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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
Study provides evidence that downregulation of NUSAP1 can inhibit the proliferation, migration, and invasion of IBC cells by regulating CDK1 and DLGAP5 expression and enhances the drug susceptibility to E-ADM.
Cyclin-dependent kinase 1 (CDK1) and CDK2 have opposing roles in regulating interactions of splicing factor 3B1 with chromatin
Our results indicate that MCM7 may exert certain functions on spindle formation to prevent cytokinesis during early mitosis by regulating CDK1 activity.
Results demonstrated that CDK1 was increased in human breast cancer and promotes cell proliferation and cell cycle in breast cancer cell lines.
The expression levels of RNASEH2A, CDK1, and CD151 and their combination could predict the survival of renal cell carcinoma 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-181a was down-regulated in NSCLC and miR-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-490-3p DLEU1 may influence the expression of CDK1, CCND1 and SMARCD1 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-CDC25C and P53-P21WAF1 signaling pathway.
CDK1-mediated mitotic phosphorylation of PDZ-binding kinase is involved in cytokinesis and inhibits its oncogenic activity.
DNM2 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.
With tissue microarrays of hepatocellular carcinoma (HCC) patients, we determined the prognostic values of the core genes in the network and found that RAD21, CDK1, and HDAC2 expression levels were negatively associated with overall survival for HCC patients. The multivariate Cox regression analyses suggested that CDK1 was an independent prognostic factor, which was validated in an independent case cohort.
this study shows that CDK1 is a prognostic biomarker for lung adenocarcinoma
cytoplasmic Cdk1 expression is elevated in ovarian cancer and predicts a poor overall survival
findings demonstrate the involvement of consensus Cdk1 phosphorylation sites on Mis18 complex assembly and thus provide a rationale for cell cycle-regulated timing of Mis18 assembly and CENP-A deposition
S130 of p21 is phosphorylated by Cdk1/cyclin B1 during mitosis, which reduces p21's stability and binding affinity to Cdk1/cyclin B1
CDK9, in addition to CDK1, has roles in mediating the growth inhibitory effect of dinaciclib on cyclin B1 in triple negative breast cancer
inactivation induces anaphase and simultaneously triggers cytoplasmic formin-mediated F-actin polymerisation that propels the spindle into the cortex causing it to protrude while anaphase progresses
Results provide evidence that cdc2/cyclin B1 kinase activation was synchronous with the initial appearance of cytoskeletal lesions in mouse with Niemann-Pick disease type C.
CDK1, Aurora-B, and Rho-kinase phosphorylate keratin 5/14.
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).
our results show that the phosphorylation of 4E-BP1 promotes translation at the onset of meiosis to support the spindle assembly and suggest an important role of CDK1 and mTOR 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 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 phosphorylation is required for efficient separation of desmin-IFs and generally detected in muscular mitotic cells in vivo.
using in vitro dephosphorylation assays, we demonstrate that Mastl promotes persistent MPS1 phosphorylation by inhibiting PP2A/B55-mediated MPS1 dephosphorylation rather than affecting Cdk1 kinase activity. Our findings establish a key regulatory function of the Greatwall kinase/Mastl - PP2A/B55 pathway in preventing premature SAC silencing
oxidative stress-induced DNA damage of mouse zygotes triggers the cell cycle checkpoint, which results in G2/M cell cycle arrest, and that phospho-Cdc25B (Ser323), phospho-Cdc25C (Ser216), and phospho-Cdc2 (Tyr15) participate in activating the G2/M checkpoint.
CDK1 is required upstream of a checkpoint-associated cell death as well as meiotic metaphase progression in mouse spermatocytes.
CDK1 is a synthetic lethal target for KRAS mutant tumors.
Our data demonstrate that ES cells are uniquely sensitive to CDK1 inhibition via a p53/NOXA/MCL1 pathway.
Ubiquitin-dependent degradation of GATA 2 is promoted by Fbw7, is cyclin B-CDK1-mediated Thr176 phosphorylation-dependent, and influences hematopoietic cell differentiation.
HDAC3 controls G2/M phase progression mainly through posttranslational stabilization of the G2/M cyclin-dependent kinase 1.
Our findings reveal the following novel molecular mechanisms controlling mitochondrial fission during A/R injury of cardiomyocytes resulted from both increased activation Drp1 through Cdk1, PKCdelta, and calcineurin-mediated pathways, respectively
CDK1 activation proceeds with concomitant inhibition by CDC6, which tunes the timing of the M-phase entry during the embryonic cell cycle
FlnB loss reduced Cdk1 phosphorylation (an inhibitor of G2/M phase progression) and Cdk1 inhibition in chondrocytes mimicked the null FlnB, premature differentiation phenotype, through a beta1-integrin receptor- Pi3k/Akt mediated pathway.
CDK1-dependent phosphorylations required for the initiation of nuclear membrane disassembly during mitosis are adapted for removal of nuclei during fiber cell differentiation.
intestinal clock controls the expression of key cell cycle regulators, such as cdc2, wee1, p21, PCNA and cdk2, but only weakly influences cyclin B1, cyclin B2 and cyclin E1 expression.
Oligosaccharides of hyaluronan induce angiogenesis through distinct CD44 and RHAMM-mediated signalling pathways involving Cdc2 and gamma-adducin.
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 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 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.
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, but also causes persistent inhibitory phosphorylation of tyr-15-cyclin-dependent kinase 1.
Greatwall kinase and cyclin B-Cdk1 are both critical constituents of M-phase-promoting factor.
By promoting CtIP-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.
Results suggest that the specific synthesis of either B-type cyclins or c-Mos, induced by progesterone, is required to induce meiotic maturation and Cdc2 activation.
Cyclin B dissociation from CDK1 precedes cyclins B degradation upon CDK1 inactivation in mitotic embryo extracts and that proteasome proteolytic activity is dispensable for both activation and inactivation of CDK1 in such extracts.
Cdk1/cyclin B has a role in regulating B-raf activation at mitosis
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 kinase activity.
Cdk1 waves are not controlled by the mitotic switch but by a double-negative feedback between Cdk1 and Chk1. 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 localization at mitotic entry and exit are directly regulated by the antagonistic cyclin B-Cdk1 and PP2A-Tws enzymes
Cdk1 mediates the role of TARA and CycA in sleep regulation.
Y15 phosphorylation can both inhibit Cdk1 catalytic activity and de-stabilize Cdk1/Cyclin 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 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.
Data show that down-regulation of Cdc2 delayed pI mitosis and altered the polarity and the number of subsequent cell divisions.
Data suggest that Cks30A interacts with Cdk1, and may regulate Cyclin A levels through the activity of a female germline-specific anaphase-promoting complex, CDC20-Cortex.
Our findings suggest a model where mitotic disassembly/reassembly of the NPCs is regulated by a dynamic equilibrium of Cdk1 and OA-sensitive phosphatase activities and provide evidence that mitotic phosphorylation mediates disassembly of the NPC.
These results show that the two potential Cdk1 phosphorylation sites on Drosophila Cdc27 are required for its chromosomal localisation during mitosis and imply that these localisations specific to Cdc27 are crucial for APC/C functions.
Based on the results obtained, it was presupposed that distribution of annulate lamellae containing cytoplasmic pores could reflect the inactivation of the mitotic kinase cdk1 in Drosophila syncytial embryos.
CDK7 and CCNH activate CDC2 by T161 phosphorylation and make up CDK-activating kinase, which is required for normal meiotic progression during porcine oocyte maturation.
Results describe the expression of maternal cyclin B1 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, 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 (eIF4A)eIF4A1 and eIF4A2 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 promoter perturbs post-embryonic development. Inhibition of CDK activity at the shoot apex 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]
The Arabidopsis thaliana Cdc2(+)/Cdc28 homolog CDKA;1 is also phosphorylated in the T-loop and that phosphorylation at the conserved Thr-161 residue is essential for its function.
phosphorylation of T161 in Arabidopsis CDKA;1 is essential for cell division during male gametogenesis
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-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-2.1/2/CDK-1 antagonize CUL-2 activity to promote stabilization of PAR-6 levels during polarization of the early C. elegans embryo.
CDK-1 activates PLK-1 via SPAT-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-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 box-containing protein, drives synapse removal in this process.
NPP-16 and CDK-1 function to arrest prophase blastomeres in C. elegans embryos
Co-depletion studies of CDK-1 and WEE-1.3 demonstrate that WEE-1.3 is dispensable in the absence of CDK-1, suggesting that CDK-1 is a major target of WEE-1.3 in C. elegans oocytes.
MBK-2 is activated during oocyte maturation by CDK-1-dependent phosphorylation of serine 68, a residue outside of the kinase domain required for full activity in vivo.
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