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Publication DateScience, ISSN 0036-8075, 8/2010, Volume 329, Issue 5995, pp. 1085 - 1088
Recognition of lipids by proteins is important for their targeting and activation in many signaling pathways, but the mechanisms that regulate such...
Inositols | Yeasts | Medical research | Starvation | Cell growth | Cell nucleus | REPORTS | Lipids | Phospholipids | Lipid metabolism | YEAST | LOCALIZATION | HOMEOSTASIS | PROTEIN | MULTIDISCIPLINARY SCIENCES | H+-ATPASE | VACUOLAR | SACCHAROMYCES-CEREVISIAE | TRANSCRIPTION FACTOR | Vacuolar Proton-Translocating ATPases - genetics | Inositol - metabolism | Saccharomyces cerevisiae - genetics | Endoplasmic Reticulum - metabolism | Recombinant Fusion Proteins - metabolism | Vacuolar Proton-Translocating ATPases - metabolism | Proton-Translocating ATPases - metabolism | Saccharomyces cerevisiae - metabolism | Cell Nucleus - metabolism | Proton-Translocating ATPases - genetics | Cation Transport Proteins - metabolism | Protein Phosphatase 1 - genetics | Cation Transport Proteins - genetics | Genes, Fungal | Transcription, Genetic | Cell Membrane - metabolism | Active Transport, Cell Nucleus | Repressor Proteins - metabolism | Gene Expression Regulation, Fungal | Signal Transduction | Repressor Proteins - genetics | Saccharomyces cerevisiae Proteins - genetics | Protein Phosphatase 1 - metabolism | Inositol - genetics | Saccharomyces cerevisiae Proteins - metabolism | Glucose - metabolism | Protein Binding | Liposomes - metabolism | Phosphatidic Acids - metabolism | Mutation | Saccharomyces cerevisiae - growth & development | Hydrogen-Ion Concentration | Proteins | Biosynthesis | Research | Metabolism | Signal transduction | Membranes | Biochemistry | Cellular biology
Inositols | Yeasts | Medical research | Starvation | Cell growth | Cell nucleus | REPORTS | Lipids | Phospholipids | Lipid metabolism | YEAST | LOCALIZATION | HOMEOSTASIS | PROTEIN | MULTIDISCIPLINARY SCIENCES | H+-ATPASE | VACUOLAR | SACCHAROMYCES-CEREVISIAE | TRANSCRIPTION FACTOR | Vacuolar Proton-Translocating ATPases - genetics | Inositol - metabolism | Saccharomyces cerevisiae - genetics | Endoplasmic Reticulum - metabolism | Recombinant Fusion Proteins - metabolism | Vacuolar Proton-Translocating ATPases - metabolism | Proton-Translocating ATPases - metabolism | Saccharomyces cerevisiae - metabolism | Cell Nucleus - metabolism | Proton-Translocating ATPases - genetics | Cation Transport Proteins - metabolism | Protein Phosphatase 1 - genetics | Cation Transport Proteins - genetics | Genes, Fungal | Transcription, Genetic | Cell Membrane - metabolism | Active Transport, Cell Nucleus | Repressor Proteins - metabolism | Gene Expression Regulation, Fungal | Signal Transduction | Repressor Proteins - genetics | Saccharomyces cerevisiae Proteins - genetics | Protein Phosphatase 1 - metabolism | Inositol - genetics | Saccharomyces cerevisiae Proteins - metabolism | Glucose - metabolism | Protein Binding | Liposomes - metabolism | Phosphatidic Acids - metabolism | Mutation | Saccharomyces cerevisiae - growth & development | Hydrogen-Ion Concentration | Proteins | Biosynthesis | Research | Metabolism | Signal transduction | Membranes | Biochemistry | Cellular biology
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Loading RightsScience, ISSN 0036-8075, 12/2010, Volume 330, Issue 6009, pp. 1344 - 1348
Autophagy is a process of self-cannibalization. Cells capture their own cytoplasm and organelles and consume them in lysosomes. The resulting breakdown...
REVIEWS | Starvation | Cellular metabolism | Liver | Lipids | Amino acids | Metabolic diseases | Nutrients | Lipid metabolism | Cancer | Tumors | PROTEIN | INSULIN-RESISTANCE | MULTIDISCIPLINARY SCIENCES | DEFICIENT | KEY ROLE | DEGRADATION | MICE | STARVATION | BETA-CELL MASS | PROMOTES | P62 | Neoplasms - metabolism | Disease | Signal Transduction | TOR Serine-Threonine Kinases - metabolism | Cell Survival | Humans | Phagosomes - metabolism | Homeostasis | Metabolism | Autophagy | Animals | Proteins - metabolism | Energy Metabolism | Neoplasms - pathology | Cell metabolism | Autophagy (Cytology) | Research | Properties | Cancer cells
REVIEWS | Starvation | Cellular metabolism | Liver | Lipids | Amino acids | Metabolic diseases | Nutrients | Lipid metabolism | Cancer | Tumors | PROTEIN | INSULIN-RESISTANCE | MULTIDISCIPLINARY SCIENCES | DEFICIENT | KEY ROLE | DEGRADATION | MICE | STARVATION | BETA-CELL MASS | PROMOTES | P62 | Neoplasms - metabolism | Disease | Signal Transduction | TOR Serine-Threonine Kinases - metabolism | Cell Survival | Humans | Phagosomes - metabolism | Homeostasis | Metabolism | Autophagy | Animals | Proteins - metabolism | Energy Metabolism | Neoplasms - pathology | Cell metabolism | Autophagy (Cytology) | Research | Properties | Cancer cells
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Loading RightsNature, ISSN 0028-0836, 04/2009, Volume 458, Issue 7242, pp. 1131 - 1135
The intracellular storage and utilization of lipids are critical to maintain cellular energy homeostasis. During nutrient deprivation, cellular lipids stored...
RAT-LIVER | CELLS | HEPATOCYTES | LIPOLYSIS | PHOSPHATIDYLINOSITOL 3-KINASE | MULTIDISCIPLINARY SCIENCES | DISEASE | LOW-DENSITY LIPOPROTEIN | STEATOHEPATITIS | STARVATION | TRIACYLGLYCEROL | Lipolysis - drug effects | Microtubule-Associated Proteins - genetics | Autophagy - physiology | Hepatocytes - metabolism | Autophagy - drug effects | Hepatocytes - cytology | Lysosomes - metabolism | Liver - drug effects | Dietary Fats - pharmacology | Food Deprivation | Microtubule-Associated Proteins - deficiency | Fatty Acids - metabolism | Hepatocytes - drug effects | Cell Line | Oxidation-Reduction | Liver - metabolism | Phagosomes - metabolism | Rats | Cholesterol - metabolism | Triglycerides - metabolism | Animals | Autophagy-Related Protein 5 | Lipid Metabolism - drug effects | Liver - cytology | Mice | Physiological aspects | Research | Lipid metabolism | Liver cells | Phagocytosis | Proteins | Lipids | Alternative energy sources | Metabolic syndrome | Rodents
RAT-LIVER | CELLS | HEPATOCYTES | LIPOLYSIS | PHOSPHATIDYLINOSITOL 3-KINASE | MULTIDISCIPLINARY SCIENCES | DISEASE | LOW-DENSITY LIPOPROTEIN | STEATOHEPATITIS | STARVATION | TRIACYLGLYCEROL | Lipolysis - drug effects | Microtubule-Associated Proteins - genetics | Autophagy - physiology | Hepatocytes - metabolism | Autophagy - drug effects | Hepatocytes - cytology | Lysosomes - metabolism | Liver - drug effects | Dietary Fats - pharmacology | Food Deprivation | Microtubule-Associated Proteins - deficiency | Fatty Acids - metabolism | Hepatocytes - drug effects | Cell Line | Oxidation-Reduction | Liver - metabolism | Phagosomes - metabolism | Rats | Cholesterol - metabolism | Triglycerides - metabolism | Animals | Autophagy-Related Protein 5 | Lipid Metabolism - drug effects | Liver - cytology | Mice | Physiological aspects | Research | Lipid metabolism | Liver cells | Phagocytosis | Proteins | Lipids | Alternative energy sources | Metabolic syndrome | Rodents
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Loading RightsScience, ISSN 0036-8075, 1/2011, Volume 331, Issue 6016, pp. 456 - 461
Adenosine monophosphate—activated protein kinase (AMPK) is a conserved sensor of intracellular energy activated in response to low nutrient availability and...
Birds of prey | Medical research | Phosphorylation | Starvation | Mitochondria | Hepatocytes | Complementary DNA | Liver | REPORTS | Cell lines | Vehicles | TARGET | CATALYTIC SUBUNIT | METFORMIN | COMPLEX | METABOLISM | ROLES | MULTIDISCIPLINARY SCIENCES | DISEASE | C-ELEGANS | AUTOPHAGY | DOMAINS | AMP-Activated Protein Kinases - metabolism | Mitochondria, Liver - metabolism | Sequestosome-1 Protein | Humans | Caenorhabditis elegans Proteins - metabolism | Intracellular Signaling Peptides and Proteins - metabolism | Hepatocytes - metabolism | Autophagy | Autophagy-Related Protein-1 Homolog | Intracellular Signaling Peptides and Proteins - genetics | Protein-Serine-Threonine Kinases - metabolism | Cell Line | Caenorhabditis elegans - metabolism | Signal Transduction | Cell Survival | Liver - metabolism | Metformin - pharmacology | Protein-Serine-Threonine Kinases - genetics | Phenformin - pharmacology | Transcription Factors - metabolism | Insulin - metabolism | Animals | Energy Metabolism | Intracellular Signaling Peptides and Proteins - chemistry | Mitochondria, Liver - ultrastructure | Cell Line, Tumor | Mice | Protein-Serine-Threonine Kinases - chemistry | Adaptor Proteins, Signal Transducing - metabolism | Caenorhabditis elegans Proteins - genetics | Autophagy (Cytology) | Research | Properties | Protein kinases
Birds of prey | Medical research | Phosphorylation | Starvation | Mitochondria | Hepatocytes | Complementary DNA | Liver | REPORTS | Cell lines | Vehicles | TARGET | CATALYTIC SUBUNIT | METFORMIN | COMPLEX | METABOLISM | ROLES | MULTIDISCIPLINARY SCIENCES | DISEASE | C-ELEGANS | AUTOPHAGY | DOMAINS | AMP-Activated Protein Kinases - metabolism | Mitochondria, Liver - metabolism | Sequestosome-1 Protein | Humans | Caenorhabditis elegans Proteins - metabolism | Intracellular Signaling Peptides and Proteins - metabolism | Hepatocytes - metabolism | Autophagy | Autophagy-Related Protein-1 Homolog | Intracellular Signaling Peptides and Proteins - genetics | Protein-Serine-Threonine Kinases - metabolism | Cell Line | Caenorhabditis elegans - metabolism | Signal Transduction | Cell Survival | Liver - metabolism | Metformin - pharmacology | Protein-Serine-Threonine Kinases - genetics | Phenformin - pharmacology | Transcription Factors - metabolism | Insulin - metabolism | Animals | Energy Metabolism | Intracellular Signaling Peptides and Proteins - chemistry | Mitochondria, Liver - ultrastructure | Cell Line, Tumor | Mice | Protein-Serine-Threonine Kinases - chemistry | Adaptor Proteins, Signal Transducing - metabolism | Caenorhabditis elegans Proteins - genetics | Autophagy (Cytology) | Research | Properties | Protein kinases
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Loading RightsThe Journal of Cell Biology, ISSN 0021-9525, 4/2009, Volume 185, Issue 2, pp. 305 - 321
Autophagy, an intracellular degradative pathway, maintains cell homeostasis under normal and stress conditions. Nascent double-membrane autophagosomes...
Starvation | Transferrins | 3T3 cells | Small interfering RNA | HeLa cells | Antibodies | CHO cells | Endosomes | Golgi apparatus | P branes | CORE MACHINERY | TRANSPORT | UNFOLDED PROTEIN RESPONSE | MULTIVESICULAR BODIES | MEMBRANE | EPSILON-COP | ENDOCYTIC PATHWAYS | BETA-COP | CELL MUTANT | GOLGI-COMPLEX | CELL BIOLOGY | Mannose-Binding Lectins - metabolism | RNA, Small Interfering - genetics | Membrane Glycoproteins - metabolism | Microtubule-Associated Proteins - genetics | Microtubule-Associated Proteins - metabolism | Sequestosome-1 Protein | Humans | Ubiquitin - metabolism | Autophagy - physiology | Coat Protein Complex I - metabolism | Recombinant Fusion Proteins - metabolism | Endosomes - metabolism | Protein Subunits - metabolism | Lysosomal-Associated Membrane Protein 1 - genetics | Membrane Proteins - metabolism | Protein Subunits - genetics | Biomarkers - metabolism | Cell Line | Membrane Proteins - genetics | Lysosomal-Associated Membrane Protein 2 - genetics | Phagosomes - metabolism | Ubiquitin - genetics | Coat Protein Complex I - genetics | Membrane Glycoproteins - genetics | Animals | Mannose-Binding Lectins - genetics | Adaptor Proteins, Signal Transducing - genetics | Recombinant Fusion Proteins - genetics | Golgi Apparatus - metabolism | Lysosomal-Associated Membrane Protein 1 - metabolism | Adaptor Proteins, Signal Transducing - metabolism | Transferrin - metabolism | Lysosomal-Associated Membrane Protein 2 - metabolism | RNA, Small Interfering - metabolism | Ubiquitin | Gas vesicles | Physiological aspects | Research | Phagocytosis | Proteins | Studies | Membranes | Biochemistry | Cells
Starvation | Transferrins | 3T3 cells | Small interfering RNA | HeLa cells | Antibodies | CHO cells | Endosomes | Golgi apparatus | P branes | CORE MACHINERY | TRANSPORT | UNFOLDED PROTEIN RESPONSE | MULTIVESICULAR BODIES | MEMBRANE | EPSILON-COP | ENDOCYTIC PATHWAYS | BETA-COP | CELL MUTANT | GOLGI-COMPLEX | CELL BIOLOGY | Mannose-Binding Lectins - metabolism | RNA, Small Interfering - genetics | Membrane Glycoproteins - metabolism | Microtubule-Associated Proteins - genetics | Microtubule-Associated Proteins - metabolism | Sequestosome-1 Protein | Humans | Ubiquitin - metabolism | Autophagy - physiology | Coat Protein Complex I - metabolism | Recombinant Fusion Proteins - metabolism | Endosomes - metabolism | Protein Subunits - metabolism | Lysosomal-Associated Membrane Protein 1 - genetics | Membrane Proteins - metabolism | Protein Subunits - genetics | Biomarkers - metabolism | Cell Line | Membrane Proteins - genetics | Lysosomal-Associated Membrane Protein 2 - genetics | Phagosomes - metabolism | Ubiquitin - genetics | Coat Protein Complex I - genetics | Membrane Glycoproteins - genetics | Animals | Mannose-Binding Lectins - genetics | Adaptor Proteins, Signal Transducing - genetics | Recombinant Fusion Proteins - genetics | Golgi Apparatus - metabolism | Lysosomal-Associated Membrane Protein 1 - metabolism | Adaptor Proteins, Signal Transducing - metabolism | Transferrin - metabolism | Lysosomal-Associated Membrane Protein 2 - metabolism | RNA, Small Interfering - metabolism | Ubiquitin | Gas vesicles | Physiological aspects | Research | Phagocytosis | Proteins | Studies | Membranes | Biochemistry | Cells
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Loading RightsDevelopmental Cell, ISSN 1534-5807, 04/2015, Volume 33, Issue 1, pp. 36 - 46
Organ wasting, related to changes in nutrition and metabolic activity of cells and tissues, is observed under conditions of starvation and in the context...
CANCER CACHEXIA | GENE | RNA-SEQ | MUSCLE ATROPHY | IN-VIVO | GROWTH | HIPPO PATHWAY | TUMOR-SUPPRESSOR | STEM-CELL PROLIFERATION | DEVELOPMENTAL BIOLOGY | DROSOPHILA | CELL BIOLOGY | Metabolomics | Wasting Syndrome - metabolism | Oligonucleotide Array Sequence Analysis | Male | Muscle, Skeletal - metabolism | Gene Expression Profiling | Stem Cells - cytology | Drosophila Proteins - metabolism | Muscle, Skeletal - cytology | Ovary - cytology | Stem Cells - metabolism | Drosophila melanogaster - genetics | Drosophila melanogaster - metabolism | Fat Body - cytology | Hyperglycemia - pathology | Trans-Activators - genetics | Female | Nuclear Proteins - genetics | Fat Body - metabolism | Insulin Secretion | Real-Time Polymerase Chain Reaction | Ovary - metabolism | Biomarkers - metabolism | RNA, Messenger - genetics | Cells, Cultured | Hemolymph - metabolism | Nuclear Proteins - metabolism | Reverse Transcriptase Polymerase Chain Reaction | Animals, Genetically Modified - metabolism | Blotting, Western | Gastrointestinal Tract - metabolism | Hyperglycemia - metabolism | Insulin - metabolism | Animals | Animals, Genetically Modified - growth & development | Animals, Genetically Modified - genetics | Insulin - chemistry | Drosophila melanogaster - growth & development | Trans-Activators - metabolism | Gastrointestinal Tract - cytology | Drosophila Proteins - genetics | Insulin-Like Growth Factor I - antagonists & inhibitors | Insulin-Like Growth Factor I - metabolism | Wasting Syndrome - pathology | Enzymes | Starvation | Analysis | Stem cells | Physiological aspects | Development and progression | Cellular signal transduction | Ovarian cancer | Medical colleges | Resveratrol
CANCER CACHEXIA | GENE | RNA-SEQ | MUSCLE ATROPHY | IN-VIVO | GROWTH | HIPPO PATHWAY | TUMOR-SUPPRESSOR | STEM-CELL PROLIFERATION | DEVELOPMENTAL BIOLOGY | DROSOPHILA | CELL BIOLOGY | Metabolomics | Wasting Syndrome - metabolism | Oligonucleotide Array Sequence Analysis | Male | Muscle, Skeletal - metabolism | Gene Expression Profiling | Stem Cells - cytology | Drosophila Proteins - metabolism | Muscle, Skeletal - cytology | Ovary - cytology | Stem Cells - metabolism | Drosophila melanogaster - genetics | Drosophila melanogaster - metabolism | Fat Body - cytology | Hyperglycemia - pathology | Trans-Activators - genetics | Female | Nuclear Proteins - genetics | Fat Body - metabolism | Insulin Secretion | Real-Time Polymerase Chain Reaction | Ovary - metabolism | Biomarkers - metabolism | RNA, Messenger - genetics | Cells, Cultured | Hemolymph - metabolism | Nuclear Proteins - metabolism | Reverse Transcriptase Polymerase Chain Reaction | Animals, Genetically Modified - metabolism | Blotting, Western | Gastrointestinal Tract - metabolism | Hyperglycemia - metabolism | Insulin - metabolism | Animals | Animals, Genetically Modified - growth & development | Animals, Genetically Modified - genetics | Insulin - chemistry | Drosophila melanogaster - growth & development | Trans-Activators - metabolism | Gastrointestinal Tract - cytology | Drosophila Proteins - genetics | Insulin-Like Growth Factor I - antagonists & inhibitors | Insulin-Like Growth Factor I - metabolism | Wasting Syndrome - pathology | Enzymes | Starvation | Analysis | Stem cells | Physiological aspects | Development and progression | Cellular signal transduction | Ovarian cancer | Medical colleges | Resveratrol
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Inflammasome-driven catecholamine catabolism in macrophages blunts lipolysis during ageing
Nature, ISSN 0028-0836, 10/2017, Volume 550, Issue 7674, pp. 119 - 123
Catecholamine-induced lipolysis, the first step in the generation of energy substrates by the hydrolysis of triglycerides(1), declines with age(2,3). The...
MONOAMINE-OXIDASE | CELLS | OBESITY | ACTIVATION | MULTIDISCIPLINARY SCIENCES | ACCUMULATION | IDENTIFICATION | GENE ONTOLOGY | DEFICIENCY | ADIPOSE-TISSUE | AGE | Inflammasomes - metabolism | Lipolysis - drug effects | Catecholamines - metabolism | Growth Differentiation Factor 3 - metabolism | Sterol Esterase - metabolism | Aging - drug effects | Adipose Tissue - cytology | Caspase 1 - metabolism | Gene Expression Profiling | Growth Differentiation Factor 3 - deficiency | Lipolysis - genetics | Adipose Tissue - metabolism | Aging - genetics | Monoamine Oxidase Inhibitors - pharmacology | NLR Family, Pyrin Domain-Containing 3 Protein - metabolism | Lipase - metabolism | NLR Family, Pyrin Domain-Containing 3 Protein - deficiency | Gene Expression Regulation - drug effects | Macrophages - metabolism | Animals | Norepinephrine - metabolism | Growth Differentiation Factor 3 - genetics | Adipocytes - metabolism | Mice | Adipose Tissue - drug effects | Catecholamines - pharmacology | Aging - metabolism | Monoamine Oxidase - metabolism | Aging | Observations | Catecholamine metabolism | Health aspects | Elderly people | Adipose tissue | Oxidase | Genomes | Adipocytes | Kinases | Macrophages | Lipase | Caspase-1 | Reduction | Energy resources | Clonal deletion | Deletion | Noradrenaline | Age | Enzymes | Starvation | Fasting | Body temperature | Aging (artificial) | Glycerol | Caspase | Principal components analysis | Triglycerides | Inflammation | Bioavailability | Metabolism | Gene expression | Sympathetic nervous system | Catecholamine | Fatty acids | Substrates | Lipolysis | Amine oxidase (flavin-containing) | Signaling | Catabolism | Norepinephrine | Elderly | Geriatrics
MONOAMINE-OXIDASE | CELLS | OBESITY | ACTIVATION | MULTIDISCIPLINARY SCIENCES | ACCUMULATION | IDENTIFICATION | GENE ONTOLOGY | DEFICIENCY | ADIPOSE-TISSUE | AGE | Inflammasomes - metabolism | Lipolysis - drug effects | Catecholamines - metabolism | Growth Differentiation Factor 3 - metabolism | Sterol Esterase - metabolism | Aging - drug effects | Adipose Tissue - cytology | Caspase 1 - metabolism | Gene Expression Profiling | Growth Differentiation Factor 3 - deficiency | Lipolysis - genetics | Adipose Tissue - metabolism | Aging - genetics | Monoamine Oxidase Inhibitors - pharmacology | NLR Family, Pyrin Domain-Containing 3 Protein - metabolism | Lipase - metabolism | NLR Family, Pyrin Domain-Containing 3 Protein - deficiency | Gene Expression Regulation - drug effects | Macrophages - metabolism | Animals | Norepinephrine - metabolism | Growth Differentiation Factor 3 - genetics | Adipocytes - metabolism | Mice | Adipose Tissue - drug effects | Catecholamines - pharmacology | Aging - metabolism | Monoamine Oxidase - metabolism | Aging | Observations | Catecholamine metabolism | Health aspects | Elderly people | Adipose tissue | Oxidase | Genomes | Adipocytes | Kinases | Macrophages | Lipase | Caspase-1 | Reduction | Energy resources | Clonal deletion | Deletion | Noradrenaline | Age | Enzymes | Starvation | Fasting | Body temperature | Aging (artificial) | Glycerol | Caspase | Principal components analysis | Triglycerides | Inflammation | Bioavailability | Metabolism | Gene expression | Sympathetic nervous system | Catecholamine | Fatty acids | Substrates | Lipolysis | Amine oxidase (flavin-containing) | Signaling | Catabolism | Norepinephrine | Elderly | Geriatrics
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Loading RightsPLoS ONE, ISSN 1932-6203, 04/2017, Volume 12, Issue 4, pp. e0173676 - e0173676
Autophagy is a catabolic mechanism to degrade cellular components to maintain cellular energy levels during starvation, a condition where PPAR alpha may be...
INSULIN SIGNALING TRANSDUCTION | GLUCOSE-HOMEOSTASIS | FIBROBLAST-GROWTH-FACTOR-21 | DEACETYLATION | METABOLISM | PATHWAY | STEATOSIS | MULTIDISCIPLINARY SCIENCES | RESISTANCE | RECEPTORS | FOXO1 | TOR Serine-Threonine Kinases - metabolism | Autophagy-Related Protein 7 - metabolism | Fibroblast Growth Factors - genetics | Autophagy-Related Protein 5 - genetics | fas Receptor - metabolism | Autophagy - drug effects | Fibroblast Growth Factors - metabolism | TOR Serine-Threonine Kinases - genetics | Liver - drug effects | fas Receptor - genetics | Autophagy - genetics | Proto-Oncogene Proteins c-akt - metabolism | Forkhead Box Protein O1 - metabolism | Signal Transduction | Liver - metabolism | PPAR alpha - genetics | Ubiquitin-Conjugating Enzymes - genetics | Stearoyl-CoA Desaturase - genetics | Mice, Knockout | Triglycerides - metabolism | Sequestosome-1 Protein - genetics | Ubiquitin-Conjugating Enzymes - metabolism | Cysteine Endopeptidases - genetics | Autophagy-Related Protein 5 - metabolism | Beclin-1 - genetics | Stearoyl-CoA Desaturase - metabolism | Mice | PPAR alpha - metabolism | Autophagy-Related Proteins - antagonists & inhibitors | Blood Glucose - metabolism | Autophagy-Related Proteins - metabolism | Forkhead Box Protein O1 - genetics | Autophagy-Related Protein 5 - antagonists & inhibitors | Microtubule-Associated Proteins - genetics | Microtubule-Associated Proteins - metabolism | Proto-Oncogene Proteins c-akt - genetics | Fenofibrate - pharmacology | Cysteine Endopeptidases - metabolism | Autophagy-Related Proteins - genetics | Sequestosome-1 Protein - metabolism | Sterol Regulatory Element Binding Protein 1 - metabolism | Autophagy-Related Protein 7 - antagonists & inhibitors | Mice, Inbred C57BL | Autophagy-Related Protein 7 - genetics | Gene Expression Regulation - drug effects | Animals | Sterol Regulatory Element Binding Protein 1 - genetics | PPAR alpha - agonists | Ubiquitin-Conjugating Enzymes - antagonists & inhibitors | Beclin-1 - metabolism | Transcription factors | Adipose tissue | Liver | Body weight | AKT protein | Biochemistry | Glucose | Assaying | Proteins | Signal transduction | Temperature effects | Fibroblasts | Physiology | Acetylation | Inhibition | Growth factors | Hepatotoxicity | Activation analysis | Methanol | Starvation | Ethanol | AMP | Metabolism | Insulin | Fatty acids | Studies | Acetaminophen | Food intake | Weight reduction | Animal welfare | Circulation | Drugs | Biotechnology | Drug abuse | Laboratories | Centrifugation | Glass | Homeostasis | Activation | Biology | Kinases | AMP-activated protein kinase | Autophagy | Nutrient status | Rodents | Nutrients | Oxidation | Heart diseases | Age | Epinephrine | AKT1 protein | Fasting | Chloroform | Diabetes mellitus | Cardiomyocytes | Acclimatization | Triglycerides | Pharmacology | Nitrogen | Calories | Medicine | Nuclear fuels | Protein kinase | Insulin resistance | Diabetes | Index Medicus
INSULIN SIGNALING TRANSDUCTION | GLUCOSE-HOMEOSTASIS | FIBROBLAST-GROWTH-FACTOR-21 | DEACETYLATION | METABOLISM | PATHWAY | STEATOSIS | MULTIDISCIPLINARY SCIENCES | RESISTANCE | RECEPTORS | FOXO1 | TOR Serine-Threonine Kinases - metabolism | Autophagy-Related Protein 7 - metabolism | Fibroblast Growth Factors - genetics | Autophagy-Related Protein 5 - genetics | fas Receptor - metabolism | Autophagy - drug effects | Fibroblast Growth Factors - metabolism | TOR Serine-Threonine Kinases - genetics | Liver - drug effects | fas Receptor - genetics | Autophagy - genetics | Proto-Oncogene Proteins c-akt - metabolism | Forkhead Box Protein O1 - metabolism | Signal Transduction | Liver - metabolism | PPAR alpha - genetics | Ubiquitin-Conjugating Enzymes - genetics | Stearoyl-CoA Desaturase - genetics | Mice, Knockout | Triglycerides - metabolism | Sequestosome-1 Protein - genetics | Ubiquitin-Conjugating Enzymes - metabolism | Cysteine Endopeptidases - genetics | Autophagy-Related Protein 5 - metabolism | Beclin-1 - genetics | Stearoyl-CoA Desaturase - metabolism | Mice | PPAR alpha - metabolism | Autophagy-Related Proteins - antagonists & inhibitors | Blood Glucose - metabolism | Autophagy-Related Proteins - metabolism | Forkhead Box Protein O1 - genetics | Autophagy-Related Protein 5 - antagonists & inhibitors | Microtubule-Associated Proteins - genetics | Microtubule-Associated Proteins - metabolism | Proto-Oncogene Proteins c-akt - genetics | Fenofibrate - pharmacology | Cysteine Endopeptidases - metabolism | Autophagy-Related Proteins - genetics | Sequestosome-1 Protein - metabolism | Sterol Regulatory Element Binding Protein 1 - metabolism | Autophagy-Related Protein 7 - antagonists & inhibitors | Mice, Inbred C57BL | Autophagy-Related Protein 7 - genetics | Gene Expression Regulation - drug effects | Animals | Sterol Regulatory Element Binding Protein 1 - genetics | PPAR alpha - agonists | Ubiquitin-Conjugating Enzymes - antagonists & inhibitors | Beclin-1 - metabolism | Transcription factors | Adipose tissue | Liver | Body weight | AKT protein | Biochemistry | Glucose | Assaying | Proteins | Signal transduction | Temperature effects | Fibroblasts | Physiology | Acetylation | Inhibition | Growth factors | Hepatotoxicity | Activation analysis | Methanol | Starvation | Ethanol | AMP | Metabolism | Insulin | Fatty acids | Studies | Acetaminophen | Food intake | Weight reduction | Animal welfare | Circulation | Drugs | Biotechnology | Drug abuse | Laboratories | Centrifugation | Glass | Homeostasis | Activation | Biology | Kinases | AMP-activated protein kinase | Autophagy | Nutrient status | Rodents | Nutrients | Oxidation | Heart diseases | Age | Epinephrine | AKT1 protein | Fasting | Chloroform | Diabetes mellitus | Cardiomyocytes | Acclimatization | Triglycerides | Pharmacology | Nitrogen | Calories | Medicine | Nuclear fuels | Protein kinase | Insulin resistance | Diabetes | Index Medicus
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Loading RightsEMBO reports, ISSN 1469-221X, 01/2018, Volume 19, Issue 1, pp. 57 - 72
Eukaryotic cells store lipids in cytosolic organelles known as lipid droplets ( LD s). Lipid droplet bud from the endoplasmic reticulum ( ER ), and may be...
lipid droplet | membrane contact site | nuclear | nutritional stress | vacuole junction | endoplasmic reticulum | nuclear ER–vacuole junction | STORAGE | BIOCHEMISTRY & MOLECULAR BIOLOGY | SACCHAROMYCES-CEREVISIAE | MASS-SPECTROMETRY | CELL BIOLOGY | YEAST | nuclear ER-vacuole junction | JUNCTIONS | SITES | SCALE | PROTEINS | EXPRESSION | Vacuoles - ultrastructure | Triglycerides - biosynthesis | Coenzyme A Ligases - genetics | Fatty Acid Synthases - metabolism | Cytosol - drug effects | Stress, Physiological | Endoplasmic Reticulum - metabolism | Saccharomyces cerevisiae - drug effects | Saccharomyces cerevisiae - ultrastructure | Time-Lapse Imaging | Vacuoles - drug effects | Endoplasmic Reticulum - ultrastructure | Coenzyme A Ligases - metabolism | Saccharomyces cerevisiae - metabolism | Lipid Droplets - ultrastructure | Cerulenin - pharmacology | Endoplasmic Reticulum - drug effects | Intermediate Filament Proteins - genetics | Lipid Metabolism - genetics | Glycerol - pharmacology | Acetic Acid - metabolism | Culture Media - chemistry | Lipid Droplets - metabolism | Fatty Acid Synthases - genetics | Gene Expression Regulation, Fungal | Transformation, Genetic | Lipid Droplets - drug effects | Acetic Acid - pharmacology | Glucose - pharmacology | Receptors, Cytoplasmic and Nuclear - genetics | Saccharomyces cerevisiae Proteins - genetics | Plasmids - metabolism | Glucose - deficiency | Glycerol - metabolism | Culture Media - pharmacology | Lipid Metabolism - drug effects | Plasmids - chemistry | Saccharomyces cerevisiae Proteins - metabolism | Vacuoles - metabolism | Cytosol - metabolism | Intermediate Filament Proteins - metabolism | Fatty Acids - biosynthesis | Receptors, Cytoplasmic and Nuclear - metabolism | Starvation | Nutrient deficiency | Yeast | Lipids | Tethering | Biosynthesis | Metabolism | Organelles | Fatty acids | Stress | Contact stresses | Budding | Endoplasmic reticulum | Membrane & Intracellular Transport
lipid droplet | membrane contact site | nuclear | nutritional stress | vacuole junction | endoplasmic reticulum | nuclear ER–vacuole junction | STORAGE | BIOCHEMISTRY & MOLECULAR BIOLOGY | SACCHAROMYCES-CEREVISIAE | MASS-SPECTROMETRY | CELL BIOLOGY | YEAST | nuclear ER-vacuole junction | JUNCTIONS | SITES | SCALE | PROTEINS | EXPRESSION | Vacuoles - ultrastructure | Triglycerides - biosynthesis | Coenzyme A Ligases - genetics | Fatty Acid Synthases - metabolism | Cytosol - drug effects | Stress, Physiological | Endoplasmic Reticulum - metabolism | Saccharomyces cerevisiae - drug effects | Saccharomyces cerevisiae - ultrastructure | Time-Lapse Imaging | Vacuoles - drug effects | Endoplasmic Reticulum - ultrastructure | Coenzyme A Ligases - metabolism | Saccharomyces cerevisiae - metabolism | Lipid Droplets - ultrastructure | Cerulenin - pharmacology | Endoplasmic Reticulum - drug effects | Intermediate Filament Proteins - genetics | Lipid Metabolism - genetics | Glycerol - pharmacology | Acetic Acid - metabolism | Culture Media - chemistry | Lipid Droplets - metabolism | Fatty Acid Synthases - genetics | Gene Expression Regulation, Fungal | Transformation, Genetic | Lipid Droplets - drug effects | Acetic Acid - pharmacology | Glucose - pharmacology | Receptors, Cytoplasmic and Nuclear - genetics | Saccharomyces cerevisiae Proteins - genetics | Plasmids - metabolism | Glucose - deficiency | Glycerol - metabolism | Culture Media - pharmacology | Lipid Metabolism - drug effects | Plasmids - chemistry | Saccharomyces cerevisiae Proteins - metabolism | Vacuoles - metabolism | Cytosol - metabolism | Intermediate Filament Proteins - metabolism | Fatty Acids - biosynthesis | Receptors, Cytoplasmic and Nuclear - metabolism | Starvation | Nutrient deficiency | Yeast | Lipids | Tethering | Biosynthesis | Metabolism | Organelles | Fatty acids | Stress | Contact stresses | Budding | Endoplasmic reticulum | Membrane & Intracellular Transport
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Loading RightsCell Metabolism, ISSN 1550-4131, 09/2014, Volume 20, Issue 3, pp. 526 - 540
AMPK and mTOR play principal roles in governing metabolic programs; however, mechanisms underlying the coordination of the two inversely regulated kinases...
GLUCOSE-HOMEOSTASIS | GROWTH-CONTROL | TUMOR-SUPPRESSOR COMPLEX | PROTEIN-KINASE CASCADE | RAG GTPASES | PHOSPHORYLATION | AMINO-ACIDS | ENDOCRINOLOGY & METABOLISM | TUBEROUS SCLEROSIS | EARLY ENDOSOME | ALLOSTERIC ACTIVATION | CELL BIOLOGY | Cell Line | AMP-Activated Protein Kinases - metabolism | Starvation | TOR Serine-Threonine Kinases - metabolism | Humans | Lysosomes - enzymology | Vacuolar Proton-Translocating ATPases - metabolism | Axin Protein - metabolism | Endosomes - metabolism | Mechanistic Target of Rapamycin Complex 1 | Multiprotein Complexes - metabolism | Animals | Lysosomes - metabolism | HEK293 Cells | Glucose - metabolism | Mice | Enzyme Activation | Adaptor Proteins, Signal Transducing - metabolism | Protein-Serine-Threonine Kinases - metabolism | Purines | Glucose metabolism | Safety and security measures | Glucose | Phosphotransferases | Dextrose | Adenosine triphosphatase | Food | Index Medicus
GLUCOSE-HOMEOSTASIS | GROWTH-CONTROL | TUMOR-SUPPRESSOR COMPLEX | PROTEIN-KINASE CASCADE | RAG GTPASES | PHOSPHORYLATION | AMINO-ACIDS | ENDOCRINOLOGY & METABOLISM | TUBEROUS SCLEROSIS | EARLY ENDOSOME | ALLOSTERIC ACTIVATION | CELL BIOLOGY | Cell Line | AMP-Activated Protein Kinases - metabolism | Starvation | TOR Serine-Threonine Kinases - metabolism | Humans | Lysosomes - enzymology | Vacuolar Proton-Translocating ATPases - metabolism | Axin Protein - metabolism | Endosomes - metabolism | Mechanistic Target of Rapamycin Complex 1 | Multiprotein Complexes - metabolism | Animals | Lysosomes - metabolism | HEK293 Cells | Glucose - metabolism | Mice | Enzyme Activation | Adaptor Proteins, Signal Transducing - metabolism | Protein-Serine-Threonine Kinases - metabolism | Purines | Glucose metabolism | Safety and security measures | Glucose | Phosphotransferases | Dextrose | Adenosine triphosphatase | Food | Index Medicus
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