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[PMID]: 28851706 [Au] Autor: Lane SIR; Morgan SL; Wu T; Collins JK; Merriman JA; ElInati E; Turner JM; Jones KT [Ad] Endereço: Biological Sciences, Faculty of Natural and Environmental Sciences, University of Southampton, Southampton, SO17 1BJ, UK Simon.Lane@soton.ac.uk K.T.Jones@soton.ac.uk. [Ti] Título: DNA damage induces a kinetochore-based ATM/ATR-independent SAC arrest unique to the first meiotic division in mouse oocytes. [So] Source: Development;144(19):3475-3486, 2017 10 01. [Is] ISSN: 1477-9129 [Cp] País de publicação: England [La] Idioma: eng [Ab] Resumo: Mouse oocytes carrying DNA damage arrest in meiosis I, thereby preventing creation of embryos with deleterious mutations. The arrest is dependent on activation of the spindle assembly checkpoint, which results in anaphase-promoting complex (APC) inhibition. However, little is understood about how this checkpoint is engaged following DNA damage. Here, we find that within minutes of DNA damage checkpoint proteins are assembled at the kinetochore, not at damage sites along chromosome arms, such that the APC is fully inhibited within 30 min. Despite this robust response, there is no measurable loss in k-fibres, or tension across the bivalent. Through pharmacological inhibition we observed that the response is dependent on Mps1 kinase, aurora kinase and Haspin. Using oocyte-specific knockouts we find the response does not require the DNA damage response kinases ATM or ATR. Furthermore, checkpoint activation does not occur in response to DNA damage in fully mature eggs during meiosis II, despite the divisions being separated by just a few hours. Therefore, mouse oocytes have a unique ability to sense DNA damage rapidly by activating the checkpoint at their kinetochores. [Mh] Termos MeSH primário: Proteínas Mutadas de Ataxia Telangiectasia/metabolismo Dano ao DNA Cinetocoros/metabolismo Pontos de Checagem da Fase M do Ciclo Celular Meiose Oócitos/citologia Oócitos/metabolismo [Mh] Termos MeSH secundário: Ciclossomo-Complexo Promotor de Anáfase/metabolismo Animais Aurora Quinases/metabolismo Centrômero/efeitos dos fármacos Centrômero/metabolismo Peptídeos e Proteínas de Sinalização Intracelular/metabolismo Cinetocoros/efeitos dos fármacos Pontos de Checagem da Fase M do Ciclo Celular/efeitos dos fármacos Meiose/efeitos dos fármacos Camundongos Modelos Biológicos Oócitos/efeitos dos fármacos Inibidores de Proteínas Quinases/farmacologia Proteínas Serina-Treonina Quinases/metabolismo [Pt] Tipo de publicação: JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T [Nm] Nome de substância: 0 (Gsg2 protein, mouse); 0 (Intracellular Signaling Peptides and Proteins); 0 (Protein Kinase Inhibitors); EC 2.3.2.27 (Anaphase-Promoting Complex-Cyclosome); EC 2.7.1.- (Atr protein, mouse); EC 2.7.1.- (Ttk protein, mouse); EC 2.7.11.1 (Ataxia Telangiectasia Mutated Proteins); EC 2.7.11.1 (Aurora Kinases); EC 2.7.11.1 (Protein-Serine-Threonine Kinases) [Em] Mês de entrada: 1710 [Cu] Atualização por classe: 171126 [Lr] Data última revisão: 171126 [Sb] Subgrupo de revista: IM [Da] Data de entrada para processamento: 170831 [St] Status: MEDLINE [do] DOI: 10.1242/dev.153965

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[PMID]: 28698300 [Au] Autor: Kim T; Lara-Gonzalez P; Prevo B; Meitinger F; Cheerambathur DK; Oegema K; Desai A [Ad] Endereço: Ludwig Institute for Cancer Research, San Diego, California 92093, USA. [Ti] Título: Kinetochores accelerate or delay APC/C activation by directing Cdc20 to opposing fates. [So] Source: Genes Dev;31(11):1089-1094, 2017 Jun 01. [Is] ISSN: 1549-5477 [Cp] País de publicação: United States [La] Idioma: eng [Ab] Resumo: Mitotic duration is determined by activation of the anaphase-promoting complex/cyclosome (APC/C) bound to its coactivator, Cdc20. Kinetochores, the microtubule-interacting machines on chromosomes, restrain mitotic exit when not attached to spindle microtubules by generating a Cdc20-containing complex that inhibits the APC/C. Here, we show that flux of Cdc20 through kinetochores also accelerates mitotic exit by promoting its dephosphorylation by kinetochore-localized protein phosphatase 1, which allows Cdc20 to activate the APC/C. Both APC/C activation and inhibition depend on Cdc20 fluxing through the same binding site at kinetochores. The microtubule attachment status of kinetochores therefore optimizes mitotic duration by controlling the balance between opposing Cdc20 fates. [Mh] Termos MeSH primário: Ciclossomo-Complexo Promotor de Anáfase/genética Proteínas Cdc20/metabolismo Cinetocoros/metabolismo Ativação Transcricional [Mh] Termos MeSH secundário: Animais Caenorhabditis elegans/enzimologia Caenorhabditis elegans/genética Proteínas Cdc20/genética Fosforilação Ligação Proteica Proteína Fosfatase 1/metabolismo [Pt] Tipo de publicação: JOURNAL ARTICLE [Nm] Nome de substância: 0 (Cdc20 Proteins); EC 2.3.2.27 (Anaphase-Promoting Complex-Cyclosome); EC 3.1.3.16 (Protein Phosphatase 1) [Em] Mês de entrada: 1710 [Cu] Atualização por classe: 171025 [Lr] Data última revisão: 171025 [Sb] Subgrupo de revista: IM [Da] Data de entrada para processamento: 170713 [St] Status: MEDLINE [do] DOI: 10.1101/gad.302067.117

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[PMID]: 28604743 [Au] Autor: Garzón J; Rodríguez R; Kong Z; Chabes A; Rodríguez-Acebes S; Méndez J; Moreno S; García-Higuera I [Ad] Endereço: Instituto de Biología Funcional y Genómica (IBFG)-CSIC, Salamanca University, Salamanca, Spain. [Ti] Título: Shortage of dNTPs underlies altered replication dynamics and DNA breakage in the absence of the APC/C cofactor Cdh1. [So] Source: Oncogene;36(42):5808-5818, 2017 Oct 19. [Is] ISSN: 1476-5594 [Cp] País de publicação: England [La] Idioma: eng [Ab] Resumo: The APC/C-Cdh1 ubiquitin-ligase complex targets cell cycle regulators for proteosomal degradation and helps prevent tumor development and accumulation of chromosomal aberrations. Replication stress has been proposed to be the main driver of genomic instability in the absence of Cdh1, but the real contribution of APC/C-Cdh1 to efficient replication, especially in normal cells, remains unclear. Here we show that, in primary MEFs, acute depletion or permanent ablation of Cdh1 slowed down replication fork movement and increased origin activity. Partial inhibition of origin firing does not accelerate replication forks, suggesting that fork progression is intrinsically limited in the absence of Cdh1. Moreover, exogenous supply of nucleotide precursors, or ectopic overexpression of RRM2, the regulatory subunit of Ribonucleotide Reductase, restore replication efficiency, indicating that dNTP availability could be impaired upon Cdh1 loss. Indeed, we found reduced dNTP levels in Cdh1-deficient MEFs. Importantly, DNA breakage is also significantly alleviated by increasing intracellular dNTP pools, strongly suggesting that genomic instability is the result of aberrant replication. These observations highlight the relevance of APC/C-Cdh1 activity during G1 to ensure an adequate supply of dNTPs to the replisome, prevent replication stress and the resulting chromosomal breaks and, ultimately, suppress tumorigenesis. [Mh] Termos MeSH primário: Ciclossomo-Complexo Promotor de Anáfase/metabolismo Proteínas Cdh1/fisiologia Quebras de DNA Replicação do DNA Desoxirribonucleotídeos/metabolismo Fase G1 [Mh] Termos MeSH secundário: Animais Células Cultivadas Embrião de Mamíferos/citologia Embrião de Mamíferos/metabolismo Feminino Fibroblastos/citologia Fibroblastos/metabolismo Instabilidade Genômica Masculino Camundongos Camundongos Knockout Ribonucleosídeo Difosfato Redutase/metabolismo [Pt] Tipo de publicação: JOURNAL ARTICLE [Nm] Nome de substância: 0 (Cdh1 Proteins); 0 (Deoxyribonucleotides); 0 (Fzr1 protein, mouse); EC 1.17.4.- (ribonucleotide reductase M2); EC 1.17.4.1 (Ribonucleoside Diphosphate Reductase); EC 2.3.2.27 (Anaphase-Promoting Complex-Cyclosome) [Em] Mês de entrada: 1710 [Cu] Atualização por classe: 171024 [Lr] Data última revisão: 171024 [Sb] Subgrupo de revista: IM [Da] Data de entrada para processamento: 170613 [St] Status: MEDLINE [do] DOI: 10.1038/onc.2017.186

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[PMID]: 28446612 [Au] Autor: Chen H; Xu X; Wang G; Zhang B; Wang G; Xin G; Liu J; Jiang Q; Zhang H; Zhang C [Ad] Endereço: From the Ministry of Education Key Laboratory of Cell Proliferation and Differentiation and the State Key Laboratory of Membrane Biology, College of Life Sciences, Peking University, Beijing 100871, China. [Ti] Título: CDK4 protein is degraded by anaphase-promoting complex/cyclosome in mitosis and reaccumulates in early G phase to initiate a new cell cycle in HeLa cells. [So] Source: J Biol Chem;292(24):10131-10141, 2017 Jun 16. [Is] ISSN: 1083-351X [Cp] País de publicação: United States [La] Idioma: eng [Ab] Resumo: CDK4 regulates G /S phase transition in the mammalian cell cycle by phosphorylating retinoblastoma family proteins. However, the mechanism underlying the regulation of CDK4 activity is not fully understood. Here, we show that CDK4 protein is degraded by anaphase-promoting complex/cyclosome (APC/C) during metaphase-anaphase transition in HeLa cells, whereas its main regulator, cyclin D1, remains intact but is sequestered in cytoplasm. CDK4 protein reaccumulates in the following G phase and shuttles between the nucleus and the cytoplasm to facilitate the nuclear import of cyclin D1. Without CDK4, cyclin D1 cannot enter the nucleus. Point mutations that disrupt CDK4 and cyclin D1 interaction impair the nuclear import of cyclin D1 and the activity of CDK4. RNAi knockdown of CDK4 also induces cytoplasmic retention of cyclin D1 and G /G phase arrest of the cells. Collectively, our data demonstrate that CDK4 protein is degraded in late mitosis and reaccumulates in the following G phase to facilitate the nuclear import of cyclin D1 for activation of CKD4 to initiate a new cell cycle in HeLa cells. [Mh] Termos MeSH primário: Ciclossomo-Complexo Promotor de Anáfase/metabolismo Ciclina D1/metabolismo Quinase 4 Dependente de Ciclina/metabolismo Fase G1 Mitose [Mh] Termos MeSH secundário: Transporte Ativo do Núcleo Celular Animais Linhagem Celular Ciclina D1/química Ciclina D1/genética Quinase 4 Dependente de Ciclina/antagonistas & inibidores Quinase 4 Dependente de Ciclina/química Quinase 4 Dependente de Ciclina/genética Indução Enzimática Estabilidade Enzimática Proteínas de Fluorescência Verde/química Proteínas de Fluorescência Verde/genética Proteínas de Fluorescência Verde/metabolismo Células HeLa Seres Humanos Camundongos Proteínas de Neoplasias/química Proteínas de Neoplasias/genética Proteínas de Neoplasias/metabolismo Sinais de Localização Nuclear/química Sinais de Localização Nuclear/genética Sinais de Localização Nuclear/metabolismo Fragmentos de Peptídeos/antagonistas & inibidores Fragmentos de Peptídeos/química Fragmentos de Peptídeos/metabolismo Mutação Puntual Estabilidade Proteica Transporte Proteico Proteólise Interferência de RNA Proteínas Recombinantes de Fusão/química Proteínas Recombinantes de Fusão/metabolismo [Pt] Tipo de publicação: COMPARATIVE STUDY; JOURNAL ARTICLE [Nm] Nome de substância: 0 (CCND1 protein, human); 0 (Neoplasm Proteins); 0 (Nuclear Localization Signals); 0 (Peptide Fragments); 0 (Recombinant Fusion Proteins); 136601-57-5 (Cyclin D1); 147336-22-9 (Green Fluorescent Proteins); EC 2.3.2.27 (Anaphase-Promoting Complex-Cyclosome); EC 2.7.11.22 (CDK4 protein, human); EC 2.7.11.22 (Cyclin-Dependent Kinase 4) [Em] Mês de entrada: 1707 [Cu] Atualização por classe: 170714 [Lr] Data última revisão: 170714 [Sb] Subgrupo de revista: IM [Da] Data de entrada para processamento: 170428 [St] Status: MEDLINE [do] DOI: 10.1074/jbc.M116.773226

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[PMID]: 28376205 [Au] Autor: Kim SJ; Hyeong Lee T; Hee Nam S; Kim JH; Oh S; Sook Cho Y; Sup Lee M; Choi S; Lee PC [Ad] Endereço: Department of Biomedical Sciences, University of Ulsan College of Medicine, ASAN Medical Center, Seoul, Korea. [Ti] Título: Association of Uba6-Specific-E2 (USE1) With Lung Tumorigenesis. [So] Source: J Natl Cancer Inst;109(3):1-11, 2017 03 01. [Is] ISSN: 1460-2105 [Cp] País de publicação: United States [La] Idioma: eng [Ab] Resumo: Background: The UBA6-specific E2 conjugating enzyme 1 (USE1) ubiquitin enzyme cascade is a poorly characterized arm of the ubiquitin-proteasome system. We investigated whether the UBA6-USE1 enzyme cascade plays a role in lung cancer tumorigenesis. Methods: USE1 expression was assessed in tumor-normal paired samples from 106 lung cancer patients by immunoblot. USE1 was stably overexpressed and knocked down in lung cancer cell lines to evaluate cell proliferation, colony formation, and invasion. Xenograft models were used to determine the effects of USE1 on tumor growth (n = 7). Proteomics analysis was used to identify proteins interacting with USE1. The USE1 gene was sequenced in lung cancer patients, and missense mutations of USE1 were generated to evaluate its function. All statistical tests were two-sided. Results: USE1 proteins were frequently overexpressed in lung cancer patients (92.5%) Stable overexpression of USE1 increased cell proliferation ( P = .002), migration ( P < .001), and invasion ( P < .001), whereas knockdown of USE1 reduced cell proliferation ( P < .001), migration ( P = .003), and invasion in lung cancer cells and xenograft models ( P < .001). USE1 was found to have a conserved D-box domain, and the level of the protein was regulated by the anaphase-promoting complex. Several missense mutations in USE1 identified in patients prolong the stability of the protein. Conclusions: USE1 proteins are frequently overexpressed in lung cancer, and missense mutations in USE1 prolong the half-life of the protein, promoting tumor formation. Our findings reveal novel roles for USE1 in lung cancer and the possible use of USE1 as a novel biomarker and therapeutic target for lung cancer treatment. [Mh] Termos MeSH primário: Carcinogênese/metabolismo Neoplasias Pulmonares/metabolismo Enzimas Ativadoras de Ubiquitina/metabolismo Ubiquitinas/metabolismo [Mh] Termos MeSH secundário: Ciclossomo-Complexo Promotor de Anáfase Animais Caderinas/metabolismo Carcinogênese/genética Proteínas Cdc20/metabolismo Linhagem Celular Tumoral Movimento Celular Proliferação Celular Técnicas de Silenciamento de Genes Seres Humanos Pulmão/metabolismo Neoplasias Pulmonares/genética Neoplasias Pulmonares/patologia Masculino Camundongos Camundongos Endogâmicos BALB C Camundongos Nus Mutação de Sentido Incorreto Invasividade Neoplásica Transplante de Neoplasias Ensaio Tumoral de Célula-Tronco Ubiquitinas/genética [Pt] Tipo de publicação: JOURNAL ARTICLE [Nm] Nome de substância: 0 (CDH1 protein, human); 0 (Cadherins); 0 (Cdc20 Proteins); 0 (UBA6 protein, human); 0 (Ubiquitins); 0 (Use1 protein, human); 156288-95-8 (CDC20 protein, human); EC 2.3.2.27 (Anaphase-Promoting Complex-Cyclosome); EC 6.2.1.45 (Ubiquitin-Activating Enzymes) [Em] Mês de entrada: 1707 [Cu] Atualização por classe: 170718 [Lr] Data última revisão: 170718 [Sb] Subgrupo de revista: IM [Da] Data de entrada para processamento: 170405 [St] Status: MEDLINE [do] DOI: 10.1093/jnci/djw224

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[PMID]: 28358323 [Au] Autor: Yu H; Zhang Y; Zhang D; Lu Y; He H; Zheng F; Wang M [Ad] Endereço: Hainan Key Laboratory for Sustainable Utilization of Tropical Bioresource, Institute of Tropical Agriculture and Forestry, Hainan University, Haikou 570228, China. yuhaiyang@hainu.edu.cn. [Ti] Título: Identification of a Ribose-Phosphate Pyrophosphokinase that Can Interact In Vivo with the Anaphase Promoting Complex/Cyclosome. [So] Source: Int J Mol Sci;18(4), 2017 Mar 30. [Is] ISSN: 1422-0067 [Cp] País de publicação: Switzerland [La] Idioma: eng [Ab] Resumo: 5-Phospho-d-ribosyl-1-diphosphate (PRPP) synthase (PRS) catalyzes the biosynthesis of PRPP, which is an important compound of metabolism in most organisms. However, no genes have been cloned, let alone studied for their biological function in rubber tree. In this study, we identify a novel protein (PRS4) that interacts in vivo with rubber tree anaphase promoting complex/cyclosome (APC/C) subunit 10 (HbAPC10) by yeast two-hybrid assays. has been cloned from rubber tree and named as . Blastp search in the genome of showed that HbPRS4 shared the highest similarity with AtPRS4, with 80.71% identity. qRT-PCR was used to determine the expression of in different tissues and under various treatments. was preferentially expressed in the bark. Moreover, the expression level of was significantly induced by the proteasome inhibitor MG132 treatment, suggesting it might be regulated by the ubiquitin/26S proteasome pathway. The amount of transcript was obviously decreased after mechanical wounding and abscisic acid (ABA) treatments, while a slight increase was observed at 24 h after ABA treatment. transcript in the latex was significantly upregulated by ethephon (ET) and methyl jasmonate (MeJA) treatments. These results suggested that HbPRS4 may be a specific substrate of HbAPC10 indirectly regulating natural rubber biosynthesis in rubber tree. [Mh] Termos MeSH primário: Ciclossomo-Complexo Promotor de Anáfase/metabolismo Proteínas de Plantas/metabolismo Ribose-Fosfato Pirofosfoquinase/metabolismo [Mh] Termos MeSH secundário: Ácido Abscísico/farmacologia Acetatos/farmacologia Ciclopentanos/farmacologia Regulação da Expressão Gênica de Plantas/efeitos dos fármacos Hevea/genética Hevea/metabolismo Leupeptinas/farmacologia Oxilipinas/farmacologia Casca de Planta/metabolismo Proteínas de Plantas/química Proteínas de Plantas/genética Ligação Proteica Ribose-Fosfato Pirofosfoquinase/química Ribose-Fosfato Pirofosfoquinase/genética [Pt] Tipo de publicação: JOURNAL ARTICLE [Nm] Nome de substância: 0 (Acetates); 0 (Cyclopentanes); 0 (Leupeptins); 0 (Oxylipins); 0 (Plant Proteins); 72S9A8J5GW (Abscisic Acid); 900N171A0F (methyl jasmonate); EC 2.3.2.27 (Anaphase-Promoting Complex-Cyclosome); EC 2.7.6.1 (Ribose-Phosphate Pyrophosphokinase); RF1P63GW3K (benzyloxycarbonylleucyl-leucyl-leucine aldehyde) [Em] Mês de entrada: 1704 [Cu] Atualização por classe: 170507 [Lr] Data última revisão: 170507 [Sb] Subgrupo de revista: IM [Da] Data de entrada para processamento: 170331 [St] Status: MEDLINE

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[PMID]: 28339487 [Au] Autor: Rai U; Najm F; Tartakoff AM [Ad] Endereço: Cell Biology Program/Department of Molecular and Microbiology, Case Western Reserve University, Cleveland, Ohio, United States of America. [Ti] Título: Nucleolar asymmetry and the importance of septin integrity upon cell cycle arrest. [So] Source: PLoS One;12(3):e0174306, 2017. [Is] ISSN: 1932-6203 [Cp] País de publicação: United States [La] Idioma: eng [Ab] Resumo: Cell cycle arrest can be imposed by inactivating the anaphase promoting complex (APC). In S. cerevisiae this arrest has been reported to stabilize a metaphase-like intermediate in which the nuclear envelope spans the bud neck, while chromatin repeatedly translocates between the mother and bud domains. The present investigation was undertaken to learn how other features of nuclear organization are affected upon depletion of the APC activator, Cdc20. We observe that the spindle pole bodies and the spindle repeatedly translocate across the narrow orifice at the level of the neck. Nevertheless, we find that the nucleolus (organized around rDNA repeats on the long right arm of chromosome XII) remains in the mother domain, marking the polarity of the nucleus. Accordingly, chromosome XII is polarized: TelXIIR remains in the mother domain and its centromere is predominantly located in the bud domain. In order to learn why the nucleolus remains in the mother domain, we studied the impact of inhibiting rRNA synthesis in arrested cells. We observed that this fragments the nucleolus and that these fragments entered the bud domain. Taken together with earlier observations, the restriction of the nucleolus to the mother domain therefore can be attributed to its massive structure. We also observed that inactivation of septins allowed arrested cells to complete the cell cycle, that the alternative APC activator, Cdh1, was required for completion of the cell cycle and that induction of Cdh1 itself caused arrested cells to progress to the end of the cell cycle. [Mh] Termos MeSH primário: Pontos de Checagem do Ciclo Celular/fisiologia Nucléolo Celular/metabolismo Saccharomyces cerevisiae/metabolismo Septinas/metabolismo [Mh] Termos MeSH secundário: Ciclossomo-Complexo Promotor de Anáfase/genética Ciclossomo-Complexo Promotor de Anáfase/metabolismo Saccharomyces cerevisiae/genética Proteínas de Saccharomyces cerevisiae/genética Proteínas de Saccharomyces cerevisiae/metabolismo Septinas/genética [Pt] Tipo de publicação: JOURNAL ARTICLE [Nm] Nome de substância: 0 (Saccharomyces cerevisiae Proteins); EC 2.3.2.27 (Anaphase-Promoting Complex-Cyclosome); EC 3.6.1.- (Septins) [Em] Mês de entrada: 1708 [Cu] Atualização por classe: 170825 [Lr] Data última revisão: 170825 [Sb] Subgrupo de revista: IM [Da] Data de entrada para processamento: 170325 [St] Status: MEDLINE [do] DOI: 10.1371/journal.pone.0174306

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[PMID]: 28298492 [Au] Autor: Heasley LR; Markus SM; DeLuca JG [Ad] Endereço: Biochemistry and Molecular Biology, Colorado State University, Fort Collins, CO 80523 jdeluca@colostate.edu steven.markus@colostate.edu lydia.heasley@colostate.edu. [Ti] Título: "Wait anaphase" signals are not confined to the mitotic spindle. [So] Source: Mol Biol Cell;28(9):1186-1194, 2017 May 01. [Is] ISSN: 1939-4586 [Cp] País de publicação: United States [La] Idioma: eng [Ab] Resumo: The spindle assembly checkpoint ensures the faithful inheritance of chromosomes by arresting mitotic progression in the presence of kinetochores that are not attached to spindle microtubules. This is achieved through inhibition of the anaphase-promoting complex/cyclosome by a kinetochore-derived "wait anaphase" signal known as the mitotic checkpoint complex. It remains unclear whether the localization and activity of these inhibitory complexes are restricted to the mitotic spindle compartment or are diffusible throughout the cytoplasm. Here we report that "wait anaphase" signals are indeed able to diffuse outside the confines of the mitotic spindle compartment. Using a cell fusion approach to generate multinucleate cells, we investigate the effects of checkpoint signals derived from one spindle compartment on a neighboring spindle compartment. We find that spindle compartments in close proximity wait for one another to align all chromosomes before entering anaphase synchronously. Synchrony is disrupted in cells with increased interspindle distances and cellular constrictions between spindle compartments. In addition, when mitotic cells are fused with interphase cells, "wait anaphase" signals are diluted, resulting in premature mitotic exit. Overall our studies reveal that anaphase inhibitors are diffusible and active outside the confines of the mitotic spindle from which they are derived. [Mh] Termos MeSH primário: Pontos de Checagem da Fase M do Ciclo Celular/fisiologia Fuso Acromático/genética [Mh] Termos MeSH secundário: Anáfase/fisiologia Ciclossomo-Complexo Promotor de Anáfase/genética Técnicas de Cultura de Células Pontos de Checagem do Ciclo Celular Proteínas de Ciclo Celular/genética Seres Humanos Cinetocoros/fisiologia Pontos de Checagem da Fase M do Ciclo Celular/genética Microtúbulos Mitose Proteínas Serina-Treonina Quinases/genética Fuso Acromático/fisiologia [Pt] Tipo de publicação: JOURNAL ARTICLE [Nm] Nome de substância: 0 (Cell Cycle Proteins); EC 2.3.2.27 (Anaphase-Promoting Complex-Cyclosome); EC 2.7.11.1 (Protein-Serine-Threonine Kinases) [Em] Mês de entrada: 1710 [Cu] Atualização por classe: 171003 [Lr] Data última revisão: 171003 [Sb] Subgrupo de revista: IM [Da] Data de entrada para processamento: 170317 [St] Status: MEDLINE [do] DOI: 10.1091/mbc.E17-01-0036

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[PMID]: 28260026 [Au] Autor: Wang R; Song Y; Liu X; Wang Q; Wang Y; Li L; Kang C; Zhang Q [Ad] Endereço: Department of Gastroenterology, Tianjin Medical University General Hospital, Tianjin 300052, P.R. China. [Ti] Título: UBE2C induces EMT through Wnt/ß­catenin and PI3K/Akt signaling pathways by regulating phosphorylation levels of Aurora-A. [So] Source: Int J Oncol;50(4):1116-1126, 2017 Apr. [Is] ISSN: 1791-2423 [Cp] País de publicação: Greece [La] Idioma: eng [Ab] Resumo: The ubiquitin-conjugating enzyme 2C (UBE2C) is the key component in the ubiquitin proteasome system (UPS) by partnering with the anaphase­promoting complex (APC/C). A high UBE2C protein expression level has been reported in various types of human tumors. However, little is known about the precise mechanism by which UBE2C expression is downregulated in gastric cancer. We found in MGC­803 and SGC­7901 gastric cancer cells UBE2C­deficient G2/M phase arrest in the cell cycle and subsequently decreased gastric adenocarcinoma tumorigenesis. In the previous study, we identified Aurora-A (AURKA) as the hub gene of the gastric cancer linkage network based genome­wide association study (eGWAS). Furthermore, knockdown of UBE2C using siRNA markedly reduced the level of phosphorylation AURKA (p­AURKA) via Wnt/ß­catenin and PI3K/Akt signaling pathways suppressed the occurrence and development of gastric cancer. Additionally, the expression of E­cadherin was up­regulated and N-cadherin was downregulated in response to UBE2C knockdown and inhibits epithelial-mesenchymal transition (EMT). Collectively, our data suggest that the activity of AURKA might be regulated by UBE2C through regulating the activity of APC/C. UBE2C may be a new marker in the diagnosis of gastric cancer and may be a potential therapeutic target for the treatment of gastric adenocarcinoma. [Mh] Termos MeSH primário: Ciclossomo-Complexo Promotor de Anáfase/metabolismo Aurora Quinase A/genética Transição Epitelial-Mesenquimal Regulação Neoplásica da Expressão Gênica Neoplasias Gástricas/genética Enzimas de Conjugação de Ubiquitina/metabolismo [Mh] Termos MeSH secundário: Antígenos CD/metabolismo Aurora Quinase A/metabolismo Caderinas/metabolismo Carcinogênese/metabolismo Linhagem Celular Tumoral Regulação para Baixo Pontos de Checagem da Fase G2 do Ciclo Celular Seres Humanos Fosfatidilinositol 3-Quinases/metabolismo Fosforilação Proteínas Proto-Oncogênicas c-akt/metabolismo Interferência de RNA RNA Interferente Pequeno Neoplasias Gástricas/metabolismo Enzimas de Conjugação de Ubiquitina/genética Via de Sinalização Wnt beta Catenina/metabolismo [Pt] Tipo de publicação: JOURNAL ARTICLE [Nm] Nome de substância: 0 (Antigens, CD); 0 (CDH1 protein, human); 0 (CDH2 protein, human); 0 (Cadherins); 0 (RNA, Small Interfering); 0 (beta Catenin); EC 2.3.2.23 (UBE2C protein, human); EC 2.3.2.23 (Ubiquitin-Conjugating Enzymes); EC 2.3.2.27 (Anaphase-Promoting Complex-Cyclosome); EC 2.7.1.- (Phosphatidylinositol 3-Kinases); EC 2.7.11.1 (AURKA protein, human); EC 2.7.11.1 (Aurora Kinase A); EC 2.7.11.1 (Proto-Oncogene Proteins c-akt) [Em] Mês de entrada: 1707 [Cu] Atualização por classe: 170717 [Lr] Data última revisão: 170717 [Sb] Subgrupo de revista: IM [Da] Data de entrada para processamento: 170306 [St] Status: MEDLINE [do] DOI: 10.3892/ijo.2017.3880

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[PMID]: 28245054 [Au] Autor: Chikashige Y; Yamane M; Okamasa K; Osakada H; Tsutsumi C; Nagahama Y; Fukuta N; Haraguchi T; Hiraoka Y [Ad] Endereço: Advanced ICT Research Institute Kobe, National Institute of Information and Communications Technology, Kobe, Japan. [Ti] Título: Fission yeast APC/C activators Slp1 and Fzr1 sequentially trigger two consecutive nuclear divisions during meiosis. [So] Source: FEBS Lett;591(7):1029-1040, 2017 Apr. [Is] ISSN: 1873-3468 [Cp] País de publicação: England [La] Idioma: eng [Ab] Resumo: In meiosis, two rounds of nuclear division occur consecutively without DNA replication between the divisions. We isolated a fission yeast mutant in which the nucleus divides only once to generate two spores, as opposed to four, in meiosis. In this mutant, we found that the initiation codon of the slp1 gene is converted to ATA, producing a reduced amount of Slp1. As a member of the Fizzy family of anaphase-promoting complex/cyclosome (APC/C) activators, Slp1 is essential for vegetative growth; however, the mutant allele shows a phenotype only in meiosis. Slp1 insufficiency delays degradation of maturation-promoting factor at the first meiotic division, and another APC/C activator, Fzr1, which acts late in meiosis, terminates meiosis immediately after the delayed first division to produce two viable spores. [Mh] Termos MeSH primário: Proteínas Cdc20/metabolismo Proteínas Cdh1/metabolismo Meiose Proteínas de Schizosaccharomyces pombe/metabolismo Schizosaccharomyces/metabolismo [Mh] Termos MeSH secundário: Ciclossomo-Complexo Promotor de Anáfase/metabolismo Western Blotting Proteínas Cdc20/genética Proteínas Cdh1/genética Divisão do Núcleo Celular/genética Microscopia de Fluorescência Mutação Schizosaccharomyces/genética Proteínas de Schizosaccharomyces pombe/genética Esporos Fúngicos/genética Esporos Fúngicos/metabolismo Fatores de Tempo [Pt] Tipo de publicação: LETTER [Nm] Nome de substância: 0 (Cdc20 Proteins); 0 (Cdh1 Proteins); 0 (Schizosaccharomyces pombe Proteins); 0 (slp1 protein, S pombe); EC 2.3.2.27 (Anaphase-Promoting Complex-Cyclosome) [Em] Mês de entrada: 1706 [Cu] Atualização por classe: 170601 [Lr] Data última revisão: 170601 [Sb] Subgrupo de revista: IM [Da] Data de entrada para processamento: 170301 [St] Status: MEDLINE [do] DOI: 10.1002/1873-3468.12612

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