Cell cycle control

2016 ◽  
pp. 31-41
Author(s):  
Simon M. Carr ◽  
Nicholas B. La Thangue
Keyword(s):  
Cell Cycle ◽  
Final Stage ◽  
Cell Cycle Progression ◽  
Cell Cycle Control ◽  
Control Mechanisms ◽  
Chromosomal Dna ◽  
Cycle Progression ◽  
M Phase ◽  
Cellular Components ◽  
Regulate Cell Cycle Progression

All cells arise by the division of existing cells in a highly regulated series of events known as the cell cycle. Whilst duplication of other cellular contents occurs throughout all stages of the cycle, chromosomal DNA is replicated only once at a stage known as S phase. Once this is complete, distribution of chromosomes and other cellular components occurs during the final stage of the cell cycle, known as M phase, or mitosis. The cell cycle is therefore regulated in a temporal fashion, so that entry into subsequent cell cycle stages only occurs once the previous stage has been completed. A number of signalling mechanisms monitor the integrity of cell cycle progression, and later cell cycle stages can be delayed if any errors need correction. This chapter gives an overview of the major control mechanisms that regulate cell cycle progression, and how these are circumvented during the onset of cancer.

scholarly journals Cyclin C influences the timing of mitosis in fission yeast

2017 ◽  
Vol 28 (13) ◽  
pp. 1738-1744 ◽  
Author(s):  
Gabor Banyai ◽  
Zsolt Szilagyi ◽  
Vera Baraznenok ◽  
Olga Khorosjutina ◽  
Claes M. Gustafsson
Keyword(s):  
Cell Cycle ◽  
Fission Yeast ◽  
Rna Polymerase Ii ◽  
Cell Cycle Progression ◽  
Cell Cycle Control ◽  
Mediator Complex ◽  
Cycle Progression ◽  
Cyclin C ◽  
M Phase

The multiprotein Mediator complex is required for the regulated transcription of nearly all RNA polymerase II–dependent genes. Mediator contains the Cdk8 regulatory subcomplex, which directs periodic transcription and influences cell cycle progression in fission yeast. Here we investigate the role of CycC, the cognate cyclin partner of Cdk8, in cell cycle control. Previous reports suggested that CycC interacts with other cellular Cdks, but a fusion of CycC to Cdk8 reported here did not cause any obvious cell cycle phenotypes. We find that Cdk8 and CycC interactions are stabilized within the Mediator complex and the activity of Cdk8-CycC is regulated by other Mediator components. Analysis of a mutant yeast strain reveals that CycC, together with Cdk8, primarily affects M-phase progression but mutations that release Cdk8 from CycC control also affect timing of entry into S phase.

scholarly journals Varicella-Zoster Virus ORF12 Protein Activates the Phosphatidylinositol 3-Kinase/Akt Pathway To Regulate Cell Cycle Progression

2012 ◽  
Vol 87 (3) ◽  
pp. 1842-1848 ◽  
Author(s):  
XueQiao Liu ◽  
Jeffrey I. Cohen
Keyword(s):  
Cell Cycle ◽  
Deletion Mutant ◽  
Cell Cycle Progression ◽  
Phase Cell ◽  
Akt Pathway ◽  
Wild Type ◽  
Cycle Progression ◽  
Varicella Zoster ◽  
M Phase ◽  
Regulate Cell Cycle Progression

ABSTRACTVaricella-zoster virus (VZV) activates the phosphatidylinositol 3-kinase (PI3K)/Akt pathway and alters cell cycle progression, but the viral protein(s) responsible for these activities is unknown. We previously reported that the VZV open reading frame 12 (ORF12) protein triggers phosphorylation of ERK. Here, we demonstrate that the VZV ORF12 protein also activates the PI3K/Akt pathway to regulate cell cycle progression. Transfection of cells with a plasmid expressing the ORF12 protein induced phosphorylation of Akt, which was dependent on PI3K. Infection of cells with wild-type VZV triggered phosphorylation of Akt, while infection with an ORF12 deletion mutant induced less phosphorylated Akt. The activation of Akt by ORF12 protein was associated with its binding to the p85 subunit of PI3K. Infection of cells with wild-type VZV resulted in increased levels of cyclin B1, cyclin D3, and phosphorylated glycogen synthase kinase 3β (GSK-3β), while infection with the ORF12 deletion mutant induced lower levels of these proteins. Wild-type VZV infection reduced the G1phase cell population and increased the M phase cell population, while infection with the ORF12 deletion mutant had a reduced effect on the G1and M phase populations. Inhibition of Akt activity with LY294002 reduced the G1and M phase differences observed in cells infected with wild-type and ORF12 mutant viruses. In conclusion, we have found that the VZV ORF12 protein activates the PI3K/Akt pathway to regulate cell cycle progression. Since VZV replicates in both dividing (e.g., keratinocytes) and nondividing (neurons) cells, the ability of the VZV ORF12 protein to regulate the cell cycle is likely important for VZV replication in various cell types in the body.

scholarly journals Potassium channels in cell cycle and cell proliferation

2014 ◽  
Vol 369 (1638) ◽  
pp. 20130094 ◽  
Author(s):  
Diana Urrego ◽  
Adam P. Tomczak ◽  
Farrah Zahed ◽  
Walter Stühmer ◽  
Luis A. Pardo
Keyword(s):  
Cell Cycle ◽  
Cell Proliferation ◽  
Potassium Channels ◽  
Normal Cell ◽  
Cell Cycle Progression ◽  
Cell Cycle Control ◽  
Control Mechanisms ◽  
Cycle Progression ◽  
Uncontrolled Cell Proliferation ◽  
Normal Cell Cycle

Normal cell-cycle progression is a crucial task for every multicellular organism, as it determines body size and shape, tissue renewal and senescence, and is also crucial for reproduction. On the other hand, dysregulation of the cell-cycle progression leading to uncontrolled cell proliferation is the hallmark of cancer. Therefore, it is not surprising that it is a tightly regulated process, with multifaceted and very complex control mechanisms. It is now well established that one of those mechanisms relies on ion channels, and in many cases specifically on potassium channels. Here, we summarize the possible mechanisms underlying the importance of potassium channels in cell-cycle control and briefly review some of the identified channels that illustrate the multiple ways in which this group of proteins can influence cell proliferation and modulate cell-cycle progression.

scholarly journals The Morphogenesis Checkpoint in Saccharomyces cerevisiae: Cell Cycle Control of Swe1p Degradation by Hsl1p and Hsl7p

1999 ◽  
Vol 19 (10) ◽  
pp. 6929-6939 ◽  
Author(s):  
John N. McMillan ◽  
Mark S. Longtine ◽  
Rey A. L. Sia ◽  
Chandra L. Theesfeld ◽  
Elaine S. G. Bardes ◽  
...  
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Cell Cycle ◽  
Cell Cycle Progression ◽  
Cell Cycle Control ◽  
Negative Regulators ◽  
Cycle Progression ◽  
Bud Formation ◽  
M Phase ◽  
Subsequent Degradation ◽  
Morphogenesis Checkpoint

ABSTRACT In Saccharomyces cerevisiae, the Wee1 family kinase Swe1p is normally stable during G1 and S phases but is unstable during G2 and M phases due to ubiquitination and subsequent degradation. However, perturbations of the actin cytoskeleton lead to a stabilization and accumulation of Swe1p. This response constitutes part of a morphogenesis checkpoint that couples cell cycle progression to proper bud formation, but the basis for the regulation of Swe1p degradation by the morphogenesis checkpoint remains unknown. Previous studies have identified a protein kinase, Hsl1p, and a phylogenetically conserved protein of unknown function, Hsl7p, as putative negative regulators of Swe1p. We report here that Hsl1p and Hsl7p act in concert to target Swe1p for degradation. Both proteins are required for Swe1p degradation during the unperturbed cell cycle, and excess Hsl1p accelerates Swe1p degradation in the G2-M phase. Hsl1p accumulates periodically during the cell cycle and promotes the periodic phosphorylation of Hsl7p. Hsl7p can be detected in a complex with Swe1p in cell lysates, and the overexpression of Hsl7p or Hsl1p produces an effective override of the G2arrest imposed by the morphogenesis checkpoint. These findings suggest that Hsl1p and Hsl7p interact directly with Swe1p to promote its recognition by the ubiquitination complex, leading ultimately to its destruction.

scholarly journals Cdk1-Mediated Phosphorylation of Human ATF7 at Thr-51 and Thr-53 Promotes Cell-Cycle Progression into M Phase

PLoS ONE ◽  
2014 ◽  
Vol 9 (12) ◽  
pp. e116048 ◽  
Author(s):  
Hitomi Hasegawa ◽  
Kenichi Ishibashi ◽  
Shoichi Kubota ◽  
Chihiro Yamaguchi ◽  
Ryuzaburo Yuki ◽  
...  
Keyword(s):  
Cell Cycle ◽  
Cell Cycle Progression ◽  
Cycle Progression ◽  
M Phase

scholarly journals Regulation of Cell Cycle Progression by Growth Factor-Induced Cell Signaling

Cells ◽  
2021 ◽  
Vol 10 (12) ◽  
pp. 3327
Author(s):  
Zhixiang Wang
Keyword(s):  
Cell Cycle ◽  
Growth Factor ◽  
Signaling Pathways ◽  
Tyrosine Kinases ◽  
Cell Cycle Progression ◽  
Phase Cell ◽  
Growth Factor Signaling ◽  
Cycle Progression ◽  
M Phase

The cell cycle is the series of events that take place in a cell, which drives it to divide and produce two new daughter cells. The typical cell cycle in eukaryotes is composed of the following phases: G1, S, G2, and M phase. Cell cycle progression is mediated by cyclin-dependent kinases (Cdks) and their regulatory cyclin subunits. However, the driving force of cell cycle progression is growth factor-initiated signaling pathways that control the activity of various Cdk–cyclin complexes. While the mechanism underlying the role of growth factor signaling in G1 phase of cell cycle progression has been largely revealed due to early extensive research, little is known regarding the function and mechanism of growth factor signaling in regulating other phases of the cell cycle, including S, G2, and M phase. In this review, we briefly discuss the process of cell cycle progression through various phases, and we focus on the role of signaling pathways activated by growth factors and their receptor (mostly receptor tyrosine kinases) in regulating cell cycle progression through various phases.

scholarly journals Akt/Protein Kinase B-Dependent Phosphorylation and Inactivation of WEE1Hu Promote Cell Cycle Progression at G2/M Transition

2005 ◽  
Vol 25 (13) ◽  
pp. 5725-5737 ◽  
Author(s):  
Kazuhiro Katayama ◽  
Naoya Fujita ◽  
Takashi Tsuruo
Keyword(s):  
Cell Cycle ◽  
Cell Cycle Progression ◽  
Kinase Inhibitor ◽  
Phosphorylation Site ◽  
Cytoplasmic Localization ◽  
M Cell ◽  
Serine Threonine Kinase ◽  
Cycle Progression ◽  
M Phase ◽  
Promote Cell Cycle Progression

ABSTRACT The serine/threonine kinase Akt is known to promote cell growth by regulating the cell cycle in G1 phase through activation of cyclin/Cdk kinases and inactivation of Cdk inhibitors. However, how the G2/M phase is regulated by Akt remains unclear. Here, we show that Akt counteracts the function of WEE1Hu. Inactivation of Akt by chemotherapeutic drugs or the phosphatidylinositide-3-OH kinase inhibitor LY294002 induced G2/M arrest together with the inhibitory phosphorylation of Cdc2. Because the increased Cdc2 phosphorylation was completely suppressed by wee1hu gene silencing, WEE1Hu was associated with G2/M arrest induced by Akt inactivation. Further analyses revealed that Akt directly bound to and phosphorylated WEE1Hu during the S to G2 phase. Serine-642 was identified as an Akt-dependent phosphorylation site. WEE1Hu kinase activity was not affected by serine-642 phosphorylation. We revealed that serine-642 phosphorylation promoted cytoplasmic localization of WEE1Hu. The nuclear-to-cytoplasmic translocation was mediated by phosphorylation-dependent WEE1Hu binding to 14-3-3θ but not 14-3-3β or -σ. These results indicate that Akt promotes G2/M cell cycle progression by inducing phosphorylation-dependent 14-3-3θ binding and cytoplasmic localization of WEE1Hu.

scholarly journals Cell Cycle-Dependence of Autophagic Activity and Inhibition of Autophagosome Formation at M Phase in Tobacco BY-2 Cells

2020 ◽  
Vol 21 (23) ◽  
pp. 9166
Author(s):  
Shigeru Hanamata ◽  
Takamitsu Kurusu ◽  
Kazuyuki Kuchitsu
Keyword(s):  
Cell Cycle ◽  
Cell Cycle Progression ◽  
Plant Cells ◽  
Regulatory Mechanisms ◽  
Cdk Inhibitor ◽  
Autophagosome Formation ◽  
Cycle Progression ◽  
M Phase ◽  
Cell Cycle Dependence ◽  
Cycle Dependence

Autophagy is ubiquitous in eukaryotic cells and plays an essential role in stress adaptation and development by recycling nutrients and maintaining cellular homeostasis. However, the dynamics and regulatory mechanisms of autophagosome formation during the cell cycle in plant cells remain poorly elucidated. We here analyzed the number of autophagosomes during cell cycle progression in synchronized tobacco BY-2 cells expressing YFP-NtATG8a as a marker for the autophagosomes. Autophagosomes were abundant in the G2 and G1 phases of interphase, though they were much less abundant in the M and S phases. Autophagosomes drastically decreased during the G2/M transition, and the CDK inhibitor roscovitine inhibited the G2/M transition and the decrease in autophagosomes. Autophagosomes were rapidly increased by a proteasome inhibitor, MG-132. MG-132-induced autophagosome formation was also markedly lower in the M phases than during interphase. These results indicate that the activity of autophagosome formation is differently regulated at each cell cycle stage, which is strongly suppressed during mitosis.

scholarly journals Inactivation of CtIP Leads to Early Embryonic Lethality Mediated by G1 Restraint and to Tumorigenesis by Haploid Insufficiency

2005 ◽  
Vol 25 (9) ◽  
pp. 3535-3542 ◽  
Author(s):  
Phang-Lang Chen ◽  
Feng Liu ◽  
Suna Cai ◽  
Xiaoqin Lin ◽  
Aihua Li ◽  
...  
Keyword(s):  
Cell Cycle ◽  
Transcriptional Repression ◽  
Cell Cycle Progression ◽  
Tumor Formation ◽  
3T3 Cells ◽  
Embryonic Fibroblasts ◽  
Cycle Progression ◽  
Early Embryonic Lethality ◽  
Nih 3T3 ◽  
Regulate Cell Cycle Progression

ABSTRACT CtIP interacts with a group of tumor suppressor proteins including RB (retinoblastoma protein), BRCA1, Ikaros, and CtBP, which regulate cell cycle progression through transcriptional repression as well as chromatin remodeling. However, how CtIP exerts its biological function in cell cycle progression remains elusive. To address this issue, we generated an inactivated Ctip allele in mice by inserting a neo gene into exon 5. The corresponding Ctip − / − embryos died at embryonic day 4.0 (E4.0), and the blastocysts failed to enter S phase but accumulated in G1, leading to a slightly elevated cell death. Mouse NIH 3T3 cells depleted of Ctip were arrested at G1 with the concomitant increase in hypophosphorylated Rb and Cdk inhibitors, p21. However, depletion of Ctip failed to arrest Rb − / − mouse embryonic fibroblasts (MEF) or human osteosarcoma Saos-2 cells at G1, suggesting that this arrest is RB dependent. Importantly, the life span of Ctip +/ − heterozygotes was shortened by the development of multiple types of tumors, predominantly, large lymphomas. The wild-type Ctip allele and protein remained detectable in these tumors, suggesting that haploid insufficiency of Ctip leads to tumorigenesis. Taken together, this finding uncovers a novel G1/S regulation in that CtIP counteracts Rb-mediated G1 restraint. Deregulation of this function leads to a defect in early embryogenesis and contributes, in part, to tumor formation.

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