Base de dados : MEDLINE
Pesquisa : G04.670 [Categoria DeCS]
Referências encontradas : 157 [refinar]
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[PMID]:28655762
[Au] Autor:Yadav PK; Rajasekharan R
[Ad] Endereço:From the Lipidomic Centre, Department of Lipid Science, and.
[Ti] Título:The m A methyltransferase Ime4 epitranscriptionally regulates triacylglycerol metabolism and vacuolar morphology in haploid yeast cells.
[So] Source:J Biol Chem;292(33):13727-13744, 2017 Aug 18.
[Is] ISSN:1083-351X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:-Methyladenosine (m A) is among the most common modifications in eukaryotic mRNA. The role of yeast m A methyltransferase, Ime4, in meiosis and sporulation in diploid strains is very well studied, but its role in haploid strains has remained unknown. Here, with the help of an immunoblotting strategy and Ime4-GFP protein localization studies, we establish the physiological role of Ime4 in haploid cells. Our data showed that Ime4 epitranscriptionally regulates triacylglycerol metabolism and vacuolar morphology through the long-chain fatty acyl-CoA synthetase Faa1, independently of the RNA methylation complex (MIS complex). The MIS complex consists of the Ime4, Mum2, and Slz1 proteins. Our affinity enrichment strategy (methylated RNA immunoprecipitation assays) using m A polyclonal antibodies coupled with mRNA isolation, quantitative real-time PCR, and standard PCR analyses confirmed the presence of m A-modified transcripts in haploid yeast cells. The term "epitranscriptional regulation" encompasses the RNA modification-mediated regulation of genes. Moreover, we demonstrate that the Aft2 transcription factor up-regulates expression. Because the m A methylation machinery is fundamentally conserved throughout eukaryotes, our findings will help advance the rapidly emerging field of RNA epitranscriptomics. The metabolic link identified here between m A methylation and triacylglycerol metabolism via the Ime4 protein provides new insights into lipid metabolism and the pathophysiology of lipid-related metabolic disorders, such as obesity. Because the yeast vacuole is an analogue of the mammalian lysosome, our findings pave the way to better understand the role of m A methylation in lysosome-related functions and diseases.
[Mh] Termos MeSH primário: Fator 2 Ativador da Transcrição/metabolismo
Coenzima A Ligases/metabolismo
Metiltransferases/metabolismo
Processamento Pós-Transcricional do RNA
Proteínas de Saccharomyces cerevisiae/metabolismo
Saccharomyces cerevisiae/fisiologia
Vacúolos/metabolismo
[Mh] Termos MeSH secundário: Fator 2 Ativador da Transcrição/genética
Substituição de Aminoácidos
Proteínas de Ciclo Celular/química
Proteínas de Ciclo Celular/genética
Proteínas de Ciclo Celular/metabolismo
Coenzima A Ligases/genética
Diploide
Epigênese Genética
Deleção de Genes
Regulação Fúngica da Expressão Gênica
Haploidia
Proteínas Luminescentes/genética
Proteínas Luminescentes/metabolismo
Metilação
Metiltransferases/química
Metiltransferases/genética
Microscopia Eletrônica de Varredura
Mutagênese Sítio-Dirigida
Mutação
Tamanho das Organelas
Proteínas Recombinantes de Fusão/metabolismo
Saccharomyces cerevisiae/genética
Saccharomyces cerevisiae/ultraestrutura
Proteínas de Saccharomyces cerevisiae/química
Proteínas de Saccharomyces cerevisiae/genética
Triglicerídeos/metabolismo
Vacúolos/ultraestrutura
[Pt] Tipo de publicação:COMPARATIVE STUDY; JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Activating Transcription Factor 2); 0 (Cell Cycle Proteins); 0 (Luminescent Proteins); 0 (Mum2 protein, S cerevisiae); 0 (Recombinant Fusion Proteins); 0 (Saccharomyces cerevisiae Proteins); 0 (Slz1 protein, S cerevisiae); 0 (Triglycerides); EC 2.1.1.- (Methyltransferases); EC 2.1.1.- (mRNA(adenine-N6)-methyltransferase); EC 6.2.1.- (Coenzyme A Ligases); EC 6.2.1.- (Faa1 protein, S cerevisiae)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170906
[Lr] Data última revisão:
170906
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170629
[St] Status:MEDLINE
[do] DOI:10.1074/jbc.M117.783761


  2 / 157 MEDLINE  
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[PMID]:27838812
[Au] Autor:Lounis MA; Lalonde S; Rial SA; Bergeron KF; Ralston JC; Mutch DM; Mounier C
[Ad] Endereço:Département des sciences biologiques et centre de recherche BioMed, Université du Québec à Montréal, Case Postale 8888, Succursale Centre-ville, Montréal, QC, H3C 3P8, Canada.
[Ti] Título:Hepatic BSCL2 (Seipin) Deficiency Disrupts Lipid Droplet Homeostasis and Increases Lipid Metabolism via SCD1 Activity.
[So] Source:Lipids;52(2):129-150, 2017 Feb.
[Is] ISSN:1558-9307
[Cp] País de publicação:Germany
[La] Idioma:eng
[Ab] Resumo:Berardinelli-Seip congenital lipodystrophy (BSCL) is an autosomal recessive disorder. The more severe form, designated BSCL2, arises due to mutations in the BSCL2 gene. Patients with BSCL2, as well as Bscl2 mice, have a near total absence of body fat, an organomegaly, and develop metabolic disorders including insulin resistance and hepatic steatosis. The function of the Seipin (BSCL2) protein remains poorly understood. Several lines of evidence have indicated that Seipin may have distinct functions in adipose versus non-adipose cells. Here we present evidence that BSCL2/Bscl2 plays a role in lipid droplet (LD) biogenesis and homeostasis in primary and cultured hepatocytes. Our results show that decreasing BSCL2/Bscl2 expression in hepatocytes increases the number and size of LD, as well as the expression of genes implicated in their formation and stability. We also show that knocking down SCD1 expression reverses the phenotype associated with Seipin deficiency. Interestingly, BSCL2 knockdown induces SCD1 expression and activity, potentially leading to increased basal phosphorylation of proteins involved in the insulin signaling cascade, as well as further increasing fatty acid uptake and de novo lipogenesis. In conclusion, our results suggest that a hepatic BSCL2/Bscl2 deficiency induces the increase and expansion of LD, potentially via increased SCD1 activity.
[Mh] Termos MeSH primário: Subunidades gama da Proteína de Ligação ao GTP/deficiência
Hepatócitos/citologia
Gotículas Lipídicas/metabolismo
Metabolismo dos Lipídeos
Estearoil-CoA Dessaturase/genética
[Mh] Termos MeSH secundário: Animais
Técnicas de Introdução de Genes
Técnicas de Silenciamento de Genes
Células Hep G2
Hepatócitos/metabolismo
Homeostase
Seres Humanos
Insulina/metabolismo
Tamanho das Organelas
Fosforilação
Ratos
Estearoil-CoA Dessaturase/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (BSCL2 protein, human); 0 (GTP-Binding Protein gamma Subunits); 0 (Insulin); EC 1.14.19.1 (SCD1 protein, human); EC 1.14.19.1 (Stearoyl-CoA Desaturase)
[Em] Mês de entrada:1707
[Cu] Atualização por classe:171105
[Lr] Data última revisão:
171105
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161114
[St] Status:MEDLINE
[do] DOI:10.1007/s11745-016-4210-5


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[PMID]:26961980
[Au] Autor:Luks L; Sacchi S; Pollegioni L; Dietrich DR
[Ad] Endereço:Human and Environmental Toxicology, University of Konstanz, Universitätsstrasse 10, 78457, Constance, Germany.
[Ti] Título:Novel insights into renal D-amino acid oxidase accumulation: propiverine changes DAAO localization and peroxisomal size in vivo.
[So] Source:Arch Toxicol;91(1):427-437, 2017 Jan.
[Is] ISSN:1432-0738
[Cp] País de publicação:Germany
[La] Idioma:eng
[Ab] Resumo:Chronic exposure to propiverine, a frequently prescribed pharmaceutical for treatment of overactive bladder and incontinence, provokes massive protein accumulation in the cytosol and nucleus of renal proximal tubule epithelial cells in rats. Previously, the accumulating protein was identified as D-amino acid oxidase (DAAO), a peroxisomal flavoenzyme expressed in kidney, liver and brain. The cellular mechanism of propiverine-induced DAAO accumulation, however, remains unexplained and poorly characterized. Therefore, to further increase the understanding of DAAO accumulation in rat kidney, this study aimed to characterize DAAO accumulations using differential immunofluorescent staining of rat kidney sections as well as in vitro binding analyses and proteasomal activity studies. We demonstrated that propiverine is neither a ligand of DAAO nor an inhibitor of the proteasome in vitro. However, propiverine treatment resulted in a significant decrease of peroxisomal size in rat proximal tubule epithelial cells. Moreover, peroxisomal catalase also accumulated in the cytosol and nuclei of propiverine-treated rats concurrently with DAAO. Taken together, our study indicates that propiverine treatment affects the trafficking and/or degradation of peroxisomal proteins such as DAAO and catalase by a so far unique and unknown mechanism.
[Mh] Termos MeSH primário: Benzilatos/efeitos adversos
Antagonistas Colinérgicos/efeitos adversos
D-Aminoácido Oxidase/metabolismo
Túbulos Renais Proximais/efeitos dos fármacos
Peroxissomos/efeitos dos fármacos
Agentes Urológicos/efeitos adversos
[Mh] Termos MeSH secundário: Animais
Benzilatos/administração & dosagem
Catalase/metabolismo
Núcleo Celular/efeitos dos fármacos
Núcleo Celular/enzimologia
Núcleo Celular/metabolismo
Antagonistas Colinérgicos/administração & dosagem
Citosol/efeitos dos fármacos
Citosol/enzimologia
Citosol/metabolismo
D-Aminoácido Oxidase/química
D-Aminoácido Oxidase/genética
Relação Dose-Resposta a Droga
Estabilidade Enzimática/efeitos dos fármacos
Feminino
Seres Humanos
Túbulos Renais Proximais/citologia
Túbulos Renais Proximais/enzimologia
Masculino
Camundongos
Tamanho das Organelas/efeitos dos fármacos
Peroxissomos/metabolismo
Transporte Proteico/efeitos dos fármacos
Ratos
Ratos Endogâmicos F344
Proteínas Recombinantes/química
Proteínas Recombinantes/metabolismo
Testes de Toxicidade Crônica
Agentes Urológicos/administração & dosagem
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Benzilates); 0 (Cholinergic Antagonists); 0 (Recombinant Proteins); 0 (Urological Agents); 468GE2241L (propiverine); EC 1.11.1.6 (Catalase); EC 1.4.3.3 (D-Amino-Acid Oxidase)
[Em] Mês de entrada:1703
[Cu] Atualização por classe:170817
[Lr] Data última revisão:
170817
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160311
[St] Status:MEDLINE
[do] DOI:10.1007/s00204-016-1685-z


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[PMID]:27480804
[Au] Autor:Malacrida L; Astrada S; Briva A; Bollati-Fogolín M; Gratton E; Bagatolli LA
[Ad] Endereço:Área de Investigación Respiratoria, Departamento de Fisiopatología, Hospital de Clínicas, Facultad de Medicina, Universidad de la República, Uruguay; Unidad de Bioquímica y Proteómica Analítica, Institut Pasteur de Montevideo, Uruguay; Laboratory for Fluorescence Dynamics, Biomedical Engineering Dep
[Ti] Título:Spectral phasor analysis of LAURDAN fluorescence in live A549 lung cells to study the hydration and time evolution of intracellular lamellar body-like structures.
[So] Source:Biochim Biophys Acta;1858(11):2625-2635, 2016 11.
[Is] ISSN:0006-3002
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:Using LAURDAN spectral imaging and spectral phasor analysis we concurrently studied the growth and hydration state of subcellular organelles (lamellar body-like, LB-like) from live A549 lung cancer cells at different post-confluence days. Our results reveal a time dependent two-step process governing the size and hydration of these intracellular LB-like structures. Specifically, a first step (days 1 to 7) is characterized by an increase in their size, followed by a second one (days 7 to 14) where the organelles display a decrease in their global hydration properties. Interestingly, our results also show that their hydration properties significantly differ from those observed in well-characterized artificial lamellar model membranes, challenging the notion that a pure lamellar membrane organization is present in these organelles at intracellular conditions. Finally, these LB-like structures show a significant increase in their hydration state upon secretion, suggesting a relevant role of entropy during this process.
[Mh] Termos MeSH primário: 2-Naftilamina/análogos & derivados
Corantes Fluorescentes/química
Membranas Intracelulares/metabolismo
Lauratos/química
Organelas/metabolismo
Água/metabolismo
[Mh] Termos MeSH secundário: 2-Naftilamina/química
Células A549
Transporte Biológico
Entropia
Seres Humanos
Membranas Intracelulares/ultraestrutura
Tamanho das Organelas
Organelas/ultraestrutura
Concentração Osmolar
Espectrometria de Fluorescência
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Fluorescent Dyes); 0 (Laurates); 059QF0KO0R (Water); CKR7XL41N4 (2-Naphthylamine); Y97FBL93VW (laurdan)
[Em] Mês de entrada:1706
[Cu] Atualização por classe:171101
[Lr] Data última revisão:
171101
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160803
[St] Status:MEDLINE


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[PMID]:27252384
[Au] Autor:Desfougères Y; Neumann H; Mayer A
[Ad] Endereço:Département de Biochimie, Université de Lausanne, Chemin des Boveresses 155, Epalinges 1066, Switzerland.
[Ti] Título:Organelle size control - increasing vacuole content activates SNAREs to augment organelle volume through homotypic fusion.
[So] Source:J Cell Sci;129(14):2817-28, 2016 Jul 15.
[Is] ISSN:1477-9137
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Cells control the size of their compartments relative to cell volume, but there is also size control within each organelle. Yeast vacuoles neither burst nor do they collapse into a ruffled morphology, indicating that the volume of the organellar envelope is adjusted to the amount of content. It is poorly understood how this adjustment is achieved. We show that the accumulating content of yeast vacuoles activates fusion of other vacuoles, thus increasing the volume-to-surface ratio. Synthesis of the dominant compound stored inside vacuoles, polyphosphate, stimulates binding of the chaperone Sec18/NSF to vacuolar SNAREs, which activates them and triggers fusion. SNAREs can only be activated by lumenal, not cytosolic, polyphosphate (polyP). Control of lumenal polyP over SNARE activation in the cytosol requires the cytosolic cyclin-dependent kinase Pho80-Pho85 and the R-SNARE Nyv1. These results suggest that cells can adapt the volume of vacuoles to their content through feedback from the vacuole lumen to the SNAREs on the cytosolic surface of the organelle.
[Mh] Termos MeSH primário: Fusão de Membrana
Tamanho das Organelas
Proteínas SNARE/metabolismo
Proteínas de Saccharomyces cerevisiae/metabolismo
Saccharomyces cerevisiae/metabolismo
Vacúolos/metabolismo
[Mh] Termos MeSH secundário: Citosol/metabolismo
Modelos Biológicos
Polifosfatos/metabolismo
Ligação Proteica
Proteínas de Transporte Vesicular/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Polyphosphates); 0 (SNARE Proteins); 0 (Saccharomyces cerevisiae Proteins); 0 (Vesicular Transport Proteins)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170804
[Lr] Data última revisão:
170804
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160603
[St] Status:MEDLINE
[do] DOI:10.1242/jcs.184382


  6 / 157 MEDLINE  
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[PMID]:27030912
[Au] Autor:Meier I; Griffis AH; Groves NR; Wagner A
[Ad] Endereço:Department of Molecular Genetics, The Ohio State University, 520 Aronoff Laboratory, 318 West 12th Avenue, Columbus, OH 43210, USA. Electronic address: meier.56@osu.edu.
[Ti] Título:Regulation of nuclear shape and size in plants.
[So] Source:Curr Opin Cell Biol;40:114-123, 2016 Jun.
[Is] ISSN:1879-0410
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Nuclear shape and size changes have long been used by cytopathologists to diagnose, stage, and prognose cancer. However, the underlying causalities and molecular mechanisms are largely unknown. The current eukaryotic tree of life groups eukaryotes into five supergroups, with all organisms between humans and yeast falling into the supergroup Opisthokonta. The emergence of model organisms with strong molecular genetic methodology in the other supergroups has recently facilitated a broader evolutionary approach to pressing biological questions. Here, we review what is known about the control of nuclear shape and size in the Archaeplastidae, the supergroup containing the higher plants. We discuss common themes as well as differences toward a more generalized model of how eukaryotic organisms regulate nuclear morphology.
[Mh] Termos MeSH primário: Núcleo Celular
Células Vegetais/metabolismo
[Mh] Termos MeSH secundário: Evolução Biológica
Forma do Núcleo Celular
Células Eucarióticas/classificação
Células Eucarióticas/citologia
Proteínas Nucleares/metabolismo
Tamanho das Organelas
Proteínas de Plantas/metabolismo
Plantas/genética
Plantas/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (Nuclear Proteins); 0 (Plant Proteins)
[Em] Mês de entrada:1705
[Cu] Atualização por classe:170729
[Lr] Data última revisão:
170729
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160401
[St] Status:MEDLINE


  7 / 157 MEDLINE  
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[PMID]:27003693
[Au] Autor:Ma TH; Lee LW; Lee CC; Yi YH; Chan SP; Tan BC; Lo SJ
[Ad] Endereço:a Department of Biomedical Sciences, College of Medicine , Chang Gung University , TaoYuan , Taiwan.
[Ti] Título:Genetic control of nucleolar size: An evolutionary perspective.
[So] Source:Nucleus;7(2):112-20, 2016 Apr 25.
[Is] ISSN:1949-1042
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Exploiting a C. elegans mutant (ncl-1) exhibiting nucleolar abnormalities, we recently identified the let-7/ncl-1/fib-1 genetic cascade underlying proper rRNA abundance and nucleolar size. These 3 factors, let-7 (a miRNA), NCL-1 (a member of the TRIM-NHL family), and fibrillarin (a nucleolar methyltransferase), are evolutionarily conserved across metazoans. In this article, we provide several lines of bioinformatic evidence showing that human and Drosophila homologues of C. elegans NCL-1, TRIM-71 and Brat, respectively, likely act as translational suppressors of fibrillarin. Moreover, since their 3'-UTRs contain putative target sites, they may also be under the control of the let-7 miRNA. We hypothesize that let-7, TRIM and fibrillarin contribute activities in concert, and constitute a conserved network controlling nucleolar size in eukaryotes. We provide an in-depth literature review of various molecular pathways, including the let-7/ncl-1/fib-1 genetic cascade, implicated in the regulation of nucleolar size.
[Mh] Termos MeSH primário: Nucléolo Celular
Evolução Molecular
Tamanho das Organelas/genética
[Mh] Termos MeSH secundário: Animais
Caenorhabditis elegans/citologia
Caenorhabditis elegans/genética
Proteínas de Caenorhabditis elegans/genética
Proteínas de Caenorhabditis elegans/metabolismo
Seres Humanos
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (Caenorhabditis elegans Proteins)
[Em] Mês de entrada:1705
[Cu] Atualização por classe:170512
[Lr] Data última revisão:
170512
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160323
[St] Status:MEDLINE
[do] DOI:10.1080/19491034.2016.1166322


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[PMID]:26940517
[Au] Autor:Vukovic LD; Jevtic P; Edens LJ; Levy DL
[Ad] Endereço:Department of Molecular Biology, University of Wyoming, Laramie, WY, United States of America.
[Ti] Título:New Insights into Mechanisms and Functions of Nuclear Size Regulation.
[So] Source:Int Rev Cell Mol Biol;322:1-59, 2016.
[Is] ISSN:1937-6448
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:Nuclear size is generally maintained within a defined range in a given cell type. Changes in cell size that occur during cell growth, development, and differentiation are accompanied by dynamic nuclear size adjustments in order to establish appropriate nuclear-to-cytoplasmic volume relationships. It has long been recognized that aberrations in nuclear size are associated with certain disease states, most notably cancer. Nuclear size and morphology must impact nuclear and cellular functions. Understanding these functional implications requires an understanding of the mechanisms that control nuclear size. In this review, we first provide a general overview of the diverse cellular structures and activities that contribute to nuclear size control, including structural components of the nucleus, effects of DNA amount and chromatin compaction, signaling, and transport pathways that impinge on the nucleus, extranuclear structures, and cell cycle state. We then detail some of the key mechanistic findings about nuclear size regulation that have been gleaned from a variety of model organisms. Lastly, we review studies that have implicated nuclear size in the regulation of cell and nuclear function and speculate on the potential functional significance of nuclear size in chromatin organization, gene expression, nuclear mechanics, and disease. With many fundamental cell biological questions remaining to be answered, the field of nuclear size regulation is still wide open.
[Mh] Termos MeSH primário: Ciclo Celular
Núcleo Celular/metabolismo
Cromatina/metabolismo
Regulação da Expressão Gênica
Tamanho das Organelas
Transdução de Sinais
[Mh] Termos MeSH secundário: Transporte Ativo do Núcleo Celular
Animais
Citoplasma/metabolismo
Seres Humanos
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL; RESEARCH SUPPORT, NON-U.S. GOV'T; REVIEW
[Nm] Nome de substância:
0 (Chromatin)
[Em] Mês de entrada:1612
[Cu] Atualização por classe:161230
[Lr] Data última revisão:
161230
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160305
[St] Status:MEDLINE


  9 / 157 MEDLINE  
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[PMID]:26845335
[Au] Autor:Harding CR; Egarter S; Gow M; Jiménez-Ruiz E; Ferguson DJ; Meissner M
[Ad] Endereço:Wellcome Trust Centre for Molecular Parasitology, Institute of Infection, Immunity & Inflammation, College of Medical, Veterinary and Life Sciences, University of Glasgow, Glasgow, United Kingdom.
[Ti] Título:Gliding Associated Proteins Play Essential Roles during the Formation of the Inner Membrane Complex of Toxoplasma gondii.
[So] Source:PLoS Pathog;12(2):e1005403, 2016 Feb.
[Is] ISSN:1553-7374
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The inner membrane complex (IMC) of apicomplexan parasites is a specialised structure localised beneath the parasite's plasma membrane, and is important for parasite stability and intracellular replication. Furthermore, it serves as an anchor for the myosin A motor complex, termed the glideosome. While the role of this protein complex in parasite motility and host cell invasion has been well described, additional roles during the asexual life cycle are unknown. Here, we demonstrate that core elements of the glideosome, the gliding associated proteins GAP40 and GAP50 as well as members of the GAPM family, have critical roles in the biogenesis of the IMC during intracellular replication. Deletion or disruption of these genes resulted in the rapid collapse of developing parasites after initiation of the cell cycle and led to redistribution of other glideosome components.
[Mh] Termos MeSH primário: Membrana Celular/metabolismo
Vesículas Citoplasmáticas/metabolismo
Proteínas de Membrana/metabolismo
Biogênese de Organelas
Proteínas de Protozoários/metabolismo
Toxoplasma/fisiologia
[Mh] Termos MeSH secundário: Biomarcadores/metabolismo
Linhagem Celular
Membrana Celular/ultraestrutura
Vesículas Citoplasmáticas/ultraestrutura
Técnicas de Inativação de Genes
Seres Humanos
Proteínas Luminescentes/genética
Proteínas Luminescentes/metabolismo
Proteínas de Membrana/genética
Microscopia Eletrônica de Transmissão
Microscopia de Vídeo
Tamanho das Organelas
Organismos Geneticamente Modificados
Isoformas de Proteínas/genética
Isoformas de Proteínas/metabolismo
Transporte Proteico
Proteínas de Protozoários/genética
Proteínas Recombinantes de Fusão/genética
Proteínas Recombinantes de Fusão/metabolismo
Proteínas Recombinantes/genética
Proteínas Recombinantes/metabolismo
Reprodução Assexuada
Toxoplasma/crescimento & desenvolvimento
Toxoplasma/ultraestrutura
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Biomarkers); 0 (Luminescent Proteins); 0 (Membrane Proteins); 0 (Protein Isoforms); 0 (Protozoan Proteins); 0 (Recombinant Fusion Proteins); 0 (Recombinant Proteins)
[Em] Mês de entrada:1607
[Cu] Atualização por classe:161019
[Lr] Data última revisão:
161019
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160205
[St] Status:MEDLINE
[do] DOI:10.1371/journal.ppat.1005403


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[PMID]:26787463
[Au] Autor:Mierzejewska J; Chreptowicz K
[Ad] Endereço:Department of Drug Technology and Biotechnology, Institute of Biotechnology, Faculty of Chemistry, Warsaw University of Technology, Warsaw, Poland.
[Ti] Título:Lack of Maf1 enhances pyruvate kinase activity and fermentative metabolism while influencing lipid homeostasis in Saccharomyces cerevisiae.
[So] Source:FEBS Lett;590(1):93-100, 2016 Jan.
[Is] ISSN:1873-3468
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:The Maf1 protein is a general negative repressor of RNA polymerase III, which is conserved in eukaryotes from yeast to humans. Herein, we show the yeast maf1Δ mutant increases pyruvate kinase activity, the key enzyme in glycolysis and an important player in switching between fermentative and oxidative metabolism. We observed enhanced ethanol production and elevated lipid content in the maf1Δ strain grown on glucose. However, after shifting to a non-fermentable carbon source, the opposite effect was observed, and the mutant cells accumulated smaller lipid droplets. Thus, it has been concluded that the Maf1 protein is essential for regulation of glucose metabolism and lipid homeostasis.
[Mh] Termos MeSH primário: Glicólise
Homeostase
Metabolismo dos Lipídeos
Mutação
Piruvato Quinase/metabolismo
Proteínas de Saccharomyces cerevisiae/metabolismo
Saccharomyces cerevisiae/fisiologia
Fatores de Transcrição/metabolismo
[Mh] Termos MeSH secundário: Western Blotting
Etanol/metabolismo
Fermentação
Deleção de Genes
Glucose/metabolismo
Glicerol/metabolismo
Cinética
Gotículas Lipídicas/metabolismo
Tamanho das Organelas
Oxirredução
Proteínas Recombinantes/metabolismo
Saccharomyces cerevisiae/citologia
Saccharomyces cerevisiae/crescimento & desenvolvimento
Proteínas de Saccharomyces cerevisiae/genética
Fatores de Transcrição/genética
[Pt] Tipo de publicação:COMPARATIVE STUDY; JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (MAF1 protein, S cerevisiae); 0 (Recombinant Proteins); 0 (Saccharomyces cerevisiae Proteins); 0 (Transcription Factors); 3K9958V90M (Ethanol); EC 2.7.1.40 (Pyruvate Kinase); IY9XDZ35W2 (Glucose); PDC6A3C0OX (Glycerol)
[Em] Mês de entrada:1608
[Cu] Atualização por classe:160120
[Lr] Data última revisão:
160120
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160121
[St] Status:MEDLINE
[do] DOI:10.1002/1873-3468.12033



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