Base de dados : MEDLINE
Pesquisa : A11.284.430.214.190.750.820 [Categoria DeCS]
Referências encontradas : 7758 [refinar]
Mostrando: 1 .. 10   no formato [Detalhado]

página 1 de 776 ir para página                         

  1 / 7758 MEDLINE  
              next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:29293652
[Au] Autor:Stockum A; Snijders AP; Maertens GN
[Ad] Endereço:Imperial College London, Department of Medicine, Division of Infectious Diseases, Norfolk Place, London, United Kingdom.
[Ti] Título:USP11 deubiquitinates RAE1 and plays a key role in bipolar spindle formation.
[So] Source:PLoS One;13(1):e0190513, 2018.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Correct segregation of the mitotic chromosomes into daughter cells is a highly regulated process critical to safeguard genome stability. During M phase the spindle assembly checkpoint (SAC) ensures that all kinetochores are correctly attached before its inactivation allows progression into anaphase. Upon SAC inactivation, the anaphase promoting complex/cyclosome (APC/C) E3 ligase ubiquitinates and targets cyclin B and securin for proteasomal degradation. Here, we describe the identification of Ribonucleic Acid Export protein 1 (RAE1), a protein previously shown to be involved in SAC regulation and bipolar spindle formation, as a novel substrate of the deubiquitinating enzyme (DUB) Ubiquitin Specific Protease 11 (USP11). Lentiviral knock-down of USP11 or RAE1 in U2OS cells drastically reduces cell proliferation and increases multipolar spindle formation. We show that USP11 is associated with the mitotic spindle, does not regulate SAC inactivation, but controls ubiquitination of RAE1 at the mitotic spindle, hereby functionally modulating its interaction with Nuclear Mitotic Apparatus protein (NuMA).
[Mh] Termos MeSH primário: Proteínas Associadas à Matriz Nuclear/metabolismo
Proteínas de Transporte Nucleocitoplasmático/metabolismo
Fuso Acromático
Tioléster Hidrolases/metabolismo
[Mh] Termos MeSH secundário: Linhagem Celular Tumoral
Proliferação Celular
Técnicas de Silenciamento de Genes
Células HEK293
Seres Humanos
Peptídeos e Proteínas de Sinalização Intracelular/metabolismo
Ligação Proteica
Especificidade por Substrato
Tioléster Hidrolases/genética
Ubiquitinação
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Intracellular Signaling Peptides and Proteins); 0 (Nuclear Matrix-Associated Proteins); 0 (Nucleocytoplasmic Transport Proteins); 0 (RAE1 protein, human); 0 (SPRY3 protein, human); EC 3.1.2.- (Thiolester Hydrolases); EC 3.1.2.15 (USP11 protein, human)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180221
[Lr] Data última revisão:
180221
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180103
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0190513


  2 / 7758 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:29262707
[Au] Autor:Atalay PB; Asci O; Kaya FO; Tuna BG
[Ad] Endereço:1 Department of Medical Biology and Genetics, Faculty of Medicine, Maltepe University , Istanbul , Turkey.
[Ti] Título:Hydrogen peroxide prolongs mitotic arrest in a dose dependent manner and independently of the spindle assembly checkpoint activity in Saccharomyces cerevisiae.
[So] Source:Acta Biol Hung;68(4):477-489, 2017 Dec.
[Is] ISSN:0236-5383
[Cp] País de publicação:Hungary
[La] Idioma:eng
[Ab] Resumo:Oxidative stress and chromosome missegregation are important factors that are linked to aneuploidy. A major reason for chromosome missegragation is the inappropriate activity of the spindle assembly checkpoint (SAC), a conserved surveillance mechanism that monitors the state of kinetochore-microtubule attachments to ensure equal chromosome segregation in mitosis. SAC-activation induces a prolonged mitotic arrest. Mitosis is considered the most vulnerable cell cycle phase to several external signals, therefore increasing the time cells spent in this phase via mitotic arrest induction by SAC-activating agents is favorable for cancer therapy. Cancer cells also display elevated oxidative stress due to abnormally high production of reactive oxygen species (ROS). However, the effect of increased oxidative stress on the duration of mitotic arrest remains largely unknown. In this study, we investigated the effect of H O -induced oxidative stress on the mitotic arrest induced by a SAC-activating agent (nocodazole) in Saccharomyces cerevisiae. Our data suggest that oxidative stress prolongs SAC-activation induced mitotic arrest in a dose dependent manner. We, in addition, investigated the effect of H O treatment on the mitotic arrest induced independently of SAC-activation by using a conditional mutant (cdc23) and showed that the effect of H O -induced oxidative stress on mitotic arrest is independent of the SAC activity.
[Mh] Termos MeSH primário: Pontos de Checagem do Ciclo Celular/efeitos dos fármacos
Peróxido de Hidrogênio/farmacologia
Mitose/efeitos dos fármacos
Saccharomyces cerevisiae/metabolismo
Fuso Acromático/metabolismo
[Mh] Termos MeSH secundário: Subunidade Apc8 do Ciclossomo-Complexo Promotor de Anáfase/genética
Subunidade Apc8 do Ciclossomo-Complexo Promotor de Anáfase/metabolismo
Pontos de Checagem do Ciclo Celular/genética
Relação Dose-Resposta a Droga
Mitose/genética
Mutação
Saccharomyces cerevisiae/genética
Proteínas de Saccharomyces cerevisiae/genética
Proteínas de Saccharomyces cerevisiae/metabolismo
Fuso Acromático/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Apc8 Subunit, Anaphase-Promoting Complex-Cyclosome); 0 (CDC23 protein, S cerevisiae); 0 (Saccharomyces cerevisiae Proteins); BBX060AN9V (Hydrogen Peroxide)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180216
[Lr] Data última revisão:
180216
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171222
[St] Status:MEDLINE
[do] DOI:10.1556/018.68.2017.4.12


  3 / 7758 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:28455557
[Au] Autor:Goldstein A; Siegler N; Goldman D; Judah H; Valk E; Kõivomägi M; Loog M; Gheber L
[Ad] Endereço:Department of Chemistry and Ilse Katz Institute for Nanoscale Science and Technology, Ben-Gurion University of the Negev, PO Box 653, 84105, Beer-Sheva, Israel.
[Ti] Título:Three Cdk1 sites in the kinesin-5 Cin8 catalytic domain coordinate motor localization and activity during anaphase.
[So] Source:Cell Mol Life Sci;74(18):3395-3412, 2017 09.
[Is] ISSN:1420-9071
[Cp] País de publicação:Switzerland
[La] Idioma:eng
[Ab] Resumo:The bipolar kinesin-5 motors perform essential functions in mitotic spindle dynamics. We previously demonstrated that phosphorylation of at least one of the Cdk1 sites in the catalytic domain of the Saccharomyces cerevisiae kinesin-5 Cin8 (S277, T285, S493) regulates its localization to the anaphase spindle. The contribution of these three sites to phospho-regulation of Cin8, as well as the timing of such contributions, remains unknown. Here, we examined the function and spindle localization of phospho-deficient (serine/threonine to alanine) and phospho-mimic (serine/threonine to aspartic acid) Cin8 mutants. In vitro, the three Cdk1 sites undergo phosphorylation by Clb2-Cdk1. In cells, phosphorylation of Cin8 affects two aspects of its localization to the anaphase spindle, translocation from the spindle-pole bodies (SPBs) region to spindle microtubules (MTs) and the midzone, and detachment from the mitotic spindle. We found that phosphorylation of S277 is essential for the translocation of Cin8 from SPBs to spindle MTs and the subsequent detachment from the spindle. Phosphorylation of T285 mainly affects the detachment of Cin8 from spindle MTs during anaphase, while phosphorylation at S493 affects both the translocation of Cin8 from SPBs to the spindle and detachment from the spindle. Only S493 phosphorylation affected the anaphase spindle elongation rate. We conclude that each phosphorylation site plays a unique role in regulating Cin8 functions and postulate a model in which the timing and extent of phosphorylation of the three sites orchestrates the anaphase function of Cin8.
[Mh] Termos MeSH primário: Proteína Quinase CDC2/metabolismo
Cinesina/metabolismo
Proteínas de Saccharomyces cerevisiae/química
Proteínas de Saccharomyces cerevisiae/metabolismo
[Mh] Termos MeSH secundário: Anáfase/fisiologia
Domínio Catalítico
Ciclina B/metabolismo
Cinesina/química
Cinesina/genética
Microtúbulos/metabolismo
Mutagênese Sítio-Dirigida
Fosforilação
Saccharomyces cerevisiae/citologia
Saccharomyces cerevisiae/metabolismo
Proteínas de Saccharomyces cerevisiae/genética
Fuso Acromático/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (CLB2 protein, S cerevisiae); 0 (Cyclin B); 0 (Saccharomyces cerevisiae Proteins); EC 2.7.11.22 (CDC2 Protein Kinase); EC 3.6.4.4 (Kinesin)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:180131
[Lr] Data última revisão:
180131
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170430
[St] Status:MEDLINE
[do] DOI:10.1007/s00018-017-2523-z


  4 / 7758 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:27773484
[Au] Autor:Webster A; Schuh M
[Ad] Endereço:Department of Meiosis, Max Planck Institute for Biophysical Chemistry, Am Fassberg 11, D-37077, Göttingen, Germany.
[Ti] Título:Mechanisms of Aneuploidy in Human Eggs.
[So] Source:Trends Cell Biol;27(1):55-68, 2017 01.
[Is] ISSN:1879-3088
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Eggs and sperm develop through a specialized cell division called meiosis. During meiosis, the number of chromosomes is reduced by two sequential divisions in preparation for fertilization. In human female meiosis, chromosomes frequently segregate incorrectly, resulting in eggs with an abnormal number of chromosomes. When fertilized, these eggs give rise to aneuploid embryos that usually fail to develop. As women become older, errors in meiosis occur more frequently, resulting in increased risks of infertility, miscarriage, and congenital syndromes, such as Down's syndrome. Here, we review recent studies that identify the mechanisms causing aneuploidy in female meiosis, with a particular emphasis on studies in humans.
[Mh] Termos MeSH primário: Aneuploidia
Óvulo/metabolismo
[Mh] Termos MeSH secundário: Envelhecimento/fisiologia
Seres Humanos
Meiose
Modelos Biológicos
Óvulo/citologia
Fuso Acromático/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW; RESEARCH SUPPORT, NON-U.S. GOV'T
[Em] Mês de entrada:1712
[Cu] Atualização por classe:180125
[Lr] Data última revisão:
180125
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161025
[St] Status:MEDLINE


  5 / 7758 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:29302000
[Au] Autor:Saldivar JC; Cimprich KA
[Ad] Endereço:Department of Chemical and Systems Biology, Stanford University School of Medicine, 318 Campus Drive, Stanford, CA 94305-5441, USA.
[Ti] Título:A new mitotic activity comes into focus.
[So] Source:Science;359(6371):30-31, 2018 01 05.
[Is] ISSN:1095-9203
[Cp] País de publicação:United States
[La] Idioma:eng
[Mh] Termos MeSH primário: Mitose
Fuso Acromático
[Mh] Termos MeSH secundário: Seres Humanos
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL; RESEARCH SUPPORT, NON-U.S. GOV'T; COMMENT
[Em] Mês de entrada:1801
[Cu] Atualização por classe:180113
[Lr] Data última revisão:
180113
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180106
[St] Status:MEDLINE
[do] DOI:10.1126/science.aar4799


  6 / 7758 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:28747439
[Au] Autor:Dewey EB; Johnston CA
[Ad] Endereço:Department of Biology, University of New Mexico, Albuquerque, NM 87131.
[Ti] Título:Diverse mitotic functions of the cytoskeletal cross-linking protein Shortstop suggest a role in Dynein/Dynactin activity.
[So] Source:Mol Biol Cell;28(19):2555-2568, 2017 Sep 15.
[Is] ISSN:1939-4586
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Proper assembly and orientation of the bipolar mitotic spindle is critical to the fidelity of cell division. Mitotic precision fundamentally contributes to cell fate specification, tissue development and homeostasis, and chromosome distribution within daughter cells. Defects in these events are thought to contribute to several human diseases. The underlying mechanisms that function in spindle morphogenesis and positioning remain incompletely defined, however. Here we describe diverse roles for the actin-microtubule cross-linker Shortstop (Shot) in mitotic spindle function in Shot localizes to mitotic spindle poles, and its knockdown results in an unfocused spindle pole morphology and a disruption of proper spindle orientation. Loss of Shot also leads to chromosome congression defects, cell cycle progression delay, and defective chromosome segregation during anaphase. These mitotic errors trigger apoptosis in epithelial tissue, and blocking this apoptotic response results in a marked induction of the epithelial-mesenchymal transition marker MMP-1. The actin-binding domain of Shot directly interacts with Actin-related protein-1 (Arp-1), a key component of the Dynein/Dynactin complex. Knockdown of Arp-1 phenocopies Shot loss universally, whereas chemical disruption of F-actin does so selectively. Our work highlights novel roles for Shot in mitosis and suggests a mechanism involving Dynein/Dynactin activation.
[Mh] Termos MeSH primário: Proteínas de Drosophila/metabolismo
Proteínas de Drosophila/fisiologia
Proteínas dos Microfilamentos/metabolismo
Proteínas dos Microfilamentos/fisiologia
[Mh] Termos MeSH secundário: Actinas/metabolismo
Anáfase
Animais
Ciclo Celular
Cromossomos/metabolismo
Citoesqueleto/patologia
Drosophila/metabolismo
Proteínas de Drosophila/genética
Complexo Dinactina/metabolismo
Dineínas/metabolismo
Proteínas dos Microfilamentos/genética
Proteínas Associadas aos Microtúbulos/metabolismo
Microtúbulos/metabolismo
Mitose/fisiologia
Ligação Proteica
Fuso Acromático/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Actins); 0 (Drosophila Proteins); 0 (Dynactin Complex); 0 (Microfilament Proteins); 0 (Microtubule-Associated Proteins); 0 (shot protein, Drosophila); EC 3.6.4.2 (Dyneins)
[Em] Mês de entrada:1711
[Cu] Atualização por classe:180106
[Lr] Data última revisão:
180106
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170728
[St] Status:MEDLINE
[do] DOI:10.1091/mbc.E17-04-0219


  7 / 7758 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:28466790
[Au] Autor:Omelyanchuk LV; Munzarova AF
[Ad] Endereço:Institute of Molecular and Cellular Biology, Novosibirsk, Russia.
[Ti] Título:Theoretical model of mitotic spindle microtubule growth for FRAP curve interpretation.
[So] Source:BMC Syst Biol;11(Suppl 1):378, 2017 02 24.
[Is] ISSN:1752-0509
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: Spindle FRAP curves depend on the kinetic parameters of microtubule polymerization and depolymerization. The empirical FRAP curve proposed earlier permits determination of only one such dynamic parameter, commonly called the "tubulin turnover". The aim of our study was to build a FRAP curve based on an already known kinetic model of microtubule growth. RESULTS: A numerical expression that describes the distribution of polymerizing and depolymerizing microtubule ends as a function of four kinetic parameters is presented. In addition, a theoretical FRAP curve for the metaphase spindle is constructed using previously published dynamic parameters. CONCLUSION: The numerical expression we elaborated can replace the empirical FRAP curve described earlier for a spindle comprising fluorescently marked microtubules. The curve we generated fits well the experimental data.
[Mh] Termos MeSH primário: Recuperação de Fluorescência Após Fotodegradação
Microtúbulos/metabolismo
Modelos Biológicos
Fuso Acromático/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Em] Mês de entrada:1712
[Cu] Atualização por classe:171223
[Lr] Data última revisão:
171223
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170504
[St] Status:MEDLINE
[do] DOI:10.1186/s12918-016-0378-9


  8 / 7758 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:28450458
[Au] Autor:Renicke C; Allmann AK; Lutz AP; Heimerl T; Taxis C
[Ad] Endereço:Department of Biology/Genetics, Philipps-Universität Marburg, 35043, Germany.
[Ti] Título:The Mitotic Exit Network Regulates Spindle Pole Body Selection During Sporulation of .
[So] Source:Genetics;206(2):919-937, 2017 06.
[Is] ISSN:1943-2631
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Age-based inheritance of centrosomes in eukaryotic cells is associated with faithful chromosome distribution in asymmetric cell divisions. During ascospore formation, such an inheritance mechanism targets the yeast centrosome equivalents, the spindle pole bodies (SPBs) at meiosis II onset. Decreased nutrient availability causes initiation of spore formation at only the younger SPBs and their associated genomes. This mechanism ensures encapsulation of nonsister genomes, which preserves genetic diversity and provides a fitness advantage at the population level. Here, by usage of an enhanced system for sporulation-induced protein depletion, we demonstrate that the core mitotic exit network (MEN) is involved in age-based SPB selection. Moreover, efficient genome inheritance requires Dbf2/20-Mob1 during a late step in spore maturation. We provide evidence that the meiotic functions of the MEN are more complex than previously thought. In contrast to mitosis, completion of the meiotic divisions does not strictly rely on the MEN whereas its activity is required at different time points during spore development. This is reminiscent of vegetative MEN functions in spindle polarity establishment, mitotic exit, and cytokinesis. In summary, our investigation contributes to the understanding of age-based SPB inheritance during sporulation of and provides general insights on network plasticity in the context of a specialized developmental program. Moreover, the improved system for a developmental-specific tool to induce protein depletion will be useful in other biological contexts.
[Mh] Termos MeSH primário: Proteínas de Ciclo Celular/genética
Mitose/genética
Proteínas Serina-Treonina Quinases/genética
Proteínas de Saccharomyces cerevisiae/genética
Fuso Acromático/genética
Corpos Polares do Fuso/genética
[Mh] Termos MeSH secundário: Citocinese/genética
Saccharomyces cerevisiae/genética
Esporos Fúngicos/genética
Esporos Fúngicos/crescimento & desenvolvimento
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Cell Cycle Proteins); 0 (Saccharomyces cerevisiae Proteins); EC 2.7.11.1 (DBF2 protein, S cerevisiae); EC 2.7.11.1 (Protein-Serine-Threonine Kinases)
[Em] Mês de entrada:1707
[Cu] Atualização por classe:171213
[Lr] Data última revisão:
171213
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170429
[St] Status:MEDLINE
[do] DOI:10.1534/genetics.116.194522


  9 / 7758 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:29065308
[Au] Autor:Komaki S; Schnittger A
[Ad] Endereço:University of Hamburg, Biozentrum Klein Flottbek, Department of Developmental Biology, Ohnhorststrasse 18, D-22609 Hamburg, Germany.
[Ti] Título:The Spindle Assembly Checkpoint in Arabidopsis Is Rapidly Shut Off during Severe Stress.
[So] Source:Dev Cell;43(2):172-185.e5, 2017 Oct 23.
[Is] ISSN:1878-1551
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The spindle assembly checkpoint (SAC) in animals and yeast assures equal segregation of chromosomes during cell division. The prevalent occurrence of polyploidy in flowering plants together with the observation that many plants can be readily forced to double their genomes by application of microtubule drugs raises the question of whether plants have a proper SAC. Here, we provide a functional framework of the core SAC proteins in Arabidopsis. We reveal that Arabidopsis will delay mitosis in a SAC-dependent manner if the spindle is perturbed. However, we also show that the molecular architecture of the SAC is unique in plants. Moreover, the SAC is short-lived and cannot stay active for more than 2 hr, after which the cell cycle is reset. This resetting opens the possibility for genome duplications and raises the hypothesis that a rapid termination of a SAC-induced mitotic arrest provides an adaptive advantage for plants impacting plant genome evolution.
[Mh] Termos MeSH primário: Proteínas de Arabidopsis/metabolismo
Arabidopsis/metabolismo
Pontos de Checagem do Ciclo Celular/fisiologia
Proteínas de Ciclo Celular/metabolismo
Mitose/fisiologia
Fuso Acromático/fisiologia
Estresse Fisiológico
[Mh] Termos MeSH secundário: Arabidopsis/citologia
Arabidopsis/crescimento & desenvolvimento
Microtúbulos/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Arabidopsis Proteins); 0 (Cell Cycle Proteins)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171031
[Lr] Data última revisão:
171031
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171025
[St] Status:MEDLINE


  10 / 7758 MEDLINE  
              first record previous record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:29028845
[Au] Autor:Shamsuzzaman M; Bommakanti A; Zapinsky A; Rahman N; Pascual C; Lindahl L
[Ad] Endereço:Department of Biological Sciences, University of Maryland Baltimore County (UMBC), Baltimore, Maryland, United States of America.
[Ti] Título:Analysis of cell cycle parameters during the transition from unhindered growth to ribosomal and translational stress conditions.
[So] Source:PLoS One;12(10):e0186494, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Abrogation of ribosome synthesis (ribosomal stress) leads to cell cycle arrest. However, the immediate cell response to cessation of ribosome formation and the transition from normal cell proliferation to cell cycle arrest have not been characterized. Furthermore, there are conflicting conclusions about whether cells are arrested in G2/M or G1, and whether the cause is dismantling ribosomal assembly per se, or the ensuing decreased number of translating ribosomes. To address these questions, we have compared the time kinetics of key cell cycle parameters after inhibiting ribosome formation or function in Saccharomyces cerevisiae. Within one-to-two hours of repressing genes for individual ribosomal proteins or Translation Elongation factor 3, configurations of spindles, spindle pole bodies began changing. Actin began depolarizing within 4 hours. Thus the loss of ribosome formation and function is sensed immediately. After several hours no spindles or mitotic actin rings were visible, but membrane ingression was completed in most cells and Ace2 was localized to daughter cell nuclei demonstrating that the G1 stage was reached. Thus cell division was completed without the help of a contractile actin ring. Moreover, cell wall material held mother and daughter cells together resulting in delayed cell separation, suggesting that expression or function of daughter gluconases and chitinases is inhibited. Moreover, cell development changes in very similar ways in response to inhibition of ribosome formation and function, compatible with the notion that decreased translation capacity contributes to arresting the cell cycle after abrogation of ribosome biogenesis. Potential implications for the mechanisms of diseases caused by mutations in ribosomal genes (ribosomopathies) are discussed.
[Mh] Termos MeSH primário: Ciclo Celular
Biossíntese de Proteínas
Ribossomos/genética
Saccharomyces cerevisiae/citologia
Saccharomyces cerevisiae/genética
[Mh] Termos MeSH secundário: Actinas/metabolismo
Parede Celular/metabolismo
Proteínas de Ligação a DNA/metabolismo
Fatores de Alongamento de Peptídeos/metabolismo
Ribossomos/metabolismo
Saccharomyces cerevisiae/metabolismo
Proteínas de Saccharomyces cerevisiae/metabolismo
Fuso Acromático/metabolismo
Fatores de Transcrição/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (ACE2 protein, S cerevisiae); 0 (Actins); 0 (DNA-Binding Proteins); 0 (Peptide Elongation Factors); 0 (Saccharomyces cerevisiae Proteins); 0 (Transcription Factors); 0 (YEF3 protein, S cerevisiae)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171031
[Lr] Data última revisão:
171031
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171014
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0186494



página 1 de 776 ir para página                         
   


Refinar a pesquisa
  Base de dados : MEDLINE Formulário avançado   

    Pesquisar no campo  
1  
2
3
 
           



Search engine: iAH v2.6 powered by WWWISIS

BIREME/OPAS/OMS - Centro Latino-Americano e do Caribe de Informação em Ciências da Saúde