scholarly journals Higher order genomic organization and regulatory compartmentalization for cell cycle control at the G1/S-phase transition

2018 ◽  
Vol 233 (10) ◽  
pp. 6406-6413 ◽  
Author(s):  
Prachi N. Ghule ◽  
David J. Seward ◽  
Andrew J. Fritz ◽  
Joseph R. Boyd ◽  
Andre J. van Wijnen ◽  
...  
Keyword(s):  
Phase Transition ◽  
Cell Cycle ◽  
Genomic Organization ◽  
Cell Cycle Control ◽  
Higher Order ◽  
S Phase

Cell Cycle Control of Transcription at the G1/S Phase Transition

2003 ◽  
pp. 31-48
Author(s):  
André J. van Wijnen ◽  
Gary S. Stein ◽  
Janet L. Stein ◽  
Jane B. Lian
Keyword(s):  
Phase Transition ◽  
Cell Cycle ◽  
Cell Cycle Control ◽  
S Phase

scholarly journals c-Rel arrests the proliferation of HeLa cells and affects critical regulators of the G1/S-phase transition.

1997 ◽  
Vol 17 (11) ◽  
pp. 6526-6536 ◽  
Author(s):  
J Bash ◽  
W X Zong ◽  
C Gélinas
Keyword(s):  
Phase Transition ◽  
Cell Cycle ◽  
Hela Cells ◽  
P53 Protein ◽  
Cell Cycle Control ◽  
S Phase ◽  
Cell Cycle Regulators ◽  
Transactivation Domains ◽  
Steady State Levels

A tetracycline-regulated system was used to characterize the effects of c-Rel on cell proliferation. The expression of c-Rel in HeLa cells led to growth arrest at the G1/S-phase transition, which correlated with its nuclear localization and the induction of endogenous IkappaB alpha expression. These changes were accompanied by a decrease in E2F DNA binding and the accumulation of the hypophosphorylated form of Rb. In vitro kinase assays showed a reduction in Cdk2 kinase activity that correlated with elevated levels of p21WAF1 Cdk inhibitor and p53 tumor suppressor protein. While the steady-state levels of WAF1 transcripts were increased, pulse-chase analysis revealed a sharp increase in p53 protein stability. Importantly, the deletion of the C-terminal transactivation domains of c-Rel abolished these effects. Together, these studies demonstrate that c-Rel can affect cell cycle control and suggest the involvement of the p21WAF1 and p53 cell cycle regulators.

The Schizosaccharomyces pombe hus5 gene encodes a ubiquitin conjugating enzyme required for normal mitosis

1995 ◽  
Vol 108 (2) ◽  
pp. 475-486 ◽  
Author(s):  
F. al-Khodairy ◽  
T. Enoch ◽  
I.M. Hagan ◽  
A.M. Carr
Keyword(s):  
Cell Cycle ◽  
Dna Synthesis ◽  
Schizosaccharomyces Pombe ◽  
Cell Cycle Control ◽  
S Phase ◽  
Temperature Sensitive ◽  
Checkpoint Control ◽  
Ubiquitin Conjugating Enzyme ◽  
Efficient Recovery ◽  
Mediate Cell

Normal eukaryotic cells do not enter mitosis unless DNA is fully replicated and repaired. Controls called ‘checkpoints’, mediate cell cycle arrest in response to unreplicated or damaged DNA. Two independent Schizosaccharomyces pombe mutant screens, both of which aimed to isolate new elements involved in checkpoint controls, have identified alleles of the hus5+ gene that are abnormally sensitive to both inhibitors of DNA synthesis and to ionizing radiation. We have cloned and sequenced the hus5+ gene. It is a novel member of the E2 family of ubiquitin conjugating enzymes (UBCs). To understand the role of hus5+ in cell cycle control we have characterized the phenotypes of the hus5 mutants and the hus5 gene disruption. We find that, whilst the mutants are sensitive to inhibitors of DNA synthesis and to irradiation, this is not due to an inability to undergo mitotic arrest. Thus, the hus5+ gene product is not directly involved in checkpoint control. However, in common with a large class of previously characterized checkpoint genes, it is required for efficient recovery from DNA damage or S-phase arrest and manifests a rapid death phenotype in combination with a temperature sensitive S phase and late S/G2 phase cdc mutants. In addition, hus5 deletion mutants are severely impaired in growth and exhibit high levels of abortive mitoses, suggesting a role for hus5+ in chromosome segregation. We conclude that this novel UBC enzyme plays multiple roles and is virtually essential for cell proliferation.

Yeast L double-stranded ribonucleic acid is synthesized during the G1 phase but not the S phase of the cell cycle

1981 ◽  
Vol 1 (8) ◽  
pp. 673-679
Author(s):  
V A Zakian ◽  
D W Wagner ◽  
W L Fangman
Keyword(s):  
Cell Cycle ◽  
Deoxyribonucleic Acid ◽  
Cell Cycle Control ◽  
S Phase ◽  
G1 Phase ◽  
Restrictive Temperature ◽  
Permissive Temperature ◽  
Phase Synthesis ◽  
Ribonucleic Acids ◽  
Alpha Factor

The cytoplasm of Saccharomyces cerevisiae contains two major classes of protein-encapsulated double-stranded ribonucleic acids (dsRNA's), L and M. Replication of L and M dsRNA's was examined in cells arrested in the G1 phase by either alpha-factor, a yeast mating pheromone, or the restrictive temperature for a cell cycle mutant (cdc7). [3H]uracil was added during the arrest periods to cells prelabeled with [14C]uracil, and replication was monitored by determining the ratio of 3H/14C for purified dsRNA's. Like mitochondrial deoxyribonucleic acid, both L and M dsRNA's were synthesized in the G1 arrested cells. The replication of L dsRNA was also examined during the S phase, using cells synchronized in two different ways. Cells containing the cdc7 mutation, treated sequentially with alpha-factor and then the restrictive temperature, enter a synchronous S phase when transferred to permissive temperature. When cells entered the S phase, synthesis of L dsRNA ceased, and little or no synthesis was detected throughout the S phase. Synthesis of L dsRNA was also observed in G1 phase cells isolated from asynchronous cultures by velocity centrifugation. Again, synthesis ceased when cells entered the S phase. These results indicate that L dsRNA replication is under cell cycle control. The control differs from that of mitochondrial deoxyribonucleic acid, which replicates in all phases of the cell cycle, and from that of 2-micron DNA, a multiple-copy plasmid whose replication is confined to the S phase.

Glucose and glutamine metabolism control by APC and SCF during the G1-to-S phase transition of the cell cycle

2014 ◽  
Vol 70 (2) ◽  
pp. 569-581 ◽  
Author(s):  
Irving Omar Estévez-García ◽  
Verónica Cordoba-Gonzalez ◽  
Eleazar Lara-Padilla ◽  
Abel Fuentes-Toledo ◽  
Ramcés Falfán-Valencia ◽  
...  
Keyword(s):  
Phase Transition ◽  
Cell Cycle ◽  
S Phase ◽  
Glutamine Metabolism

An architectural perspective of cell-cycle control at the G1/S phase cell-cycle transition

2006 ◽  
Vol 209 (3) ◽  
pp. 706-710 ◽  
Author(s):  
Gary S. Stein ◽  
André J. van Wijnen ◽  
Janet L. Stein ◽  
Jane B. Lian ◽  
Martin Montecino ◽  
...  
Keyword(s):  
Cell Cycle ◽  
Cell Cycle Control ◽  
S Phase ◽  
Phase Cell ◽  
Cell Cycle Transition ◽  
Architectural Perspective

scholarly journals A-myb is expressed in bovine vascular smooth muscle cells during the late G1-to-S phase transition and cooperates with c-myc to mediate progression to S phase.

1997 ◽  
Vol 17 (5) ◽  
pp. 2448-2457 ◽  
Author(s):  
D J Marhamati ◽  
R E Bellas ◽  
M Arsura ◽  
K E Kypreos ◽  
G E Sonenshein
Keyword(s):  
Phase Transition ◽  
Cell Cycle ◽  
Smooth Muscle ◽  
Growth Factor ◽  
Smooth Muscle Cells ◽  
Muscle Cells ◽  
S Phase ◽  
Cdna Clones ◽  
Transactivation Domain ◽  
Rna Levels

The Myb family of transcription factors is defined by homology within the DNA binding domain and includes c-Myb, A-Myb, and B-Myb. The protein products of the myb genes all bind the Myb-binding site (MBS) [YG(A/G)C(A/C/G)GTT(G/A)]. A-myb has been found to display a limited pattern of expression. Here we report that bovine aortic smooth muscle cells (SMCs) express A-myb. Sequence analysis of isolated bovine A-myb cDNA clones spanning the entire coding region indicated extensive homology with the human gene, including the putative transactivation domain. Expression of A-myb was cell cycle dependent; levels of A-myb RNA increased in the late G1-to-S phase transition following serum stimulation of serum-deprived quiescent SMC cultures and peaked in S phase. Nuclear run-on analysis revealed that an increased rate of transcription can account for most of the increase in A-myb RNA levels. Treatment of SMC cultures with 5,6-dichlorobenzimidazole riboside, a selective inhibitor of RNA polymerase II, indicated an approximate 4-h half-life for A-myb mRNA during the S phase of the cell cycle. Expression of A-myb by SMCs was stimulated by basic fibroblast growth factor, in a cell density-dependent fashion. Cotransfection of a human A-myb expression vector activated a multimerized MBS element-driven reporter construct approximately 30-fold in SMCs. The activity of c-myb and c-myc promoters, which both contain multiple MBS elements, were similarly transactivated, approximately 30- and 50-fold, respectively, upon cotransfection with human A-myb. Lastly, A-myb RNA levels could be increased by a combination of phorbol ester plus insulin-like growth factor 1. To test the role of myb family members in progression through the cell cycle, we comicroinjected c-myc and myb expression vectors into serum-deprived quiescent SMCs. The combination of c-myc and either A-myb or c-myb but not B-myb synergistically led to entry into S phase, whereas microinjection of any vector alone had little effect on S phase entry. Thus, these results suggest that A-myb is a potent transactivator in bovine SMCs and that its expression induces progression into S phase of the cell cycle.

scholarly journals Ran1 functions to control the Cdc10/Sct1 complex through Puc1.

1997 ◽  
Vol 8 (6) ◽  
pp. 1117-1128 ◽  
Author(s):  
M Caligiuri ◽  
T Connolly ◽  
D Beach
Keyword(s):  
Phase Transition ◽  
Cell Cycle ◽  
Protein Kinase ◽  
Cell Fate ◽  
Biochemical Analysis ◽  
Control Cell ◽  
S Phase ◽  
Present Evidence ◽  
Phosphorylation State

We have undertaken a biochemical analysis of the regulation of the G1/S-phase transition and commitment to the cell cycle in the fission yeast Schizosaccharomyces pombe. The execution of Start requires the activity of the Cdc2 protein kinase and the Sct1/Cdc10 transcription complex. Progression through G1 also requires the Ran1 protein kinase whose inactivation leads to activation of the meiotic pathway under conditions normally inhibitory to this process. We have found that in addition to Cdc2, Sct1/Cdc10 complex formation requires Ran1. We demonstrate that the Puc1 cyclin associates with Ran1 and Cdc10 in vivo and that the Ran1 protein kinase functions to control the association between Puc1 and Cdc10. In addition, we present evidence that the phosphorylation state of Cdc10 is altered upon inactivation of Ran1. These results provide biochemical evidence that demonstrate one mechanism by which the Ran1 protein kinase serves to control cell fate through Cdc10 and Puc1.

Regulation of intracellular pH during the G1/S-phase transition of the neuroblastoma cell cycle

1988 ◽  
Vol 174 (2) ◽  
pp. 521-524 ◽  
Author(s):  
Johannes Boonstra ◽  
Leon G.J. Tertoolen ◽  
Christine L. Mummery ◽  
Siegfried W. de Laat
Keyword(s):  
Phase Transition ◽  
Cell Cycle ◽  
Intracellular Ph ◽  
Neuroblastoma Cell ◽  
S Phase

scholarly journals p27kip1 controls H-Ras/MAPK activation and cell cycle entry via modulation of MT stability

2015 ◽  
Vol 112 (45) ◽  
pp. 13916-13921 ◽  
Author(s):  
Linda Fabris ◽  
Stefania Berton ◽  
Ilenia Pellizzari ◽  
Ilenia Segatto ◽  
Sara D’Andrea ◽  
...  
Keyword(s):  
Phase Transition ◽  
Cell Cycle ◽  
Signaling Pathway ◽  
Mapk Pathway ◽  
Mapk Signaling ◽  
S Phase ◽  
Point Of View ◽  
Cell Cycle Entry ◽  
Pathway Activation ◽  
Direct Binding

The cyclin-dependent kinase (CDK) inhibitor p27kip1 is a critical regulator of the G1/S-phase transition of the cell cycle and also regulates microtubule (MT) stability. This latter function is exerted by modulating the activity of stathmin, an MT-destabilizing protein, and by direct binding to MTs. We recently demonstrated that increased proliferation in p27kip1-null mice is reverted by concomitant deletion of stathmin in p27kip1/stathmin double-KO mice, suggesting that a CDK-independent function of p27kip1 contributes to the control of cell proliferation. Whether the regulation of MT stability by p27kip1 impinges on signaling pathway activation and contributes to the decision to enter the cell cycle is largely unknown. Here, we report that faster cell cycle entry of p27kip1-null cells was impaired by the concomitant deletion of stathmin. Using gene expression profiling coupled with bioinformatic analyses, we show that p27kip1 and stathmin conjunctly control activation of the MAPK pathway. From a molecular point of view, we observed that p27kip1, by controlling MT stability, impinges on H-Ras trafficking and ubiquitination levels, eventually restraining its full activation. Our study identifies a regulatory axis controlling the G1/S-phase transition, relying on the regulation of MT stability by p27kip1 and finely controlling the spatiotemporal activation of the Ras-MAPK signaling pathway.

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