scholarly journals Metabolic status rather than cell cycle signals control quiescence entry and exit

2011 ◽  
Vol 192 (6) ◽  
pp. 949-957 ◽  
Author(s):  
Damien Laporte ◽  
Anne Lebaudy ◽  
Annelise Sahin ◽  
Benoît Pinson ◽  
Johanna Ceschin ◽  
...  
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Cell Cycle ◽  
Cell Growth ◽  
Carbon Source ◽  
Schizosaccharomyces Pombe ◽  
Metabolic Status ◽  
Cellular Structures ◽  
Entry And Exit ◽  
Molecular Determinants ◽  
Cell Growth And Proliferation

Quiescence is defined as a temporary arrest of proliferation, yet it likely encompasses various cellular situations. Our knowledge about this widespread cellular state remains limited. In particular, little is known about the molecular determinants that orchestrate quiescence establishment and exit. Here we show that upon carbon source exhaustion, budding yeast can enter quiescence from all cell cycle phases. Moreover, using cellular structures that are candidate markers for quiescence, we found that the first steps of quiescence exit can be triggered independently of cell growth and proliferation by the sole addition of glucose in both Saccharomyces cerevisiae and Schizosaccharomyces pombe. Importantly, glucose needs to be internalized and catabolized all the way down to glycolysis to mobilize quiescent cell specific structures, but, strikingly, ATP replenishment is apparently not the key signal. Altogether, these findings strongly suggest that quiescence entry and exit primarily rely on cellular metabolic status and can be uncoupled from the cell cycle.

scholarly journals Time varying mobility and turnover of actomyosin ring components during cytokinesis in Schizosaccharomyces pombe

2020 ◽  
pp. mbc.E20-09-0588
Author(s):  
Anton Kamnev ◽  
Saravanan Palani ◽  
Paola Zambon ◽  
Tom Cheffings ◽  
Nigel Burroughs ◽  
...  
Keyword(s):  
Cell Cycle ◽  
Schizosaccharomyces Pombe ◽  
Fluorescence Recovery After Photobleaching ◽  
Myosin Ii ◽  
Cellular Structures ◽  
Time Varying ◽  
Mobile Fraction ◽  
Novel Strategy ◽  
Cycle Dependent ◽  
Mobile Protein

Cytokinesis in many eukaryotes is dependent on a contractile actomyosin ring (AMR), composed of F-actin, myosin II, and other actin and myosin II regulators. Through fluorescence recovery after photobleaching experiments, many components of the AMR have been shown to be mobile and to undergo constant exchange with the cytosolic pools. However, how the mobility of its components changes at distinct stages of mitosis and cytokinesis has not been addressed. Here, we describe the mobility of eight Schizosaccharomyces pombe AMR proteins at different stages of mitosis and cytokinesis using an approach we have developed. We identified 3 classes of proteins, which showed 1) high (Ain1, Myo2, Myo51), 2) low (Rng2, Mid1, Myp2, Cdc12), and 3) cell cycle dependent (Cdc15) mobile fractions. We observed that the F-BAR protein Cdc15 undergoes a 20∼30% reduction in its mobile fraction after spindle breakdown and initiation of AMR contraction. Moreover, our data indicate that this change in Cdc15 mobility is dependent on the SIN-signalling pathway. Our work offers a novel strategy to estimate cell cycle-dependent mobile protein fractions in cellular structures and provides a valuable dataset, that is of interest to researchers working on cytokinesis.

scholarly journals Bombyx mori Dihydroorotate Dehydrogenase: Knockdown Inhibits Cell Growth and Proliferation via Inducing Cell Cycle Arrest

2018 ◽  
Vol 19 (9) ◽  
pp. 2581 ◽  
Author(s):  
Erhu Zhao ◽  
Xiaolan Jiang ◽  
Hongjuan Cui
Keyword(s):  
Cell Cycle ◽  
Amino Acid ◽  
Dna Replication ◽  
Cell Growth ◽  
Cell Cycle Arrest ◽  
Bombyx Mori ◽  
Dihydroorotate Dehydrogenase ◽  
Pyrimidine Synthesis ◽  
Cycle Arrest ◽  
Cell Growth And Proliferation

Dihydroorotate dehydrogenase (DHODH), in the de novo pyrimidine biosynthetic pathway, is the fourth enzyme of pyrimidine synthesis and is used to oxidize dihydroorotate and hence to orotat. We cloned and characterized here the dhod of silkworms, Bombyx mori. The full-length cDNA sequence of dhod is 1339 bp, including an open reading frame (ORF) of 1173 bp that encoded a 390 amino acid protein. And two domains were involved in the Dihydroorotate dehydrogenase amino acid sequence of silkworms, Bombyx mori (BmDHODH), namely a DHO_dh domain and a transmembrane domain in N-termina. The silkworm dhod is expressed throughout development and in nine tissues. Moreover, knockdown of the silkworm dhod gene reduced cell growth and proliferation through G2/M phase cell cycle arrest. Similarly, DHODH inhibitor (leflunomide) also reduced cell growth and proliferation, with a significant decrease of cyclin B and cdk2. DHODH is the fourth enzyme of pyrimidine synthesis, so we also found that leflunomide can inhibit, at least in part, the endomitotic DNA replication in silk glands cells. These findings demonstrate that downregulation of BmDHODH inhibits cell growth and proliferation in silkworm cells, and the endomitotic DNA replication in silk gland cells.

scholarly journals Mammalian Orc1 Protein Is Selectively Released from Chromatin and Ubiquitinated during the S-to-M Transition in the Cell Division Cycle

2002 ◽  
Vol 22 (1) ◽  
pp. 105-116 ◽  
Author(s):  
Cong-Jun Li ◽  
Melvin L. DePamphilis
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Cell Cycle ◽  
Cell Division ◽  
Schizosaccharomyces Pombe ◽  
Half Life ◽  
S Phase ◽  
Cell Division Cycle ◽  
26S Proteasome ◽  
Selective Dissociation

ABSTRACT Previous studies have shown that changes in the affinity of the hamster Orc1 protein for chromatin during the M-to-G1 transition correlate with the activity of hamster origin recognition complexes (ORCs) and the appearance of prereplication complexes at specific sites. Here we show that Orc1 is selectively released from chromatin as cells enter S phase, converted into a mono- or diubiquitinated form, and then deubiquitinated and re-bound to chromatin during the M-to-G1 transition. Orc1 is degraded by the 26S proteasome only when released into the cytosol, and peptide additions to Orc1 make it hypersensitive to polyubiquitination. In contrast, Orc2 remains tightly bound to chromatin throughout the cell cycle and is not a substrate for ubiquitination. Since the concentration of Orc1 remains constant throughout the cell cycle, and its half-life in vivo is the same as that of Orc2, ubiquitination of non-chromatin-bound Orc1 presumably facilitates the inactivation of ORCs by sequestering Orc1 during S phase. Thus, in contrast to yeast (Saccharomyces cerevisiae and Schizosaccharomyces pombe), mammalian ORC activity appears to be regulated during each cell cycle through selective dissociation and reassociation of Orc1 from chromatin-bound ORCs.

scholarly journals Artesunate Impairs Growth in Cisplatin-Resistant Bladder Cancer Cells by Cell Cycle Arrest, Apoptosis and Autophagy Induction

Cells ◽  
2020 ◽  
Vol 9 (12) ◽  
pp. 2643
Author(s):  
Fuguang Zhao ◽  
Olesya Vakhrusheva ◽  
Sascha D. Markowitsch ◽  
Kimberly S. Slade ◽  
Igor Tsaur ◽  
...  
Keyword(s):  
Cell Cycle ◽  
Dna Damage ◽  
Bladder Cancer ◽  
Cell Growth ◽  
Significant Inhibition ◽  
Cycle Arrest ◽  
Damage Repair ◽  
Autophagy Induction ◽  
Cell Growth And Proliferation ◽  
The Impact

Cisplatin, which induces DNA damage, is standard chemotherapy for advanced bladder cancer (BCa). However, efficacy is limited due to resistance development. Since artesunate (ART), a derivative of artemisinin originating from Traditional Chinese Medicine, has been shown to exhibit anti-tumor activity, and to inhibit DNA damage repair, the impact of artesunate on cisplatin-resistant BCa was evaluated. Cisplatin-sensitive (parental) and cisplatin-resistant BCa cells, RT4, RT112, T24, and TCCSup, were treated with ART (1–100 µM). Cell growth, proliferation, and cell cycle phases were investigated, as were apoptosis, necrosis, ferroptosis, autophagy, metabolic activity, and protein expression. Exposure to ART induced a time- and dose-dependent significant inhibition of tumor cell growth and proliferation of parental and cisplatin-resistant BCa cells. This inhibition was accompanied by a G0/G1 phase arrest and modulation of cell cycle regulating proteins. ART induced apoptos is by enhancing DNA damage, especially in the resistant cells. ART did not induce ferroptosis, but led to a disturbance of mitochondrial respiration and ATP generation. This impairment correlated with autophagy accompanied by a decrease in LC3B-I and an increase in LC3B-II. Since ART significantly inhibits proliferative and metabolic aspects of cisplatin-sensitive and cisplatin-resistant BCa cells, it may hold potential in treating advanced and therapy-resistant BCa.

scholarly journals A gene family for acidic ribosomal proteins in Schizosaccharomyces pombe: two essential and two nonessential genes.

1990 ◽  
Vol 10 (5) ◽  
pp. 2341-2348 ◽  
Author(s):  
M Beltrame ◽  
M E Bianchi
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Cell Growth ◽  
Gene Family ◽  
Schizosaccharomyces Pombe ◽  
Cell Survival ◽  
Ribosomal Proteins ◽  
The Other ◽  
Haploid Genome ◽  
Ribosomal Subunits ◽  
Physical Organization

We have cloned the genes for small acidic ribosomal proteins (A-proteins) of the fission yeast Schizosaccharomyces pombe. S. pombe contains four transcribed genes for small A-proteins per haploid genome, as is the case for Saccharomyces cerevisiae. In contrast, multicellular eucaryotes contain two transcribed genes per haploid genome. The four proteins of S. pombe, besides sharing a high overall similarity, form two couples of nearly identical sequences. Their corresponding genes have a very conserved structure and are transcribed to a similar level. Surprisingly, of each couple of genes coding for nearly identical proteins, one is essential for cell growth, whereas the other is not. We suggest that the unequal importance of the four small A-proteins for cell survival is related to their physical organization in 60S ribosomal subunits.

scholarly journals The sweet side of the cell cycle

2017 ◽  
Vol 45 (2) ◽  
pp. 313-322 ◽  
Author(s):  
Ee Phie Tan ◽  
Francesca E. Duncan ◽  
Chad Slawson
Keyword(s):  
Cell Cycle ◽  
Cell Division ◽  
Cell Growth ◽  
Chromosomal Segregation ◽  
Cellular Environment ◽  
Mammalian Cell Cycle ◽  
Intracellular Proteins ◽  
Organismal Development ◽  
Cell Growth And Proliferation ◽  
Mitosis And Meiosis

Cell division (mitosis) and gamete production (meiosis) are fundamental requirements for normal organismal development. The mammalian cell cycle is tightly regulated by different checkpoints ensuring complete and precise chromosomal segregation and duplication. In recent years, researchers have become increasingly interested in understanding how O-GlcNAc regulates the cell cycle. The O-GlcNAc post-translation modification is an O-glycosidic bond of a single β-N-acetylglucosamine sugar to serine/threonine residues of intracellular proteins. This modification is sensitive toward changes in nutrient levels in the cellular environment making O-GlcNAc a nutrient sensor capable of influencing cell growth and proliferation. Numerous studies have established that O-GlcNAcylation is essential in regulating mitosis and meiosis, while loss of O-GlcNAcylation is lethal in growing cells. Moreover, aberrant O-GlcNAcylation is linked with cancer and chromosomal segregation errors. In this review, we will discuss how O-GlcNAc controls different aspects of the cell cycle with a particular emphasis on mitosis and meiosis.

scholarly journals Dynamic metabolic network modeling of a mammalian cell cycle using time-course multi-omics data

2021 ◽  
Author(s):  
Ho-Joon Lee ◽  
Fangzhou Shen ◽  
Alec Eames ◽  
Mark P Jedrychowski ◽  
Sriram Chandrasekaran
Keyword(s):  
Cell Cycle ◽  
Cell Growth ◽  
Time Course ◽  
Metabolic Networks ◽  
Proteomics Data ◽  
Modeling Framework ◽  
Dynamic Genome ◽  
Metabolic Network Modeling ◽  
Cell Growth And Proliferation ◽  
The Impact

Cell cycle is a fundamental process for cell growth and proliferation, and its dysregulation leads to many diseases. How metabolic networks are regulated and rewired during the cell cycle is unknown. Here we apply a dynamic genome-scale metabolic modeling framework (DFA) to simulate a cell cycle of cytokine-activated murine pro-B cells. Phase-specific reaction activity predicted by DFA using time-course metabolomics were validated using matched time-course proteomics and phospho-proteomics data. Our model correctly predicted changes in methionine metabolism at the G1/S transition and the activation of lysine metabolism, nucleotides synthesis, fatty acid elongation and heme biosynthesis at the critical G0/G1 transition into cell growth and proliferation. Metabolic fluxes predicted from proteomics and phosphoproteomics constrained metabolic models were highly consistent with DFA fluxes and revealed that most reaction fluxes are regulated indirectly. Our model can help predict the impact of changes in nutrients, enzymes, or regulators on this critical cellular process.

scholarly journals A gene family for acidic ribosomal proteins in Schizosaccharomyces pombe: two essential and two nonessential genes

1990 ◽  
Vol 10 (5) ◽  
pp. 2341-2348
Author(s):  
M Beltrame ◽  
M E Bianchi
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Cell Growth ◽  
Gene Family ◽  
Schizosaccharomyces Pombe ◽  
Cell Survival ◽  
Ribosomal Proteins ◽  
The Other ◽  
Haploid Genome ◽  
Ribosomal Subunits ◽  
Physical Organization

We have cloned the genes for small acidic ribosomal proteins (A-proteins) of the fission yeast Schizosaccharomyces pombe. S. pombe contains four transcribed genes for small A-proteins per haploid genome, as is the case for Saccharomyces cerevisiae. In contrast, multicellular eucaryotes contain two transcribed genes per haploid genome. The four proteins of S. pombe, besides sharing a high overall similarity, form two couples of nearly identical sequences. Their corresponding genes have a very conserved structure and are transcribed to a similar level. Surprisingly, of each couple of genes coding for nearly identical proteins, one is essential for cell growth, whereas the other is not. We suggest that the unequal importance of the four small A-proteins for cell survival is related to their physical organization in 60S ribosomal subunits.

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