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  1 / 1702 MEDLINE  
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[PMID]:28470605
[Au] Autor:Errasti-Murugarren E; Rodríguez-Banqueri A; Vázquez-Ibar JL
[Ad] Endereço:Institute for Research in Biomedicine (IRB Barcelona), Barcelona Institute of Science and Technology, 08028, Barcelona, Spain.
[Ti] Título:Split GFP Complementation as Reporter of Membrane Protein Expression and Stability in E. coli: A Tool to Engineer Stability in a LAT Transporter.
[So] Source:Methods Mol Biol;1586:181-195, 2017.
[Is] ISSN:1940-6029
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Obtaining enough quantity of recombinant membrane transport proteins with optimal purity and stability for structural studies is a remarkable challenge. In this chapter, we describe a protocol to engineer SteT, the amino acid transporter of Bacillus subtilis, in order to improve its heterologous expression in Escherichia coli and its stability in detergent micelles. We built a library of 70 SteT mutants, combining a random mutagenesis protocol with a split GFP assay as reporter of protein folding and membrane insertion. Mutagenesis was restricted to residues situated in the transmembrane domains. Improved versions of SteT were successfully identified after analyzing the expression yield and monodispersity in detergent micelles of the library's members.
[Mh] Termos MeSH primário: Sistemas de Transporte de Aminoácidos/genética
Bacillus subtilis/genética
Proteínas de Bactérias/genética
Clonagem Molecular/métodos
Escherichia coli/genética
Engenharia de Proteínas/métodos
[Mh] Termos MeSH secundário: Sistemas de Transporte de Aminoácidos/química
Bacillus subtilis/química
Proteínas de Bactérias/química
Detergentes/química
Proteínas de Fluorescência Verde/química
Proteínas de Fluorescência Verde/genética
Modelos Moleculares
Dobramento de Proteína
Estabilidade Proteica
Proteínas Recombinantes de Fusão/química
Proteínas Recombinantes de Fusão/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Amino Acid Transport Systems); 0 (Bacterial Proteins); 0 (Detergents); 0 (Recombinant Fusion Proteins); 147336-22-9 (Green Fluorescent Proteins)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180220
[Lr] Data última revisão:
180220
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170505
[St] Status:MEDLINE
[do] DOI:10.1007/978-1-4939-6887-9_11


  2 / 1702 MEDLINE  
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[PMID]:29032150
[Au] Autor:Sundararajan T; Manzardo AM; Butler MG
[Ad] Endereço:Department of Psychiatry and Behavioral Sciences, University of Kansas Medical Center, Kansas City, KS, United States.
[Ti] Título:Functional analysis of schizophrenia genes using GeneAnalytics program and integrated databases.
[So] Source:Gene;641:25-34, 2018 Jan 30.
[Is] ISSN:1879-0038
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:Schizophrenia (SCZ) is a chronic debilitating neuropsychiatric disorder with multiple risk factors involving numerous complex genetic influences. We examined and updated a master list of clinically relevant and susceptibility genes associated with SCZ reported in the literature and genomic databases dedicated to gene discovery for characterization of SCZ genes. We used the commercially available GeneAnalytics computer-based gene analysis program and integrated genomic databases to create a molecular profile of the updated list of 608 SCZ genes to model their impact in select categories (tissues and cells, diseases, pathways, biological processes, molecular functions, phenotypes and compounds) using specialized GeneAnalytics algorithms. Genes for schizophrenia were predominantly expressed in the cerebellum, cerebral cortex, medulla oblongata, thalamus and hypothalamus. Psychiatric/behavioral disorders incorporating SCZ genes included ADHD, bipolar disorder, autism spectrum disorder and alcohol dependence as well as cancer, Alzheimer's and Parkinson's disease, sleep disturbances and inflammation. Function based analysis of major biological pathways and mechanisms associated with SCZ genes identified glutaminergic receptors (e.g., GRIA1, GRIN2, GRIK4, GRM5), serotonergic receptors (e.g., HTR2A, HTR2C), GABAergic receptors (e.g., GABRA1, GABRB2), dopaminergic receptors (e.g., DRD1, DRD2), calcium-related channels (e.g., CACNA1H, CACNA1B), solute transporters (e.g., SLC1A1, SLC6A2) and for neurodevelopment (e.g., ADCY1, MEF2C, NOTCH2, SHANK3). Biological mechanisms involving synaptic transmission, regulation of membrane potential and transmembrane ion transport were identified as leading molecular functions associated with SCZ genes. Our approach to interrogate SCZ genes and their interactions at various levels has increased our knowledge and insight into the disease process possibly opening new avenues for therapeutic intervention.
[Mh] Termos MeSH primário: Estudo de Associação Genômica Ampla
Transporte de Íons/genética
Potenciais da Membrana/genética
Esquizofrenia/genética
Transmissão Sináptica/genética
[Mh] Termos MeSH secundário: Sistemas de Transporte de Aminoácidos/genética
Canais de Cálcio/genética
Cerebelo/citologia
Córtex Cerebral/citologia
Bases de Dados Genéticas
Seres Humanos
Hipotálamo/citologia
Bulbo/citologia
Receptores Dopaminérgicos/genética
Receptores de GABA-A/genética
Receptores Ionotrópicos de Glutamato/genética
Receptores de Serotonina/genética
Tálamo/citologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Amino Acid Transport Systems); 0 (Calcium Channels); 0 (Receptors, Dopamine); 0 (Receptors, GABA-A); 0 (Receptors, Ionotropic Glutamate); 0 (Receptors, Serotonin)
[Em] Mês de entrada:1711
[Cu] Atualização por classe:171128
[Lr] Data última revisão:
171128
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171017
[St] Status:MEDLINE


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[PMID]:29053970
[Au] Autor:Wyant GA; Abu-Remaileh M; Wolfson RL; Chen WW; Freinkman E; Danai LV; Vander Heiden MG; Sabatini DM
[Ad] Endereço:Whitehead Institute for Biomedical Research, Cambridge, MA 02142, USA; Department of Biology, Massachusetts Institute of Technology, 9 Cambridge Center, Cambridge, MA 02142, USA; Howard Hughes Medical Institute, Cambridge, MA 02139, USA; Koch Institute for Integrative Cancer Research, 77 Massachuset
[Ti] Título:mTORC1 Activator SLC38A9 Is Required to Efflux Essential Amino Acids from Lysosomes and Use Protein as a Nutrient.
[So] Source:Cell;171(3):642-654.e12, 2017 Oct 19.
[Is] ISSN:1097-4172
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The mTORC1 kinase is a master growth regulator that senses many environmental cues, including amino acids. Activation of mTORC1 by arginine requires SLC38A9, a poorly understood lysosomal membrane protein with homology to amino acid transporters. Here, we validate that SLC38A9 is an arginine sensor for the mTORC1 pathway, and we uncover an unexpectedly central role for SLC38A9 in amino acid homeostasis. SLC38A9 mediates the transport, in an arginine-regulated fashion, of many essential amino acids out of lysosomes, including leucine, which mTORC1 senses through the cytosolic Sestrin proteins. SLC38A9 is necessary for leucine generated via lysosomal proteolysis to exit lysosomes and activate mTORC1. Pancreatic cancer cells, which use macropinocytosed protein as a nutrient source, require SLC38A9 to form tumors. Thus, through SLC38A9, arginine serves as a lysosomal messenger that couples mTORC1 activation to the release from lysosomes of the essential amino acids needed to drive cell growth.
[Mh] Termos MeSH primário: Sistemas de Transporte de Aminoácidos/metabolismo
Aminoácidos Essenciais/metabolismo
Lisossomos/metabolismo
Complexos Multiproteicos/metabolismo
Serina-Treonina Quinases TOR/metabolismo
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Sistemas de Transporte de Aminoácidos/química
Sistemas de Transporte de Aminoácidos/genética
Animais
Arginina/metabolismo
Linhagem Celular
Linhagem Celular Tumoral
Seres Humanos
Masculino
Alvo Mecanístico do Complexo 1 de Rapamicina
Camundongos
Camundongos Endogâmicos C57BL
Alinhamento de Sequência
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Amino Acid Transport Systems); 0 (Amino Acids, Essential); 0 (Multiprotein Complexes); 0 (SLC38A9 protein, human); 0 (SLC38A9 protein, mouse); 94ZLA3W45F (Arginine); EC 2.7.1.1 (TOR Serine-Threonine Kinases); EC 2.7.11.1 (Mechanistic Target of Rapamycin Complex 1)
[Em] Mês de entrada:1711
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171021
[St] Status:MEDLINE


  4 / 1702 MEDLINE  
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[PMID]:28670736
[Au] Autor:Ji X; Zhao L; Luo H; Zhang X; Jin Y; Liu W
[Ad] Endereço:Key Laboratory of Animal Biotechnology, the Ministry of Agriculture, College of Veterinary Medicine, Northwest Agriculture & Forest University, Yangling, Shaanxi, China.
[Ti] Título:Amino acids suppress the expression of PAT1 on lysosomes via inducing the cleavage of a targeting signal.
[So] Source:FEBS Lett;591(15):2279-2289, 2017 Aug.
[Is] ISSN:1873-3468
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:The lysosome-associated transporter proton-coupled amino acid transporter 1 (PAT1) promotes nutrient recycling through releasing luminal amino acids into the cytosol. Using HEK293 cells expressing an EGFP-tagged PAT1 (EGFP-PAT1) as a model, we identified a consensus tyrosine-based targeting signal in the cytosolic N-terminal region of PAT1, which facilitates its expression on the lysosome. Interestingly, this signal can be removed via protein cleavage in an amino acid-sensitive manner. The cleavage is suppressed upon amino acid starvation and is induced by amino acid replenishment. However, amino acid deficiency does not suppress the cleavage of amino acid-binding mutants of EGFP-PAT1. Our data support a mechanism, whereby amino acid binding induces PAT1 cleavage to remove a targeting signal, thus suppressing the expression of PAT1 on the lysosome.
[Mh] Termos MeSH primário: Sistemas de Transporte de Aminoácidos/metabolismo
Aminoácidos/metabolismo
Lisossomos/metabolismo
Simportadores/metabolismo
[Mh] Termos MeSH secundário: Alanina/genética
Motivos de Aminoácidos
Substituição de Aminoácidos
Sistemas de Transporte de Aminoácidos/genética
Aminoácidos/farmacologia
Retroalimentação Fisiológica
Proteínas de Fluorescência Verde/genética
Proteínas de Fluorescência Verde/metabolismo
Células HEK293/efeitos dos fármacos
Seres Humanos
Lisossomos/efeitos dos fármacos
Alvo Mecanístico do Complexo 1 de Rapamicina
Complexos Multiproteicos/metabolismo
Mutação
Sinais Direcionadores de Proteínas
Proteínas Recombinantes/genética
Proteínas Recombinantes/metabolismo
Simportadores/genética
Serina-Treonina Quinases TOR/metabolismo
Tirosina/genética
[Pt] Tipo de publicação:LETTER
[Nm] Nome de substância:
0 (Amino Acid Transport Systems); 0 (Amino Acids); 0 (Multiprotein Complexes); 0 (Protein Sorting Signals); 0 (Recombinant Proteins); 0 (SLC36A1 protein, human); 0 (Symporters); 0 (enhanced green fluorescent protein); 147336-22-9 (Green Fluorescent Proteins); 42HK56048U (Tyrosine); EC 2.7.1.1 (TOR Serine-Threonine Kinases); EC 2.7.11.1 (Mechanistic Target of Rapamycin Complex 1); OF5P57N2ZX (Alanine)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170704
[St] Status:MEDLINE
[do] DOI:10.1002/1873-3468.12738


  5 / 1702 MEDLINE  
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[PMID]:28655293
[Au] Autor:Zhao C; Nabity PD
[Ad] Endereço:Department of Botany and Plant Sciences, University of California, Riverside, Riverside, CA, 92521, USA.
[Ti] Título:Plant manipulation through gall formation constrains amino acid transporter evolution in sap-feeding insects.
[So] Source:BMC Evol Biol;17(1):153, 2017 Jun 27.
[Is] ISSN:1471-2148
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: The herbivore lifestyle leads to encounters with plant toxins and requires mechanisms to overcome suboptimal nutrient availability in plant tissues. Although the evolution of bacterial endosymbiosis alleviated many of these challenges, the ability to manipulate plant nutrient status has evolved in lineages with and without nutritional symbionts. Whether and how these alternative nutrient acquisition strategies interact or constrain insect evolution is unknown. We studied the transcriptomes of galling and free-living aphidomorphs to characterize how amino acid transporter evolution is influenced by the ability to manipulate plant resource availability. RESULTS: Using a comparative approach we found phylloxerids retain nearly all amino acid transporters as other aphidomorphs, despite loss of nutritional endosymbiosis. Free living species show more transporters than galling species within the same genus, family, or infraorder, indicating plant hosts influence the maintenance and evolution of nutrient transport within herbivores. Transcript profiles also show lineage specificity and suggest some genes may facilitate life without endosymbionts or the galling lifestyle. CONCLUSIONS: The transcript abundance profiles we document across fluid feeding herbivores support plant host constraint on insect amino acid transporter evolution. Given amino acid uptake, transport, and catabolism underlie the success of herbivory as a life history strategy, this suggests that plant host nutrient quality, whether constitutive or induced, alters the selective environment surrounding the evolution and maintenance of endosymbiosis.
[Mh] Termos MeSH primário: Sistemas de Transporte de Aminoácidos/genética
Afídeos/genética
Evolução Molecular
Herbivoria
Proteínas de Insetos/genética
[Mh] Termos MeSH secundário: Animais
Afídeos/classificação
Afídeos/fisiologia
Perfilação da Expressão Gênica
Filogenia
Fenômenos Fisiológicos Vegetais
Tumores de Planta
Simbiose
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Amino Acid Transport Systems); 0 (Insect Proteins)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171018
[Lr] Data última revisão:
171018
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170629
[St] Status:MEDLINE
[do] DOI:10.1186/s12862-017-1000-5


  6 / 1702 MEDLINE  
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[PMID]:28615378
[Au] Autor:van der Wielen N; Moughan PJ; Mensink M
[Ad] Endereço:Division of Human Nutrition, Wageningen University, Wageningen, Netherlands; and.
[Ti] Título:Amino Acid Absorption in the Large Intestine of Humans and Porcine Models.
[So] Source:J Nutr;147(8):1493-1498, 2017 Aug.
[Is] ISSN:1541-6100
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Dietary protein quality has been recognized as a critical issue by international authorities because it can affect important functions of the body. To predict protein quality, the FAO introduced the Digestible Indispensable Amino Acid Score. This score depends on ileal amino acid (AA) digestibility; therefore, the assumption is made that AAs are not absorbed in nutritionally relevant amounts from the large intestine. This article reviews the evidence for this assumption by considering the role of the mammalian large intestine in dietary protein and AA digestion and absorption, with particular reference to adult humans. Although most dietary AAs and peptides are absorbed in the small intestine, substantial amounts can enter the large intestine. Nitrogen is absorbed in the large intestine, and a series of animal experiments indicate a potential small degree of AA absorption. In humans, colonocytes have the capacity for AA absorption because AA transporters are present in the large intestine. The absorption of nutritionally relevant amounts of dietary indispensable AAs and peptides in the human large intestine has not been convincingly demonstrated, however.
[Mh] Termos MeSH primário: Sistemas de Transporte de Aminoácidos/metabolismo
Aminoácidos Essenciais/farmacocinética
Proteínas na Dieta/farmacocinética
Digestão
Absorção Intestinal
Intestino Grosso/metabolismo
[Mh] Termos MeSH secundário: Aminoácidos Essenciais/metabolismo
Animais
Proteínas na Dieta/metabolismo
Proteínas na Dieta/normas
Seres Humanos
Íleo/metabolismo
Nitrogênio/metabolismo
Peptídeos/metabolismo
Suínos
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (Amino Acid Transport Systems); 0 (Amino Acids, Essential); 0 (Dietary Proteins); 0 (Peptides); N762921K75 (Nitrogen)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170816
[Lr] Data última revisão:
170816
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170616
[St] Status:MEDLINE
[do] DOI:10.3945/jn.117.248187


  7 / 1702 MEDLINE  
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[PMID]:28548851
[Au] Autor:Wibowo M; Wang Q; Holst J; White JM; Hofmann A; Davis RA
[Ad] Endereço:Griffith Institute for Drug Discovery, Griffith University , Brisbane, QLD 4111, Australia.
[Ti] Título:Celastrofurans A-G: Dihydro-ß-agarofurans from the Australian Rainforest Vine Celastrus subspicata and Their Inhibitory Effect on Leucine Transport in Prostate Cancer Cells.
[So] Source:J Nat Prod;80(6):1918-1925, 2017 Jun 23.
[Is] ISSN:1520-6025
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Seven new dihydro-ß-agarofurans, celastrofurans A-G (1-7), along with two known secondary metabolites, 9ß-benzoyloxy-1α-furoyloxydihydro-ß-agarofuran (8) and (1R,2R,4R,5S,7R,9S,10R)-2-acetoxy-9-benzoyloxy-1-furoyloxydihydro-ß-agarofuran (9), were obtained from the leaves of the Australian rainforest vine, Celastrus subspicata. The structures of the new compounds were determined by detailed spectroscopic (1D/2D NMR) and MS data analysis. The absolute configurations of compounds 1-4 were defined by ECD and single-crystal X-ray diffraction studies. All compounds were found to exhibit inhibitory activity on leucine transport in the human prostate cancer cell line LNCaP with IC values ranging from 7.0 to 98.9 µM. Dihydro-ß-agarofurans 1-9 showed better potency than the L-type amino acid transporter (LAT) family inhibitor, 2-aminobicyclo[2.2.1]-heptane-2-carboxylic acid (BCH).
[Mh] Termos MeSH primário: Celastrus/química
Leucina/efeitos dos fármacos
Leucina/metabolismo
Neoplasias da Próstata/tratamento farmacológico
Sesquiterpenos/isolamento & purificação
Sesquiterpenos/farmacologia
[Mh] Termos MeSH secundário: Sistemas de Transporte de Aminoácidos/farmacologia
Austrália
Cristalografia por Raios X
Seres Humanos
Masculino
Estrutura Molecular
Folhas de Planta/química
Floresta Úmida
Sesquiterpenos/química
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Amino Acid Transport Systems); 0 (Sesquiterpenes); 20053-66-1 (dihydroagarofuran); GMW67QNF9C (Leucine)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170830
[Lr] Data última revisão:
170830
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170527
[St] Status:MEDLINE
[do] DOI:10.1021/acs.jnatprod.7b00220


  8 / 1702 MEDLINE  
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[PMID]:28410963
[Au] Autor:Yoganandarajah V; Li B; Umapathy A; Donaldson PJ; Lim JC
[Ad] Endereço:Department of Physiology, School of Medical Sciences, New Zealand National Eye Centre, University of Auckland, New Zealand.
[Ti] Título:Regional differences in glutathione accumulation pathways in the rat cornea: Mapping of amino acid transporters involved in glutathione synthesis.
[So] Source:Exp Eye Res;161:89-100, 2017 Aug.
[Is] ISSN:1096-0007
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:In this study we have sought to complete the identification and localisation of uptake pathways involved in accumulating precursor amino acids involved in GSH synthesis in the rat cornea. To do this, we performed reverse transcription PCR (RT-PCR) to identify the Excitatory Amino Acid Transporters (EAAT 1-5) responsible for glutamate uptake, and glycine transporters (GLYT 1-2) at the transcript level. Western blotting was used to verify protein expression, while immunolabelling of sagittal sections was used to localise transporters to the different layers of the cornea. Immunolabelling of en face sections was used to examine the subcellular distribution of proteins in the corneal endothelium. Our findings revealed EAAT 1-5 and GLYT 1-2 to be expressed at the transcript and protein level in the rat cornea. Immunohistochemistry revealed all amino acid transporters to be localised to the epithelium. In the majority of cases, labelling was restricted to the epithelium, and labelling absent from the stroma or endothelium. However, EAAT 4 and GLYT 2 labelling was detected in the stroma with EAAT 4 labelling also present in the endothelium. Overall, the identification of amino acid transporters strongly supports the existence of an intracellular GSH synthesis pathway in the rat corneal epithelium. This suggests that regional differences in GSH accumulation pathways exist, with direct uptake of GSH and intracellular synthesis of GSH restricted to the endothelial and epithelial cell layers, respectively. This information is important in the design of targeted strategies to enhance GSH levels in specific layers of the cornea to prevent against oxidative damage, corneal swelling and loss of corneal transparency.
[Mh] Termos MeSH primário: Sistema X-AG de Transporte de Aminoácidos/metabolismo
Córnea/metabolismo
Glutationa/biossíntese
Proteínas da Membrana Plasmática de Transporte de Glicina/metabolismo
[Mh] Termos MeSH secundário: Sistema X-AG de Transporte de Aminoácidos/genética
Sistemas de Transporte de Aminoácidos/fisiologia
Animais
Transporte Biológico
Western Blotting
Substância Própria/metabolismo
Epitélio Posterior/metabolismo
Epitélio Anterior/metabolismo
Técnica Indireta de Fluorescência para Anticorpo
Regulação da Expressão Gênica/fisiologia
Proteínas da Membrana Plasmática de Transporte de Glicina/genética
Ratos
Ratos Wistar
Reação em Cadeia da Polimerase Via Transcriptase Reversa
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Amino Acid Transport System X-AG); 0 (Amino Acid Transport Systems); 0 (Glycine Plasma Membrane Transport Proteins); GAN16C9B8O (Glutathione)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170821
[Lr] Data última revisão:
170821
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170416
[St] Status:MEDLINE


  9 / 1702 MEDLINE  
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[PMID]:28361363
[Au] Autor:Xu P; Gao J; Cao Z; Chee PW; Guo Q; Xu Z; Paterson AH; Zhang X; Shen X
[Ad] Endereço:Key Laboratory of Cotton and Rapeseed (Nanjing), Ministry of Agriculture, Nanjing, People's Republic of China.
[Ti] Título:Fine mapping and candidate gene analysis of qFL-chr1, a fiber length QTL in cotton.
[So] Source:Theor Appl Genet;130(6):1309-1319, 2017 Jun.
[Is] ISSN:1432-2242
[Cp] País de publicação:Germany
[La] Idioma:eng
[Ab] Resumo:KEY MESSAGE: A fiber length QTL, qFL-chr1, was fine mapped to a 0.9 cM interval of cotton chromosome 1. Two positional candidate genes showed positive correlation between gene expression level and fiber length. Prior analysis of a backcross-self mapping population derived from a cross between Gossypium hirsutum L. and G. barbadense L. revealed a QTL on chromosome 1 associated with increased fiber length (qFL-chr1), which was confirmed in three independent populations of near-isogenic introgression lines (NIILs). Here, a single NIIL, R01-40-08, was used to develop a large population segregating for the target region. Twenty-two PCR-based polymorphic markers used to genotype 1672 BC F plants identified 432 recombinants containing breakpoints in the target region. Substitution mapping using 141 informative recombinants narrowed the position of qFL-chr1 to a 1.0-cM interval between SSR markers MUSS084 and CIR018. To exclude possible effects of non-target introgressions on fiber length, different heterozygous BC F plants introgressed between SSR markers NAU3384 and CGR5144 were selected to develop sub-NILs. The qFL-chr1 was further mapped at 0.9-cM interval between MUSS422 and CIR018 by comparisons of sub-NIL phenotype, and increased fiber length by ~1 mm. The 2.38-Mb region between MUSS422 and CIR018 in G. barbadense contained 19 annotated genes. Expression levels of two of these genes, GOBAR07705 (encoding 1-aminocyclopropane-1-carboxylate synthase) and GOBAR25992 (encoding amino acid permease), were positively correlated with fiber length in a small F population, supporting these genes as candidates for qFL-chr1.
[Mh] Termos MeSH primário: Mapeamento Cromossômico
Fibra de Algodão
Gossypium/genética
Locos de Características Quantitativas
[Mh] Termos MeSH secundário: Sistemas de Transporte de Aminoácidos/genética
Genes de Plantas
Marcadores Genéticos
Genótipo
Liases/genética
Fenótipo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Amino Acid Transport Systems); 0 (Genetic Markers); EC 4.- (Lyases); EC 4.4.1.14 (1-aminocyclopropanecarboxylate synthase)
[Em] Mês de entrada:1706
[Cu] Atualização por classe:170917
[Lr] Data última revisão:
170917
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170401
[St] Status:MEDLINE
[do] DOI:10.1007/s00122-017-2890-8


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[PMID]:28336668
[Au] Autor:Castellano BM; Thelen AM; Moldavski O; Feltes M; van der Welle RE; Mydock-McGrane L; Jiang X; van Eijkeren RJ; Davis OB; Louie SM; Perera RM; Covey DF; Nomura DK; Ory DS; Zoncu R
[Ad] Endereço:Department of Molecular and Cell Biology, University of California at Berkeley, Berkeley, CA 94720, USA.
[Ti] Título:Lysosomal cholesterol activates mTORC1 via an SLC38A9-Niemann-Pick C1 signaling complex.
[So] Source:Science;355(6331):1306-1311, 2017 03 24.
[Is] ISSN:1095-9203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The mechanistic target of rapamycin complex 1 (mTORC1) protein kinase is a master growth regulator that becomes activated at the lysosome in response to nutrient cues. Here, we identify cholesterol, an essential building block for cellular growth, as a nutrient input that drives mTORC1 recruitment and activation at the lysosomal surface. The lysosomal transmembrane protein, SLC38A9, is required for mTORC1 activation by cholesterol through conserved cholesterol-responsive motifs. Moreover, SLC38A9 enables mTORC1 activation by cholesterol independently from its arginine-sensing function. Conversely, the Niemann-Pick C1 (NPC1) protein, which regulates cholesterol export from the lysosome, binds to SLC38A9 and inhibits mTORC1 signaling through its sterol transport function. Thus, lysosomal cholesterol drives mTORC1 activation and growth signaling through the SLC38A9-NPC1 complex.
[Mh] Termos MeSH primário: Sistemas de Transporte de Aminoácidos/metabolismo
Proteínas de Transporte/metabolismo
Colesterol/metabolismo
Lisossomos/metabolismo
Complexos Multiproteicos/metabolismo
Proteínas Nucleares/metabolismo
Serina-Treonina Quinases TOR/metabolismo
[Mh] Termos MeSH secundário: Motivos de Aminoácidos
Sistemas de Transporte de Aminoácidos/genética
Animais
Transporte Biológico
Células CHO
HDL-Colesterol/metabolismo
Cricetulus
Ativação Enzimática
Fibroblastos
Células HEK293
Seres Humanos
Alvo Mecanístico do Complexo 1 de Rapamicina
Camundongos
Complexos Multiproteicos/antagonistas & inibidores
Mutação
Transdução de Sinais
Serina-Treonina Quinases TOR/antagonistas & inibidores
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Amino Acid Transport Systems); 0 (Carrier Proteins); 0 (Cholesterol, HDL); 0 (Multiprotein Complexes); 0 (Nuclear Proteins); 0 (PICk1 protein, human); 0 (SLC38A9 protein, human); 97C5T2UQ7J (Cholesterol); EC 2.7.1.1 (TOR Serine-Threonine Kinases); EC 2.7.11.1 (Mechanistic Target of Rapamycin Complex 1)
[Em] Mês de entrada:1711
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170325
[St] Status:MEDLINE
[do] DOI:10.1126/science.aag1417



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