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  1 / 2050 MEDLINE  
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[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


  2 / 2050 MEDLINE  
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[PMID]:28740117
[Au] Autor:Glover TW; Wilson TE; Arlt MF
[Ad] Endereço:Department of Human Genetics; the Department of Pathology; and the Department of Pediatrics and Communicable Diseases, University of Michigan Medical School, Ann Arbor, Michigan 48109, USA.
[Ti] Título:Fragile sites in cancer: more than meets the eye.
[So] Source:Nat Rev Cancer;17(8):489-501, 2017 07 25.
[Is] ISSN:1474-1768
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Ever since initial suggestions that instability at common fragile sites (CFSs) could be responsible for chromosome rearrangements in cancers, CFSs and associated genes have been the subject of numerous studies, leading to questions and controversies about their role and importance in cancer. It is now clear that CFSs are not frequently involved in translocations or other cancer-associated recurrent gross chromosome rearrangements. However, recent studies have provided new insights into the mechanisms of CFS instability, their effect on genome instability, and their role in generating focal copy number alterations that affect the genomic landscape of many cancers.
[Mh] Termos MeSH primário: Instabilidade Cromossômica
Sítios Frágeis do Cromossomo
Variações do Número de Cópias de DNA
Neoplasias/genética
Oncogenes/genética
[Mh] Termos MeSH secundário: Anáfase
Animais
Quebra Cromossômica
Quebras de DNA de Cadeia Dupla
Replicação do DNA
Rearranjo Gênico
Seres Humanos
Metáfase
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW; RESEARCH SUPPORT, N.I.H., INTRAMURAL
[Em] Mês de entrada:1709
[Cu] Atualização por classe:180116
[Lr] Data última revisão:
180116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170726
[St] Status:MEDLINE
[do] DOI:10.1038/nrc.2017.52


  3 / 2050 MEDLINE  
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[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


  4 / 2050 MEDLINE  
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[PMID]:29017027
[Au] Autor:Vukusic K; Buda R; Bosilj A; Milas A; Pavin N; Tolic IM
[Ad] Endereço:Division of Molecular Biology, Ruder Boskovic Institute, Bijenicka cesta 54, 10000 Zagreb, Croatia.
[Ti] Título:Microtubule Sliding within the Bridging Fiber Pushes Kinetochore Fibers Apart to Segregate Chromosomes.
[So] Source:Dev Cell;43(1):11-23.e6, 2017 Oct 09.
[Is] ISSN:1878-1551
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:During cell division, mitotic spindle microtubules segregate chromosomes by exerting forces on kinetochores. What forces drive chromosome segregation in anaphase remains a central question. The current model for anaphase in human cells includes shortening of kinetochore fibers and separation of spindle poles. Both processes require kinetochores to be linked with the poles. Here we show, by combining laser ablation, photoactivation, and theoretical modeling, that kinetochores can separate without any attachment to one spindle pole. This separation requires the bridging fiber, a microtubule bundle that connects sister kinetochore fibers. Bridging fiber microtubules in intact spindles slide apart with kinetochore fibers, indicating strong crosslinks between them. We conclude that sliding of microtubules within the bridging fibers drives pole separation and pushes kinetochore fibers poleward by the friction of passive crosslinks between these fibers. Thus, sliding within the bridging fiber works together with the shortening of kinetochore fibers to segregate chromosomes.
[Mh] Termos MeSH primário: Anáfase/fisiologia
Segregação de Cromossomos/fisiologia
Cinetocoros/metabolismo
Metáfase/fisiologia
Microtúbulos/metabolismo
[Mh] Termos MeSH secundário: Células Cultivadas
Seres Humanos
Modelos Biológicos
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171023
[Lr] Data última revisão:
171023
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171011
[St] Status:MEDLINE


  5 / 2050 MEDLINE  
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[PMID]:28942021
[Au] Autor:Ifuji A; Kuga T; Kaibori Y; Saito Y; Nakayama Y
[Ad] Endereço:Department of Biochemistry & Molecular Biology, Kyoto Pharmaceutical University, Kyoto 607-8414, Japan.
[Ti] Título:A novel immunofluorescence method to visualize microtubules in the antiparallel overlaps of microtubule-plus ends in the anaphase and telophase midzone.
[So] Source:Exp Cell Res;360(2):347-357, 2017 Nov 15.
[Is] ISSN:1090-2422
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Cell division, in which duplicated chromosomes are separated into two daughter cells, is the most dynamic event during cell proliferation. Chromosome movement is powered mainly by microtubules, which vary in morphology and are organized into characteristic structures according to mitotic progression. During the later stages of mitosis, antiparallel microtubules form the spindle midzone, and the irregular formation of the midzone often leads to failure of cytokinesis, giving rise to the unequal segregation of chromosomes. However, it is difficult to analyze the morphology of these microtubules because microtubules in the antiparallel overlaps of microtubule-plus ends in the midzone are embedded in highly electron-dense matrices, impeding the access of anti-tubulin antibodies to their epitopes during immunofluorescence staining. Here, we developed a novel method to visualize selectively antiparallel microtubule overlaps in the midzone. When cells are air-dried before fixation, aligned α-tubulin staining is observed and colocalized with PRC1 in the center of the midzone of anaphase and telophase cells, suggesting that antiparallel microtubule overlaps can be visualized by this method. In air-dried cells, mCherry-α-tubulin fluorescence and ß-tubulin staining show almost the same pattern as α-tubulin staining in the midzone, suggesting that the selective visualization of antiparallel microtubule overlaps in air-dried cells is not attributed to an alteration of the antigenicity of α-tubulin. Taxol treatment extends the microtubule filaments of the midzone in air-dried cells, and nocodazole treatment conversely decreases the number of microtubules, suggesting that unstable microtubules are depolymerized during the air-drying method. It is of note that the air-drying method enables the detection of the disruption of the midzone and premature midzone formation upon Aurora B and Plk1 inhibition, respectively. These results suggest that the air-drying method is suitable for visualizing microtubules in the antiparallel overlaps of microtubule-plus ends of the midzone and for detecting their effects on midzone formation.
[Mh] Termos MeSH primário: Anáfase
Imunofluorescência/métodos
Microtúbulos/metabolismo
Fuso Acromático/metabolismo
Telófase
[Mh] Termos MeSH secundário: Animais
Células Cultivadas
Segregação de Cromossomos/fisiologia
Citocinese/fisiologia
Células HeLa
Seres Humanos
Microtúbulos/ultraestrutura
Mitose
Fuso Acromático/ultraestrutura
Suínos
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Em] Mês de entrada:1711
[Cu] Atualização por classe:171107
[Lr] Data última revisão:
171107
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170925
[St] Status:MEDLINE


  6 / 2050 MEDLINE  
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[PMID]:28821562
[Au] Autor:Tipton AR; Wren JD; Daum JR; Siefert JC; Gorbsky GJ
[Ad] Endereço:Cell Cycle and Cancer Biology Research Program, Oklahoma Medical Research Foundation, Oklahoma City, OK.
[Ti] Título:GTSE1 regulates spindle microtubule dynamics to control Aurora B kinase and Kif4A chromokinesin on chromosome arms.
[So] Source:J Cell Biol;216(10):3117-3132, 2017 Oct 02.
[Is] ISSN:1540-8140
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:In mitosis, the dynamic assembly and disassembly of microtubules are critical for normal chromosome movement and segregation. Microtubule turnover varies among different mitotic spindle microtubules, dictated by their spatial distribution within the spindle. How turnover among the various classes of spindle microtubules is differentially regulated and the resulting significance of differential turnover for chromosome movement remains a mystery. As a new tactic, we used global microarray meta-analysis (GAMMA), a bioinformatic method, to identify novel regulators of mitosis, and in this study, we describe G2- and S phase-expressed protein 1 (GTSE1). GTSE1 is expressed exclusively in late G2 and M phase. From nuclear envelope breakdown until anaphase onset, GTSE1 binds preferentially to the most stable mitotic spindle microtubules and promotes their turnover. Cells depleted of GTSE1 show defects in chromosome alignment at the metaphase plate and in spindle pole integrity. These defects are coupled with an increase in the proportion of stable mitotic spindle microtubules. A consequence of this reduced microtubule turnover is diminished recruitment and activity of Aurora B kinase on chromosome arms. This decrease in Aurora B results in diminished binding of the chromokinesin Kif4A to chromosome arms.
[Mh] Termos MeSH primário: Aurora Quinase B/metabolismo
Cromossomos Humanos/metabolismo
Cinesina/metabolismo
Proteínas Associadas aos Microtúbulos/metabolismo
Microtúbulos/metabolismo
Fuso Acromático/metabolismo
[Mh] Termos MeSH secundário: Anáfase/fisiologia
Aurora Quinase B/genética
Cromossomos Humanos/genética
Células HeLa
Seres Humanos
Cinesina/genética
Proteínas Associadas aos Microtúbulos/genética
Microtúbulos/genética
Fuso Acromático/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (GTSE1 protein, human); 0 (Microtubule-Associated Proteins); EC 2.7.11.1 (AURKB protein, human); EC 2.7.11.1 (Aurora Kinase B); EC 3.6.1.- (KIF4A protein, human); EC 3.6.4.4 (Kinesin)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171007
[Lr] Data última revisão:
171007
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170820
[St] Status:MEDLINE
[do] DOI:10.1083/jcb.201610012


  7 / 2050 MEDLINE  
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[PMID]:28712722
[Au] Autor:Tsankova A; Pham TT; Garcia DS; Otte F; Cabernard C
[Ad] Endereço:Biozentrum, University of Basel, Klingelbergstrasse 50-70, 4056 Basel, Switzerland.
[Ti] Título:Cell Polarity Regulates Biased Myosin Activity and Dynamics during Asymmetric Cell Division via Drosophila Rho Kinase and Protein Kinase N.
[So] Source:Dev Cell;42(2):143-155.e5, 2017 Jul 24.
[Is] ISSN:1878-1551
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Cell and tissue morphogenesis depends on the correct regulation of non-muscle Myosin II, but how this motor protein is spatiotemporally controlled is incompletely understood. Here, we show that in asymmetrically dividing Drosophila neural stem cells, cell intrinsic polarity cues provide spatial and temporal information to regulate biased Myosin activity. Using live cell imaging and a genetically encoded Myosin activity sensor, we found that Drosophila Rho kinase (Rok) enriches for activated Myosin on the neuroblast cortex prior to nuclear envelope breakdown (NEB). After NEB, the conserved polarity protein Partner of Inscuteable (Pins) sequentially enriches Rok and Protein Kinase N (Pkn) on the apical neuroblast cortex. Our data suggest that apical Rok first increases phospho-Myosin, followed by Pkn-mediated Myosin downregulation, possibly through Rok inhibition. We propose that polarity-induced spatiotemporal control of Rok and Pkn is important for unequal cortical expansion, ensuring correct cleavage furrow positioning and the establishment of physical asymmetry.
[Mh] Termos MeSH primário: Divisão Celular Assimétrica
Polaridade Celular
Proteínas de Drosophila/metabolismo
Drosophila melanogaster/citologia
Drosophila melanogaster/enzimologia
Miosinas/metabolismo
Proteína Quinase C/metabolismo
Quinases Associadas a rho/metabolismo
[Mh] Termos MeSH secundário: Anáfase
Animais
Forma Celular
Mutação/genética
Neurônios/citologia
Neurônios/metabolismo
Fosforilação
Transporte Proteico
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Drosophila Proteins); EC 2.7.1.- (protein kinase N); EC 2.7.11.1 (rho-Associated Kinases); EC 2.7.11.13 (Protein Kinase C); EC 3.6.4.1 (Myosins)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170925
[Lr] Data última revisão:
170925
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170718
[St] Status:MEDLINE


  8 / 2050 MEDLINE  
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[PMID]:28630147
[Au] Autor:Cullati SN; Kabeche L; Kettenbach AN; Gerber SA
[Ad] Endereço:Department of Biochemistry and Cell Biology, Geisel School of Medicine at Dartmouth, Lebanon, NH.
[Ti] Título:A bifurcated signaling cascade of NIMA-related kinases controls distinct kinesins in anaphase.
[So] Source:J Cell Biol;216(8):2339-2354, 2017 Aug 07.
[Is] ISSN:1540-8140
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:In mitosis, cells undergo a precisely orchestrated series of spatiotemporal changes in cytoskeletal structure to divide their genetic material. These changes are coordinated by a sophisticated network of protein-protein interactions and posttranslational modifications. In this study, we report a bifurcation in a signaling cascade of the NIMA-related kinases (Neks) Nek6, Nek7, and Nek9 that is required for the localization and function of two kinesins essential for cytokinesis, Mklp2 and Kif14. We demonstrate that a Nek9, Nek6, and Mklp2 signaling module controls the timely localization and bundling activity of Mklp2 at the anaphase central spindle. We further show that a separate Nek9, Nek7, and Kif14 signaling module is required for the recruitment of the Rho-interacting kinase citron to the anaphase midzone. Our findings uncover an anaphase-specific function for these effector kinesins that is controlled by specific Nek kinase signaling modules to properly coordinate cytokinesis.
[Mh] Termos MeSH primário: Anáfase
Citocinese
Cinesina/metabolismo
Quinases Relacionadas a NIMA/metabolismo
Fuso Acromático/enzimologia
[Mh] Termos MeSH secundário: Trifosfato de Adenosina/metabolismo
Cromatografia de Afinidade
Células HeLa
Seres Humanos
Hidrólise
Peptídeos e Proteínas de Sinalização Intracelular/genética
Peptídeos e Proteínas de Sinalização Intracelular/metabolismo
Cinesina/genética
Quinases Relacionadas a NIMA/genética
Proteínas Oncogênicas/genética
Proteínas Oncogênicas/metabolismo
Fosforilação
Proteínas Serina-Treonina Quinases/genética
Proteínas Serina-Treonina Quinases/metabolismo
Interferência de RNA
Transdução de Sinais
Espectrometria de Massas em Tandem
Fatores de Tempo
Transfecção
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Intracellular Signaling Peptides and Proteins); 0 (KIF20A protein, human); 0 (Oncogene Proteins); 8L70Q75FXE (Adenosine Triphosphate); EC 2.7.1.- (citron-kinase); EC 2.7.11.1 (NEK6 protein, human); EC 2.7.11.1 (NEK7 protein, human); EC 2.7.11.1 (NEK9 protein, human); EC 2.7.11.1 (NIMA-Related Kinases); EC 2.7.11.1 (Protein-Serine-Threonine Kinases); EC 3.6.1.- (KIF14 protein, human); EC 3.6.4.4 (Kinesin)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170925
[Lr] Data última revisão:
170925
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170621
[St] Status:MEDLINE
[do] DOI:10.1083/jcb.201512055


  9 / 2050 MEDLINE  
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[PMID]:28588079
[Au] Autor:Moriggi G; Gaspar SG; Nieto B; Bustelo XR; Dosil M
[Ad] Endereço:Centro de Investigación del Cáncer and Instituto de Biología Molecular y Celular del Cáncer, CSIC-University of Salamanca, 37007 Salamanca, Spain.
[Ti] Título:Focal accumulation of preribosomes outside the nucleolus during metaphase-anaphase in budding yeast.
[So] Source:RNA;23(9):1432-1443, 2017 Sep.
[Is] ISSN:1469-9001
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:contains one nucleolus that remains intact in the mother-cell side of the nucleus throughout most of mitosis. Based on this, it is assumed that the bulk of ribosome production during cell division occurs in the mother cell. Here, we show that the ribosome synthesis machinery localizes not only in the nucleolus but also at a center that is present in the bud side of the nucleus after the initiation of mitosis. This center can be visualized by live microscopy as a punctate body located in close proximity to the nuclear envelope and opposite to the nucleolus. It contains ribosomal DNA (rDNA) and precursors of both 40S and 60S ribosomal subunits. Proteins that actively participate in ribosome synthesis, but not functionally defective variants, accumulate in that site. The formation of this body occurs in the metaphase-to-anaphase transition when discrete regions of rDNA occasionally exit the nucleolus and move into the bud. Collectively, our data unveil the existence of a previously unknown mechanism for preribosome accumulation at the nuclear periphery in budding yeast. We propose that this might be a strategy to expedite the delivery of ribosomes to the growing bud.
[Mh] Termos MeSH primário: Anáfase
Nucléolo Celular/genética
Nucléolo Celular/metabolismo
Metáfase
Saccharomycetales/genética
Saccharomycetales/metabolismo
[Mh] Termos MeSH secundário: Transporte Biológico
Pontos de Checagem do Ciclo Celular/genética
DNA Ribossômico/genética
DNA Ribossômico/metabolismo
Expressão Gênica
Genes Reporter
Espaço Intracelular/metabolismo
RNA Ribossômico/genética
RNA Ribossômico/metabolismo
Ribossomos/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (DNA, Ribosomal); 0 (RNA, Ribosomal)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171009
[Lr] Data última revisão:
171009
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170608
[St] Status:MEDLINE
[do] DOI:10.1261/rna.061259.117


  10 / 2050 MEDLINE  
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[PMID]:28535376
[Au] Autor:Cheerambathur DK; Prevo B; Hattersley N; Lewellyn L; Corbett KD; Oegema K; Desai A
[Ad] Endereço:Ludwig Institute for Cancer Research, CMM-E Room 3052, 9500 Gilman Drive, La Jolla, CA 92093-0653, USA; Department of Cellular & Molecular Medicine, University of California San Diego, La Jolla, CA 92093, USA. Electronic address: dcheerambathur@ucsd.edu.
[Ti] Título:Dephosphorylation of the Ndc80 Tail Stabilizes Kinetochore-Microtubule Attachments via the Ska Complex.
[So] Source:Dev Cell;41(4):424-437.e4, 2017 May 22.
[Is] ISSN:1878-1551
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:During cell division, genome inheritance is orchestrated by microtubule attachments formed at kinetochores of mitotic chromosomes. The primary microtubule coupler at the kinetochore, the Ndc80 complex, is regulated by Aurora kinase phosphorylation of its N-terminal tail. Dephosphorylation is proposed to stabilize kinetochore-microtubule attachments by strengthening electrostatic interactions of the tail with the microtubule lattice. Here, we show that removal of the Ndc80 tail, which compromises in vitro microtubule binding, has no effect on kinetochore-microtubule attachments in the Caenorhabditis elegans embryo. Despite this, preventing Aurora phosphorylation of the tail results in prematurely stable attachments that restrain spindle elongation. This premature stabilization requires the conserved microtubule-binding Ska complex, which enriches at attachment sites prior to anaphase onset to dampen chromosome motion. We propose that Ndc80-tail dephosphorylation promotes stabilization of kinetochore-microtubule attachments via the Ska complex and that this mechanism ensures accurate segregation by constraining chromosome motion following biorientation on the spindle.
[Mh] Termos MeSH primário: Proteínas de Caenorhabditis elegans/química
Proteínas de Caenorhabditis elegans/metabolismo
Caenorhabditis elegans/metabolismo
Cinetocoros/metabolismo
Proteínas Associadas aos Microtúbulos/química
Proteínas Associadas aos Microtúbulos/metabolismo
Microtúbulos/metabolismo
Complexos Multiproteicos/metabolismo
[Mh] Termos MeSH secundário: Anáfase
Animais
Cromossomos/metabolismo
Embrião não Mamífero/citologia
Embrião não Mamífero/metabolismo
Subunidades alfa de Proteínas de Ligação ao GTP/metabolismo
Deleção de Genes
Complexos Multiproteicos/química
Fosforilação
Ligação Proteica
Polos do Fuso/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Caenorhabditis elegans Proteins); 0 (GTP-Binding Protein alpha Subunits); 0 (Microtubule-Associated Proteins); 0 (Multiprotein Complexes); 0 (NDC-80 protein, C elegans)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170913
[Lr] Data última revisão:
170913
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170524
[St] Status:MEDLINE



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