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Pesquisa : D03.383.742.686.246.150.210 [Categoria DeCS]
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  1 / 195 MEDLINE  
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[PMID]:26946259
[Au] Autor:Chauhan N; Farine L; Pandey K; Menon AK; Bütikofer P
[Ad] Endereço:Department of Biochemistry, Weill Cornell Medical College, New York 10065, USA.
[Ti] Título:Lipid topogenesis--35years on.
[So] Source:Biochim Biophys Acta;1861(8 Pt B):757-766, 2016 Aug.
[Is] ISSN:0006-3002
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:Glycerophospholipids are the principal fabric of cellular membranes. The pathways by which these lipids are synthesized were elucidated mainly through the work of Kennedy and colleagues in the late 1950s and early 1960s. Subsequently, attention turned to cell biological aspects of lipids: Where in the cell are lipids synthesized? How are lipids integrated into membranes to form a bilayer? How are they sorted and transported from their site of synthesis to other cellular destinations? These topics, collectively termed 'lipid topogenesis', were the subject of a review article in 1981 by Bell, Ballas and Coleman. We now assess what has been learned about early events of lipid topogenesis, i.e. "lipid synthesis, the integration of lipids into membranes, and lipid translocation across membranes", in the 35 years since the publication of this important review. We highlight the recent elucidation of the X-ray structures of key membrane enzymes of glycerophospholipid synthesis, progress on identifying lipid scramblase proteins needed to equilibrate lipids across membranes, and new complexities in the subcellular location and membrane topology of phosphatidylinositol synthesis revealed through a comparison of two unicellular model eukaryotes. This article is part of a Special Issue entitled: The cellular lipid landscape edited by Tim P. Levine and Anant K. Menon.
[Mh] Termos MeSH primário: Membrana Celular/metabolismo
Glicerofosfolipídeos/biossíntese
[Mh] Termos MeSH secundário: Animais
CDP-Diacilglicerol-Inositol 3-Fosfatidiltransferase/metabolismo
Membrana Celular/química
Diglicerídeos de Citidina Difosfato/biossíntese
Glicerofosfolipídeos/química
Seres Humanos
Bicamadas Lipídicas/metabolismo
Redes e Vias Metabólicas/fisiologia
Mitocôndrias/metabolismo
[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 (Cytidine Diphosphate Diglycerides); 0 (Glycerophospholipids); 0 (Lipid Bilayers); EC 2.7.8.11 (CDP-Diacylglycerol-Inositol 3-Phosphatidyltransferase)
[Em] Mês de entrada:1608
[Cu] Atualização por classe:170812
[Lr] Data última revisão:
170812
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160307
[St] Status:MEDLINE


  2 / 195 MEDLINE  
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[PMID]:26552690
[Au] Autor:Waugh MG
[Ad] Endereço:School of Life and Medical Sciences, University College London, Royal Free Campus, Rowland Hill Street, London, NW3 2PF, UK. m.waugh@ucl.ac.uk.
[Ti] Título:Assay for CDP-Diacylglycerol Generation by CDS in Membrane Fractions.
[So] Source:Methods Mol Biol;1376:247-54, 2016.
[Is] ISSN:1940-6029
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:CDP-DAG is a liponucleotide formed by the condensation of CTP with the phospholipid phosphatidic acid in a reaction catalyzed by CDP-DAG synthase (CDS). CDP-DAG is required for the synthesis of phosphatidylinositol; the parent molecule whence all seven phosphoinositides including the signaling molecules PI4P, PI(4,5)P2, and PI(3,4,5)P3 are derived. This protocol describes a highly sensitive radiometric assay to detect the generation of CDP-DAG on isolated biological membrane fractions.
[Mh] Termos MeSH primário: CDP-Diacilglicerol-Inositol 3-Fosfatidiltransferase/metabolismo
Membrana Celular/metabolismo
Diglicerídeos de Citidina Difosfato/biossíntese
[Mh] Termos MeSH secundário: Animais
Fracionamento Celular/métodos
Linhagem Celular
Cromatografia em Camada Delgada
Retículo Endoplasmático/metabolismo
Seres Humanos
Frações Subcelulares
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Cytidine Diphosphate Diglycerides); EC 2.7.8.11 (CDP-Diacylglycerol-Inositol 3-Phosphatidyltransferase)
[Em] Mês de entrada:1608
[Cu] Atualização por classe:151110
[Lr] Data última revisão:
151110
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:151111
[St] Status:MEDLINE
[do] DOI:10.1007/978-1-4939-3170-5_21


  3 / 195 MEDLINE  
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[PMID]:26149385
[Au] Autor:Sauerwald J; Jores T; Eisenberg-Bord M; Chuartzman SG; Schuldiner M; Rapaport D
[Ad] Endereço:Interfaculty Institute of Biochemistry, University of Tuebingen, Tuebingen, Germany.
[Ti] Título:Genome-Wide Screens in Saccharomyces cerevisiae Highlight a Role for Cardiolipin in Biogenesis of Mitochondrial Outer Membrane Multispan Proteins.
[So] Source:Mol Cell Biol;35(18):3200-11, 2015 Sep.
[Is] ISSN:1098-5549
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:A special group of mitochondrial outer membrane (MOM) proteins spans the membrane several times via multiple helical segments. Such multispan proteins are synthesized on cytosolic ribosomes before their targeting to mitochondria and insertion into the MOM. Previous work recognized the import receptor Tom70 and the mitochondrial import (MIM) complex, both residents of the MOM, as required for optimal biogenesis of these proteins. However, their involvement is not sufficient to explain either the entire import pathway or its regulation. To identify additional factors that are involved in the biogenesis of MOM multispan proteins, we performed complementary high-throughput visual and growth screens in Saccharomyces cerevisiae. Cardiolipin (CL) synthase (Crd1) appeared as a candidate in both screens. Our results indeed demonstrate lower steady-state levels of the multispan proteins Ugo1, Scm4, and Om14 in mitochondria from crd1Δ cells. Importantly, MOM single-span proteins were not affected by this mutation. Furthermore, organelles lacking Crd1 had a lower in vitro capacity to import newly synthesized Ugo1 and Scm4 molecules. Crd1, which is located in the mitochondrial inner membrane, condenses phosphatidylglycerol together with CDP-diacylglycerol to obtain de novo synthesized CL molecules. Hence, our findings suggest that CL is an important component in the biogenesis of MOM multispan proteins.
[Mh] Termos MeSH primário: Cardiolipinas/biossíntese
Proteínas de Membrana/metabolismo
Membranas Mitocondriais/fisiologia
Saccharomyces cerevisiae/metabolismo
Transferases (Outros Grupos de Fosfato Substituídos)/metabolismo
[Mh] Termos MeSH secundário: Diglicerídeos de Citidina Difosfato/metabolismo
Regulação Fúngica da Expressão Gênica
Proteínas de Fluorescência Verde
Proteínas de Membrana/biossíntese
Proteínas de Transporte da Membrana Mitocondrial/biossíntese
Proteínas de Transporte da Membrana Mitocondrial/metabolismo
Proteínas Mitocondriais/biossíntese
Fosfatidilgliceróis/metabolismo
Transporte Proteico/fisiologia
Proteínas de Saccharomyces cerevisiae/biossíntese
Proteínas de Saccharomyces cerevisiae/metabolismo
Fatores de Transcrição/biossíntese
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Cardiolipins); 0 (Cytidine Diphosphate Diglycerides); 0 (Membrane Proteins); 0 (Mitochondrial Membrane Transport Proteins); 0 (Mitochondrial Proteins); 0 (OM14 protein, S cerevisiae); 0 (Phosphatidylglycerols); 0 (SCM4 protein, S cerevisiae); 0 (Saccharomyces cerevisiae Proteins); 0 (Transcription Factors); 0 (UGO1 protein, S cerevisiae); 147336-22-9 (Green Fluorescent Proteins); EC 2.7.8.- (Transferases (Other Substituted Phosphate Groups)); EC 2.7.8.- (cardiolipin synthetase)
[Em] Mês de entrada:1605
[Cu] Atualização por classe:170922
[Lr] Data última revisão:
170922
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:150708
[St] Status:MEDLINE
[do] DOI:10.1128/MCB.00107-15


  4 / 195 MEDLINE  
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[PMID]:25687304
[Au] Autor:Bochud A; Conzelmann A
[Ad] Endereço:Department of Biology, University of Fribourg, Switzerland.
[Ti] Título:The active site of yeast phosphatidylinositol synthase Pis1 is facing the cytosol.
[So] Source:Biochim Biophys Acta;1851(5):629-40, 2015 May.
[Is] ISSN:0006-3002
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:Five yeast enzymes synthesizing various glycerophospholipids belong to the CDP-alcohol phosphatidyltransferase (CAPT) superfamily. They only share the so-called CAPT motif, which forms the active site of all these enzymes. Bioinformatic tools predict the CAPT motif of phosphatidylinositol synthase Pis1 as either ER luminal or cytosolic. To investigate the membrane topology of Pis1, unique cysteine residues were introduced into either native or a Cys-free form of Pis1 and their accessibility to the small, membrane permeating alkylating reagent N-ethylmaleimide (NEM) and mass tagged, non-permeating maleimides, in the presence and absence of non-denaturing detergents, was monitored. The results clearly point to a cytosolic location of the CAPT motif. Pis1 is highly sensitive to non-denaturing detergent, and low concentrations (0.05%) of dodecylmaltoside change the accessibility of single substituted Cys in the active site of an otherwise cysteine free version of Pis1. Slightly higher detergent concentrations inactivate the enzyme. Removal of the ER retrieval sequence from (wt) Pis1 enhances its activity, again suggesting an influence of the lipid environment. The central 84% of the Pis1 sequence can be aligned and fitted onto the 6 transmembrane helices of two recently crystallized archaeal members of the CAPT family. Results delineate the accessibility of different parts of Pis1 in their natural context and allow to critically evaluate the performance of different cysteine accessibility methods. Overall the results show that cytosolically made inositol and CDP-diacylglycerol can access the active site of the yeast PI synthase Pis1 from the cytosolic side and that Pis1 structure is strongly affected by mild detergents.
[Mh] Termos MeSH primário: CDP-Diacilglicerol-Inositol 3-Fosfatidiltransferase/metabolismo
Citosol/enzimologia
Saccharomyces cerevisiae/enzimologia
Transferases (Outros Grupos de Fosfato Substituídos)/metabolismo
[Mh] Termos MeSH secundário: Algoritmos
CDP-Diacilglicerol-Inositol 3-Fosfatidiltransferase/química
CDP-Diacilglicerol-Inositol 3-Fosfatidiltransferase/genética
Domínio Catalítico
Biologia Computacional
Cisteína
Diglicerídeos de Citidina Difosfato/metabolismo
Detergentes/química
Ativação Enzimática
Estabilidade Enzimática
Inositol/metabolismo
Modelos Moleculares
Mutagênese Sítio-Dirigida
Mutação
Conformação Proteica
Desnaturação Proteica
Estrutura Terciária de Proteína
Saccharomyces cerevisiae/genética
Saccharomyces cerevisiae/crescimento & desenvolvimento
Relação Estrutura-Atividade
Especificidade por Substrato
Fatores de Tempo
Transferases (Outros Grupos de Fosfato Substituídos)/química
Transferases (Outros Grupos de Fosfato Substituídos)/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Cytidine Diphosphate Diglycerides); 0 (Detergents); 4L6452S749 (Inositol); EC 2.7.8.- (Transferases (Other Substituted Phosphate Groups)); EC 2.7.8.11 (CDP-Diacylglycerol-Inositol 3-Phosphatidyltransferase); EC 2.7.8.11 (PIS1 protein, S cerevisiae); K848JZ4886 (Cysteine)
[Em] Mês de entrada:1508
[Cu] Atualização por classe:161126
[Lr] Data última revisão:
161126
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:150218
[St] Status:MEDLINE


  5 / 195 MEDLINE  
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[PMID]:25375833
[Au] Autor:D'Souza K; Kim YJ; Balla T; Epand RM
[Ad] Endereço:Department of Biochemistry and Biomedical Sciences, McMaster University , Hamilton, Ontario L8N 3Z5, Canada.
[Ti] Título:Distinct properties of the two isoforms of CDP-diacylglycerol synthase.
[So] Source:Biochemistry;53(47):7358-67, 2014 Dec 02.
[Is] ISSN:1520-4995
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:CDP-diacylglycerol synthases (CDS) are critical enzymes that catalyze the formation of CDP-diacylglycerol (CDP-DAG) from phosphatidic acid (PA). Here we show in vitro that the two isoforms of human CDS, CDS1 and CDS2, show different acyl chain specificities for its lipid substrate. CDS2 is selective for the acyl chains at the sn-1 and sn-2 positions, the most preferred species being 1-stearoyl-2-arachidonoyl-sn-phosphatidic acid. CDS1, conversely, shows no particular substrate specificity, displaying similar activities for almost all substrates tested. Additionally, we show that inhibition of CDS2 by phosphatidylinositol is also acyl chain-dependent, with the strongest inhibition seen with the 1-stearoyl-2-arachidonoyl species. CDS1 shows no acyl chain-dependent inhibition. Both CDS1 and CDS2 are inhibited by their anionic phospholipid end products, with phosphatidylinositol-(4,5)-bisphosphate showing the strongest inhibition. Our results indicate that CDS1 and CDS2 could create different CDP-DAG pools that may serve to enrich different phospholipid species with specific acyl chains.
[Mh] Termos MeSH primário: Diacilglicerol Colinofosfotransferase/metabolismo
[Mh] Termos MeSH secundário: Animais
Células COS
Cercopithecus aethiops
Diglicerídeos de Citidina Difosfato/metabolismo
Diacilglicerol Colinofosfotransferase/antagonistas & inibidores
Inibidores Enzimáticos/farmacologia
Seres Humanos
Isoenzimas/antagonistas & inibidores
Isoenzimas/metabolismo
Ácidos Fosfatídicos/química
Ácidos Fosfatídicos/metabolismo
Fosfatidilinositóis/farmacologia
Transporte Proteico
Especificidade por Substrato
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., INTRAMURAL; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Cytidine Diphosphate Diglycerides); 0 (Enzyme Inhibitors); 0 (Isoenzymes); 0 (Phosphatidic Acids); 0 (Phosphatidylinositols); EC 2.7.8.2 (Diacylglycerol Cholinephosphotransferase)
[Em] Mês de entrada:1501
[Cu] Atualização por classe:161019
[Lr] Data última revisão:
161019
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:141107
[St] Status:MEDLINE
[do] DOI:10.1021/bi501250m


  6 / 195 MEDLINE  
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[PMID]:24866973
[Au] Autor:Zhang Q; Tamura Y; Roy M; Adachi Y; Iijima M; Sesaki H
[Ad] Endereço:Department of Cell Biology, Johns Hopkins University School of Medicine, Baltimore, MD, USA.
[Ti] Título:Biosynthesis and roles of phospholipids in mitochondrial fusion, division and mitophagy.
[So] Source:Cell Mol Life Sci;71(19):3767-78, 2014 Oct.
[Is] ISSN:1420-9071
[Cp] País de publicação:Switzerland
[La] Idioma:eng
[Ab] Resumo:Mitochondria move, fuse and divide in cells. The dynamic behavior of mitochondria is central to the control of their structure and function. Three conserved mitochondrial dynamin-related GTPases (i.e., mitofusin, Opa1 and Drp1 in mammals and Fzo1, Mgm1 and Dnm1 in yeast) mediate mitochondrial fusion and division. In addition to dynamins, recent studies demonstrated that phospholipids in mitochondria also play key roles in mitochondrial dynamics by interacting with dynamin GTPases and by directly changing the biophysical properties of the mitochondrial membranes. Changes in phospholipid composition also promote mitophagy, which is a selective mitochondrial degradation process that is mechanistically coupled to mitochondrial division. In this review, we will discuss the biogenesis and function of mitochondrial phospholipids.
[Mh] Termos MeSH primário: Mitocôndrias/metabolismo
Degradação Mitocondrial/fisiologia
Dinâmica Mitocondrial/fisiologia
Fosfolipídeos/biossíntese
[Mh] Termos MeSH secundário: Animais
Diglicerídeos de Citidina Difosfato/metabolismo
Dinaminas/metabolismo
GTP Fosfo-Hidrolases/metabolismo
Proteínas de Transporte da Membrana Mitocondrial/metabolismo
Saccharomyces cerevisiae/metabolismo
Proteínas de Saccharomyces cerevisiae/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL; REVIEW
[Nm] Nome de substância:
0 (Cytidine Diphosphate Diglycerides); 0 (Mitochondrial Membrane Transport Proteins); 0 (Phospholipids); 0 (Saccharomyces cerevisiae Proteins); EC 3.6.1.- (GTP Phosphohydrolases); EC 3.6.5.5 (Dynamins)
[Em] Mês de entrada:1411
[Cu] Atualização por classe:170910
[Lr] Data última revisão:
170910
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:140529
[St] Status:MEDLINE
[do] DOI:10.1007/s00018-014-1648-6


  7 / 195 MEDLINE  
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[PMID]:23623749
[Au] Autor:Tamura Y; Harada Y; Nishikawa S; Yamano K; Kamiya M; Shiota T; Kuroda T; Kuge O; Sesaki H; Imai K; Tomii K; Endo T
[Ad] Endereço:Institute for Advanced Research, Nagoya University, Chikusa-ku, Nagoya 464-8602, Japan.
[Ti] Título:Tam41 is a CDP-diacylglycerol synthase required for cardiolipin biosynthesis in mitochondria.
[So] Source:Cell Metab;17(5):709-18, 2013 May 07.
[Is] ISSN:1932-7420
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:CDP-diacylglycerol (CDP-DAG) is central to the phospholipid biosynthesis pathways in cells. A prevailing view is that only one CDP-DAG synthase named Cds1 is present in both the endoplasmic reticulum (ER) and mitochondrial inner membrane (IM) and mediates generation of CDP-DAG from phosphatidic acid (PA) and CTP. However, we demonstrate here by using yeast Saccharomyces cerevisiae as a model organism that Cds1 resides in the ER but not in mitochondria, and that Tam41, a highly conserved mitochondrial maintenance protein, directly catalyzes the formation of CDP-DAG from PA in the mitochondrial IM. We also find that inositol depletion by overexpressing an arrestin-related protein Art5 partially restores the defects of cell growth and CL synthesis in the absence of Tam41. The present findings unveil the missing step of the cardiolipin synthesis pathway in mitochondria as well as the flexibile regulation of phospholipid biosynthesis to respond to compromised CDP-DAG synthesis in mitochondria.
[Mh] Termos MeSH primário: Cardiolipinas/biossíntese
Diacilglicerol Colinofosfotransferase/metabolismo
Mitocôndrias/metabolismo
Proteínas Mitocondriais/metabolismo
Proteínas de Saccharomyces cerevisiae/metabolismo
[Mh] Termos MeSH secundário: Cardiolipinas/metabolismo
Proteínas de Transporte/metabolismo
Diglicerídeos de Citidina Difosfato/metabolismo
Retículo Endoplasmático/metabolismo
Inositol/metabolismo
Mitocôndrias/enzimologia
Nucleotidiltransferases/metabolismo
Fosfolipídeos/metabolismo
Saccharomyces cerevisiae/enzimologia
Saccharomyces cerevisiae/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Art5 protein, S cerevisiae); 0 (Cardiolipins); 0 (Carrier Proteins); 0 (Cytidine Diphosphate Diglycerides); 0 (Mitochondrial Proteins); 0 (Phospholipids); 0 (Saccharomyces cerevisiae Proteins); 0 (TAM41 protein, S cerevisiae); 4L6452S749 (Inositol); EC 2.7.7.- (Nucleotidyltransferases); EC 2.7.7.41 (phosphatidate cytidylyltransferase); EC 2.7.8.2 (Diacylglycerol Cholinephosphotransferase)
[Em] Mês de entrada:1403
[Cu] Atualização por classe:161019
[Lr] Data última revisão:
161019
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:130430
[St] Status:MEDLINE


  8 / 195 MEDLINE  
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[PMID]:22922101
[Au] Autor:Geiger O; López-Lara IM; Sohlenkamp C
[Ad] Endereço:Centro de Ciencias Genómicas, Universidad Nacional Autónoma de México, Av. Universidad s/n, Apdo. Postal 565-A, Cuernavaca, Morelos, CP62210, Mexico. otto@ccg.unam.mx
[Ti] Título:Phosphatidylcholine biosynthesis and function in bacteria.
[So] Source:Biochim Biophys Acta;1831(3):503-13, 2013 Mar.
[Is] ISSN:0006-3002
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:Phosphatidylcholine (PC) is the major membrane-forming phospholipid in eukaryotes and is estimated to be present in about 15% of the domain Bacteria. Usually, PC can be synthesized in bacteria by either of two pathways, the phospholipid N-methylation (Pmt) pathway or the phosphatidylcholine synthase (Pcs) pathway. The three subsequent enzymatic methylations of phosphatidylethanolamine are performed by a single phospholipid N-methyltransferase in some bacteria whereas other bacteria possess multiple phospholipid N-methyltransferases each one performing one or several distinct methylation steps. Phosphatidylcholine synthase condenses choline directly with CDP-diacylglycerol to form CMP and PC. Like in eukaryotes, bacterial PC also functions as a biosynthetic intermediate during the formation of other biomolecules such as choline, diacylglycerol, or diacylglycerol-based phosphorus-free membrane lipids. Bacterial PC may serve as a specific recognition molecule but it affects the physicochemical properties of bacterial membranes as well. This article is part of a Special Issue entitled Phospholipids and Phospholipid Metabolism.
[Mh] Termos MeSH primário: Agrobacterium tumefaciens/metabolismo
Proteínas de Bactérias/metabolismo
Fosfatidilcolinas/biossíntese
Sinorhizobium meliloti/metabolismo
[Mh] Termos MeSH secundário: Animais
Colina/metabolismo
Diglicerídeos de Citidina Difosfato/metabolismo
Citidina Monofosfato/metabolismo
Seres Humanos
Isoenzimas/metabolismo
Metilação
Fosfatidil-N-Metiletanolamina N-Metiltransferase/metabolismo
Fosfatidiletanolaminas/metabolismo
Especificidade da Espécie
Transferases (Outros Grupos de Fosfato Substituídos)/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T; REVIEW
[Nm] Nome de substância:
0 (Bacterial Proteins); 0 (Cytidine Diphosphate Diglycerides); 0 (Isoenzymes); 0 (Phosphatidylcholines); 0 (Phosphatidylethanolamines); EC 2.1.1.71 (Phosphatidyl-N-Methylethanolamine N-Methyltransferase); EC 2.7.8.- (Transferases (Other Substituted Phosphate Groups)); EC 2.7.8.24 (CDP-diacylglycerol choline O-phosphatidyltransferase); F469818O25 (Cytidine Monophosphate); N91BDP6H0X (Choline)
[Em] Mês de entrada:1304
[Cu] Atualização por classe:161126
[Lr] Data última revisão:
161126
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:120828
[St] Status:MEDLINE


  9 / 195 MEDLINE  
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[PMID]:21937673
[Au] Autor:Waugh MG; Minogue S; Clayton EL; Hsuan JJ
[Ad] Endereço:Centre for Molecular Cell Biology, Division of Medicine, University College London, Royal Free Campus, London, United Kingdom. m.waugh@ucl.ac.uk
[Ti] Título:CDP-diacylglycerol phospholipid synthesis in detergent-soluble, non-raft, membrane microdomains of the endoplasmic reticulum.
[So] Source:J Lipid Res;52(12):2148-58, 2011 Dec.
[Is] ISSN:1539-7262
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Phosphatidylinositol (PI) is essential for numerous cell functions and is generated by consecutive reactions catalyzed by CDP-diacylglycerol synthase (CDS) and PI synthase. In this study, we investigated the membrane organization of CDP-diacylglycerol synthesis. Separation of mildly disrupted A431 cell membranes on sucrose density gradients revealed cofractionation of CDS and PI synthase activities with cholesterol-poor, endoplasmic reticulum (ER) membranes and partial overlap with plasma membrane caveolae. Cofractionation of CDS activity with caveolae was also observed when low-buoyant density caveolin-enriched membranes were prepared using a carbonate-based method. However, immunoisolation studies determined that CDS activity localized to ER membrane fragments containing calnexin and type III inositol (1,4,5)-trisphosphate receptors but not to caveolae. Membrane fragmentation in neutral pH buffer established that CDP-diacylglycerol and PI syntheses were restricted to a subfraction of the calnexin-positive ER. In contrast to lipid rafts enriched for caveolin, cholesterol, and GM1 glycosphingolipids, the CDS-containing ER membranes were detergent soluble. In cell imaging studies, CDS and calnexin colocalized in microdomain-sized patches of the ER and also unexpectedly at the plasma membrane. These results demonstrate that key components of the PI pathway localize to nonraft, phospholipid-synthesizing microdomains of the ER that are also enriched for calnexin.
[Mh] Termos MeSH primário: Diglicerídeos de Citidina Difosfato/biossíntese
Detergentes/química
Retículo Endoplasmático/química
Retículo Endoplasmático/metabolismo
Membranas Intracelulares/química
Membranas Intracelulares/metabolismo
Fosfolipídeos/biossíntese
[Mh] Termos MeSH secundário: CDP-Diacilglicerol-Inositol 3-Fosfatidiltransferase/metabolismo
Calnexina/metabolismo
Caveolinas/metabolismo
Linhagem Celular Tumoral
Diacilglicerol Colinofosfotransferase/metabolismo
Retículo Endoplasmático/enzimologia
Seres Humanos
Receptores de Inositol 1,4,5-Trifosfato/metabolismo
Membranas Intracelulares/enzimologia
Imagem Molecular
Transporte Proteico
Solubilidade
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Caveolins); 0 (Cytidine Diphosphate Diglycerides); 0 (Detergents); 0 (Inositol 1,4,5-Trisphosphate Receptors); 0 (Phospholipids); 139873-08-8 (Calnexin); EC 2.7.8.11 (CDP-Diacylglycerol-Inositol 3-Phosphatidyltransferase); EC 2.7.8.2 (Diacylglycerol Cholinephosphotransferase)
[Em] Mês de entrada:1203
[Cu] Atualização por classe:161019
[Lr] Data última revisão:
161019
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:110923
[St] Status:MEDLINE
[do] DOI:10.1194/jlr.M017814


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[PMID]:20385136
[Au] Autor:Shastri S; Zeeman AM; Berry L; Verburgh RJ; Braun-Breton C; Thomas AW; Gannoun-Zaki L; Kocken CH; Vial HJ
[Ad] Endereço:CNRS UMR5235, University of Montpellier 2, Place Eugene Bataillon, 34095 Montpellier Cedex 5, France.
[Ti] Título:Plasmodium CDP-DAG synthase: an atypical gene with an essential N-terminal extension.
[So] Source:Int J Parasitol;40(11):1257-68, 2010 Sep.
[Is] ISSN:1879-0135
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Cytidine diphosphate diacylglycerol synthase (CDS) diverts phosphatidic acid towards the biosynthesis of CDP-DAG, an obligatory liponucleotide intermediate in anionic phospholipid biosynthesis. The 78kDa predicted Plasmodium falciparum CDS (PfCDS) is recovered as a 50 kDa conserved C-terminal cytidylyltransferase domain (C-PfCDS) and a 28kDa fragment that corresponds to the unusually long hydrophilic asparagine-rich N-terminal extension (N-PfCDS). Here, we show that the two fragments of PfCDS are the processed forms of the 78 kDa pro-form that is encoded from a single transcript with no alternate translation start site for C-PfCDS. PfCDS, which shares 54% sequence identity with Plasmodium knowlesi CDS (PkCDS), could substitute for PkCDS in P. knowlesi. Experiments to disrupt either the full-length or the N-terminal extension of PkCDS indicate that not only the C-terminal cytidylyltransferase domain but also the N-terminal extension is essential to Plasmodium spp. PkCDS and PfCDS introduced in P. knowlesi were processed in the parasite, suggesting a conserved parasite-dependent mechanism. The N-PfCDS appears to be a peripheral membrane protein and is trafficked outside the parasite to the parasitophorous vacuole. Although the function of this unusual N-PfCDS remains enigmatic, the study here highlights features of this essential gene and its biological importance during the intra-erythrocytic cycle of the parasite.
[Mh] Termos MeSH primário: Diacilglicerol Colinofosfotransferase/química
Diacilglicerol Colinofosfotransferase/metabolismo
Plasmodium falciparum/enzimologia
Plasmodium knowlesi/enzimologia
Proteínas de Protozoários/química
Proteínas de Protozoários/metabolismo
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Animais
Cercopithecus aethiops
Diglicerídeos de Citidina Difosfato/biossíntese
Diacilglicerol Colinofosfotransferase/genética
Eritrócitos/parasitologia
Seres Humanos
Malária/parasitologia
Plasmodium falciparum/química
Plasmodium falciparum/genética
Plasmodium falciparum/crescimento & desenvolvimento
Plasmodium knowlesi/química
Plasmodium knowlesi/genética
Plasmodium knowlesi/crescimento & desenvolvimento
Estrutura Terciária de Proteína
Proteínas de Protozoários/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Cytidine Diphosphate Diglycerides); 0 (Protozoan Proteins); EC 2.7.8.2 (Diacylglycerol Cholinephosphotransferase)
[Em] Mês de entrada:1011
[Cu] Atualização por classe:100719
[Lr] Data última revisão:
100719
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:100414
[St] Status:MEDLINE
[do] DOI:10.1016/j.ijpara.2010.03.006



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