Protein kinase C inhibits the CAK-CDK2 cyclin-dependent kinase cascade and G1/S cell cycle progression in human diploid fibroblasts.

@article{Hamada1996ProteinKC,
  title={Protein kinase C inhibits the CAK-CDK2 cyclin-dependent kinase cascade and G1/S cell cycle progression in human diploid fibroblasts.},
  author={Kyoko Hamada and Noriko Takuwa and W Zhou and Mamoru Kumada and You Takuwa},
  journal={Biochimica et biophysica acta},
  year={1996},
  volume={1310 1},
  pages={
          149-56
        },
  url={https://api.semanticscholar.org/CorpusID:37712372}
}

Lower cyclin H and cyclin-dependent kinase-activating kinase activity in cell cycle arrest induced by lack of adhesion to substratum.

This report shows that either UV irradiation on an adhesive substrate or culture on a nonadhesive substrate produced K1735 melanoma growth arrest, the first report showing that cyclin H-mediated down-regulation of cdk-activating kinase activity is involved in growth arrest induced by lack of anchorage.

Protein Kinase Cδ Inhibition of S-Phase Transition in Capillary Endothelial Cells Involves the Cyclin-dependent Kinase Inhibitor p27Kip1 *

A critical role is suggested for p27Kip1 in the PKCδ-mediated S-phase arrest of rat microvascular endothelial cells, suggesting a normal cell cycle progression.

Activation of protein kinase Calpha inhibits growth of pancreatic cancer cells via p21(cip)-mediated G(1) arrest.

ThePKCalpha-induced block in cell proliferation persisted even though cells were kept in the presence of growth factors, suggesting that induction of PKCalpha results in a permanent withdrawal of pancreatic cancer cells from the cell cycle.

Protein kinase C-mediated regulation of the cell cycle.

Accumulating data indicate that a major target for PKC-mediated inhibition of cell cycle progression is the Cip/Kip cyclin-dependent kinase (cdk) inhibitor p21waf1/cip1.

PKCη enhances cell cycle progression, the expression of G1 cyclins and p21 in MCF-7 cells

The expression of PKCη in MCF-7 cells, under the control of a tetracycline-responsive inducible promoter, enhanced cell growth and affected the cell cycle at several points.

Adhesion to Substratum Kinase Activity in Cell Cycle Arrest Induced by Lack of Lower Cyclin H and Cyclin-dependent Kinase-activating

This report shows that either UV irradiation on an adhesive substrate or culture on a nonadhesive substrate produced K1735 melanoma growth arrest, the first report showing that cyclin H-mediated down-regulation of cdkactivating kinase activity is involved in growth arrest induced by lack of anchorage.

Involvement of p21 in Protein Kinase C Alpha-Induced Cell Cycle Progression

It is demonstrated that PKC activation in glioma cells increased their progression through the cell cycle through the upregulation of p21, which facilitates active cyclin-CDK complex formation.

Involvement of p21Waf1/Cip1 in Protein Kinase C Alpha-Induced Cell Cycle Progression

The results suggest that PKC α activity controls glioma cell cycle progression through the upregulation of p21Waf1/Cip1, which facilitates active cyclin-CDK complex formation.

Ras activity late in G1 phase required for p27kip1 downregulation, passage through the restriction point, and entry into S phase in growth factor-stimulated NIH 3T3 fibroblasts

Ras plays temporally distinct, phase-specific roles throughout the G1 phase and that Ras function late in G1 is required for p27kip1 downregulation and passage through the restriction point, a prerequisite for entry into the S phase.

E2F1, B-myb and selective members of cyclin/cdk subunits are targets for protein kinase C-mediated bimodal growth regulation in vascular endothelial cells.

The results indicate that the PKC signal transduction pathway, depending on the timing of activation in the G1 phase, either positively or negatively regulates the message level of growth-regulating genes that are crucial for the G 1 to S phase progression.

Cell cycle regulation of CDK2 activity by phosphorylation of Thr160 and Tyr15.

The activity of a subpopulation of CDK2 molecules is inhibited at a time in the cell cycle when overallCDK2 activity is increased, and phosphorylation on the inhibitory sites T14 and Y15 is also maximal during S phase and G2.

Activation of cyclin-dependent kinase 4 (cdk4) by mouse MO15-associated kinase

It is demonstrated that the catalytic subunit of mouse cdc2/cdk2 CAK (a 39-kDa protein designated p39MO15) can assemble with a regulatory protein present in either insect or mammalian cells to generate a CAK activity capable of phosphorylating and enzymatically activating both cdk2 and cdk4 in complexes with their respective cyclin partners.

The cdk2 kinase is required for the G1-to-S transition in mammalian cells.

Results indicate that p33cdk2 is required for the G1-to-S phase transition in mammalian cells and show evidence to suggest that the cyclin E/p33CDk2 complex is likely to be required for entry into S phase.

Direct binding of cyclin D to the retinoblastoma gene product (pRb) and pRb phosphorylation by the cyclin D-dependent kinase CDK4.

The product (pRb) of the retinoblastoma gene (RB-1) prevents S-phase entry during the cell cycle, and inactivation of this growth-suppressive function is presumed to result from pRb

Cell cycle analysis of the activity, subcellular localization, and subunit composition of human CAK (CDK-activating kinase)

A molecular characterization of a human p40MO15 homologue and its associated CAK activity suggests that the phosphorylation state of threonine 161 in p34cdc2 (and the corresponding residue in other cdks) may be regulated primarily by the availability of the cdk/cyclin substrates, and by phosphatase(s).