)-CDC25C (show CDC25C Proteins) and P53 (show TP53 Proteins)-P21WAF1 signaling pathway.
CDK1-mediated mitotic phosphorylation of PDZ-binding kinase (show PBK Proteins) is involved in cytokinesis and inhibits its oncogenic activity.
DNM2 (show DNM2 Proteins) is a substrate for CDK1-dependent phosphorylation, which plays an important role in the regulation of human sperm acrosomal exocytosis.
These findings suggest that Cdc2 is positively associatd with the development of taxol resistance. The Cdc2 inhibitor, purvalanol A, enhanced the cytotoxic effects of taxol through Op18/stathmin (show STMN1 Proteins).
Results provide evidence that cdc2/cyclin B1 (show CCNB1 Proteins) kinase activation was synchronous with the initial appearance of cytoskeletal lesions in mouse with Niemann-Pick disease type C.
CDK1, Aurora-B (show AURKC Proteins), and Rho-kinase (show ROCK2 Proteins) phosphorylate keratin 5 (show KRT36 Proteins)/14.
the ability of oocytes to mature, as well as oocyte CDK1 levels, were dependent on follicle size, but CDK1 expression in oocytes from preantral follicles was not acutely altered by the activity of follicle stimulating hormone (FSH (show BRD2 Proteins)).
our results show that the phosphorylation of 4E-BP1 (show EIF4EBP1 Proteins) promotes translation at the onset of meiosis to support the spindle assembly and suggest an important role of CDK1 and mTOR (show FRAP1 Proteins) kinases in this process
Study shows that Cdk1 phosphorylates Ska3 to promote its direct binding to the Ndc80 complex (Ndc80C), a core outer kinetochore component, also show that this phosphorylation occurs specifically during mitosis and is required for the kinetochore localization of the Ska complex.
loss of LAR (show PTPRF Proteins) activity resulted in reduced activity of CDK1.
CDK1 is a positive regulator of the IFN signaling pathway. The overexpression of CDK1 might contribute to the abnormally amplified type I IFN signaling in systemic lupus erythematosus.
Cdk1-induced desmin (show DES Proteins) phosphorylation is required for efficient separation of desmin (show DES Proteins)-IFs and generally detected in muscular mitotic cells in vivo.
using in vitro dephosphorylation assays, we demonstrate that Mastl (show MASTL Proteins) promotes persistent MPS1 phosphorylation by inhibiting PP2A (show PPP2R2B Proteins)/B55 (show MINK1 Proteins)-mediated MPS1 dephosphorylation rather than affecting Cdk1 kinase activity. Our findings establish a key regulatory function of the Greatwall (show MASTL Proteins) kinase/Mastl (show MASTL Proteins) - PP2A (show PPP2R2B Proteins)/B55 (show MINK1 Proteins) pathway in preventing premature SAC (show ADCY10 Proteins) silencing
oxidative stress-induced (show SQSTM1 Proteins) DNA damage of mouse zygotes triggers the cell cycle checkpoint, which results in G2/M cell cycle arrest, and that phospho-Cdc25B (show CDC25B Proteins) (Ser323), phospho-Cdc25C (show CDC25C Proteins) (Ser216), and phospho-Cdc2 (Tyr15) participate in activating the G2/M checkpoint.
intestinal clock controls the expression of key cell cycle regulators, such as cdc2, wee1 (show WEE1 Proteins), p21 (show CDKN1A Proteins), PCNA (show PCNA Proteins) and cdk2 (show CDK2 Proteins), but only weakly influences cyclin B1 (show CCNB1 Proteins), cyclin B2 (show CCNB2 Proteins) and cyclin E1 (show CCNE1 Proteins) expression.
Oligosaccharides of hyaluronan induce angiogenesis through distinct CD44 (show CD44 Proteins) and RHAMM (show HMMR Proteins)-mediated signalling pathways involving Cdc2 and gamma-adducin (show ADD3 Proteins).
Here the authors show that CPEB4 activity is regulated by ERK2- and Cdk1-mediated hyperphosphorylation. These phosphorylation events additively activate CPEB4 in M-phase by maintaining it in its monomeric state.
the fine-tuning of Cdc6 (show CDC6 Proteins) accumulation is essential to ensure two meiotic waves of Cdk1 activation and to avoid unscheduled DNA replication during meiotic maturation.
equilibrium between CDK1 and PP2A (show PPP2R2B Proteins) specifies the timing of M-phase entry and exit and regulates the dynamics of cyclin B degradation upon M-phase exit in Xenopus laevis first embryonic mitosis.
CDK1 activation proceeds with concomitant inhibition by CDC6 (show CDC6 Proteins), which tunes the timing of the M-phase entry during the embryonic cell cycle
Xenopus Cdk1-AS rescues HT2-19 cells from apoptosis.
Ras suppresses cyclin-dependent kinase 1 in a complex manner: It induces continuous accumulation of cyclin B2 (show CCNB2 Proteins), but also causes persistent inhibitory phosphorylation of tyr (show TYR Proteins)-15-cyclin-dependent kinase 1.
Greatwall (show MASTL Proteins) kinase and cyclin B-Cdk1 are both critical constituents of M-phase-promoting factor.
By promoting CtIP (show RBBP8 Proteins)-dependent resection of double-strand break (DSB) ends while preventing Rad51 chromatin assembly, Cdk1 inhibits both the nonhomologous and homologous modes of DSB repair during mitosis.
Examination of H1 histones reveals isoform-specific regulation by Cdk1 and RanGTP; mitotic Cdk1 functions to enhance H1 binding in egg extracts and embryos
Cdc2 displays cytoskeleton-dependent localization in blastomere cortex during Xenopus embryonic cell cycle.
Physical interaction between p115 and Cdk1, suggests that p115 sequesters or re-localizes Cdk1 during mitosis to allow the complete activation of Cdk1 and consequently correct progression through mitosis in Drosophila imaginal cells.
Here the authors show that CDK1 phosphorylation of GNU negatively regulates PNG (show ETS2 Proteins) kinase activity.
Cdk1 waves are not controlled by the mitotic switch but by a double-negative feedback between Cdk1 and Chk1 (show CHEK1 Proteins). In Drosophila embryos, Cdk1 positive feedback serves primarily to ensure the rapid onset of mitosis, while wave propagation is regulated by S phase events.
Cdk1 phosphorylates the conserved centriole protein Sas-4 during mitosis. This creates a Polo-docking site that helps recruit Polo to daughter centrioles.
Our results indicate that the cyclic changes in Gwl (show MASTL Proteins) localization at mitotic entry and exit are directly regulated by the antagonistic cyclin B-Cdk1 and PP2A (show PPP2R2B Proteins)-Tws enzymes
Cdk1 mediates the role of TARA and CycA (show CCNA2 Proteins) in sleep regulation.
Y15 phosphorylation can both inhibit Cdk1 catalytic activity and de-stabilize Cdk1/Cyclin (show PCNA Proteins) complexes, whereas T161 phosphorylation facilitates stable interactions between cyclin B and Cdk1.
Phosphorylation of Cdk1 on Y15 appeared to be crucial for developmental and DNA damage-induced G2-phase checkpoint arrest, consistent with other evidence that Myt1 (show MYT1 Proteins) is the major Y15-directed Cdk1 inhibitory kinase at this stage of development.
nonmuscle myosin II regulation by Cdc2 activity
CDK1 activation may be the cell cycle regulated event that determines the timing of emi1 destruction.
CDK7 (show CDK7 Proteins) and CCNH (show CCNH Proteins) activate CDC2 by T161 phosphorylation and make up CDK-activating kinase (show CDK7 Proteins), which is required for normal meiotic progression during porcine oocyte maturation.
Results describe the expression of maternal cyclin B1 (show CCNB1 Proteins) and Cdc2 during in vitro maturation of porcine oocytes.
Data demonstrate the presence of a novel structure in the cortex of porcine oocytes that comprises ERES and transiently accumulates CDC2 prior to germinal vesicle breakdown.
insufficient amount of Cdc2 and continuous activation of Wee1 B are the cause of meiotic failure of small oocytes in pigs
These results suggest that the inhibitory phosphorylation of CDC2, which is catalyzed by pigWee1B (show WEE2 Proteins), but not pigMyt1, is involved in the meiotic arrest of porcine oocytes.
Data show that phosphatidylcholine (PC) biosynthesis is repressed by disruption of the core cell cycle regulator CYCLIN-DEPENDENT KINASE A;1 (CDKA;1) and that this repression is reliant on PHOSPHATIDIC ACID PHOSPHOHYDROLASE (PAH).
Cyclin-dependent kinase A (CDKA) phosphorylates eukaryotic initiation factor 4A (show DDX39 Proteins) (eIF4A)eIF4A1 (show EIF4A1 Proteins) and eIF4A2 (show EIF4A2 Proteins) on a conserved threonine residue (threonine-164) within the RNA-binding motif.
CDKA;1 and CYCD3;2 are required for the terminal division in the stomatal lineage.
Data indicate that the in vivo confirmation of substrates of CDKA;1 showing a direct link between cell proliferation and the control of the redox state.
The crucial function of CDKA;1 is the control of the plant Retinoblastoma homolog RBR1 and codepletion of RBR1 and CDKA;1 rescued most defects of cdka;1 mutants.
Expression of a dominant negative CDKA;1 allele under the control of the STM (show SHMT1 Proteins) promoter perturbs post-embryonic development. Inhibition of CDK (show CDK4 Proteins) activity at the shoot apex (show APEX1 Proteins) results in premature differentiation of shoot apical meristem cells.
When a single cdka;1 sperm was delivered, either female gamete could be fertilized leading to similar proportions of seeds containing either a single endosperm or a single embryo.
However, we show here that the DNA damage checkpoint in Arabidopsis can also operate independently of the phosphorylation of CDKA;1.
CDC2A participates in the fertilization process of endosperm
The balance between cell division and differentiation is regulated through the interaction between CDKA;1 and the antiphosphatase PAS2. [CDKA;1]
These results reveal a crucial and conserved role of phosphorylation of the N terminus of Bora for Plk1 activation and mitotic entry.
CDK-1 regulates PLK-1 activity during mitosis in C. elegans embryos through multisite phosphorylation of the PLK-1 activator SPAT (show AGXT Proteins)-1
Conversion of microtubule-organizing center state involves the conserved C. elegans centrosome protein SPD-2/CEP192 and cell-cycle-dependent kinase activity from the mitotic cell.
Our results support a model in which CYB (show CSTB Proteins)-2.1/2/CDK-1 antagonize CUL-2 (show CUL2 Proteins) activity to promote stabilization of PAR-6 (show PARD6A Proteins) levels during polarization of the early C. elegans embryo.
CDK-1 activates PLK-1 via SPAT (show AGXT Proteins)-1 phosphorylation to promote entry into mitosis.
model in which Wnt signaling and CDK-1 modify WRM-1 in a temporal and spatial manner to unmask an intrinsic polarity cue required for proper orientation of the endomesoderm cell division axis
results indicate that CDC-25.1 is required for maintaining proper rate of germline mitotic cell cycle; propose that CDC-25.1 regulates the rate of germline mitotic cell cycle by counteracting WEE (show WEE1 Proteins)-1.3 and by positively controlling CDK-1
CDK-1 blocks rotation by inhibiting dynein association with microtubules.
Use of loss- and gain-of-function genetic approaches demonstrates that CYY-1, a cyclin (show PCNA Proteins) box-containing protein, drives synapse removal in this process.
NPP-16 and CDK-1 function to arrest prophase blastomeres in C. elegans embryos
The protein encoded by this gene is a member of the Ser/Thr protein kinase family. This protein is a catalytic subunit of the highly conserved protein kinase complex known as M-phase promoting factor (MPF), which is essential for G1/S and G2/M phase transitions of eukaryotic cell cycle. Mitotic cyclins stably associate with this protein and function as regulatory subunits. The kinase activity of this protein is controlled by cyclin accumulation and destruction through the cell cycle. The phosphorylation and dephosphorylation of this protein also play important regulatory roles in cell cycle control. Alternatively spliced transcript variants encoding different isoforms have been found for this gene.
cell cycle controller CDC2
, cell division control protein 2 homolog
, cell division cycle 2, G1 to S and G2 to M
, cell division protein kinase 1
, p34 protein kinase
, cyclin-dependent kinase 1
, cell cycle p34 CDC2 kinase protein
, cell division cycle 2 homolog A
, cell division cycle control protein 2a
, Cell division cycle control protein 2
, cell division cycle 2
, Cell division control protein 2 homolog 1
, cell division control protein 2-A
, cell division cycle 2 like
, cell division protein kinase 1-A
, cyclin-dependent kinase 1-A
, p34 protein kinase 1
, cdc2 kinase
, cyclin dependent kinase
, cyclin-dependent kinase
, cell division cycle 2 protein
, protein cdc2 kinase
, putative cyclin-dependent kinase A family protein
, cell division control protein 2 homolog 2
, cell division control protein 2-B
, cell division protein kinase 1-B
, cyclin-dependent kinase 1-B
, p34 protein kinase 2
, DNA polymerase delta
, DNA-directed DNA polymerase delta 1
, polymerase (DNA directed), delta 1, catalytic subunit 125kDa
, Cell division control protein 2 homolog
, Cell division protein kinase 1
, Cell division control protein 2