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animals (16) 16
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1. Full Text Clinical or ATPase domain mutations in ABCD4 disrupt the interaction between the Vitamin B12-trafficking proteins ABCD4 and LMBD1
by Fettelschoss, Victoria and Burda, Patricie and Sagné, Corinne and Coelho, David and De Laet, Corinne and Lutz, Seraina and Suormala, Terttu and Fowler, Brian and Pietrancosta, Nicolas and Gasnier, Bruno and Bornhauser, Beat and Froese, D. Sean and Baumgartner, Matthias R
Journal of Biological Chemistry, ISSN 0021-9258, 07/2017, Volume 292, Issue 28, pp. 11980 - 11991
Vitamin B 12 (cobalamin (Cbl)), in the cofactor forms methyl-Cbl and adenosyl-Cbl, is required for the function of the essential enzymes methionine synthase... 
ABCD4 | Molecular Bases of Disease | homology modeling | cblJ | fluorescence resonance energy transfer (FRET) | cblF | protein-protein interaction | vitamin B12 | inborn error of metabolism | LMBD1 | ABC transporter
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2. Full Text SNAT7 is the primary lysosomal glutamine exporter required for extracellular protein-dependent growth of cancer cells
by Verdon, Quentin and Boonen, Marielle and Ribes, Christopher and Jadot, Michel and Gasnier, Bruno and Sagné, Corinne
Proceedings of the National Academy of Sciences of the United States of America, ISSN 0027-8424, 05/2017, Volume 114, Issue 18, pp. E3602 - E3611
Lysosomes degrade cellular components sequestered by autophagy or extracellular material internalized by endocytosis and phagocytosis. The macromolecule... 
Cell nutrition | Transporter | Lysosome | Cancer | Glutamine | RAS | cell nutrition | MULTIDISCIPLINARY SCIENCES | TFEB | MECHANISMS | glutamine | IDENTIFICATION | FIBROBLASTS | MTORC1 | AMINO-ACIDS | transporter | VITAMIN-B-12 METABOLISM | TRANSCRIPTIONAL CONTROL | cancer | lysosome | Neoplasms - metabolism | Humans | Lysosomes - genetics | Glutamine - metabolism | Tumor Microenvironment | Amino Acid Transport Systems, Neutral - metabolism | Neoplasm Proteins - metabolism | Amino Acid Transport Systems, Neutral - genetics | Lysosomes - metabolism | Neoplasms - genetics | Glutamine - genetics | Lysosomes - pathology | HeLa Cells | Neoplasm Proteins - genetics | Neoplasms - pathology | Intracellular Membranes - metabolism | Extracellular matrix | Health aspects | Cancer cells | Biological Sciences | PNAS Plus
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3. Full Text An extended proteome map of the lysosomal membrane reveals novel potential transporters
by Chapel, Agnès and Kieffer-Jaquinod, Sylvie and Sagné, Corinne and Verdon, Quentin and Ivaldi, Corinne and Mellal, Mourad and Thirion, Jaqueline and Jadot, Michel and Bruley, Christophe and Garin, Jérôme and Gasnier, Bruno and Journet, Agnès
Molecular and Cellular Proteomics, ISSN 1535-9476, 06/2013, Volume 12, Issue 6, pp. 1572 - 1588
Lysosomes are membrane-bound endocytic organelles that play a major role in degrading cell macromolecules and recycling their building blocks. A comprehensive... 
MOLECULAR CHARACTERIZATION | LATE ENDOSOMES | SHOTGUN PROTEOMICS | AMINO-ACIDS | BIOCHEMICAL RESEARCH METHODS | VITAMIN-B-12 METABOLISM | ENDOPLASMIC-RETICULUM | PROTEINS | IDENTIFICATION | MASS-SPECTROMETRY | PHAGOSOMAL PROTEOME | Biomarkers - metabolism | Gene Expression | Proteome - genetics | Lysosome-Associated Membrane Glycoproteins - metabolism | Lysosomes - chemistry | Rats, Wistar | Humans | Liver - metabolism | Molecular Sequence Annotation | Membrane Transport Proteins - isolation & purification | Rats | Male | Hepatocytes - metabolism | Intracellular Membranes - chemistry | Liver - chemistry | Animals | Membrane Transport Proteins - genetics | Lysosome-Associated Membrane Glycoproteins - genetics | Membrane Transport Proteins - metabolism | Hepatocytes - chemistry | HeLa Cells | Proteome - isolation & purification | Proteome - metabolism | Microscopy, Fluorescence | Research
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4. Full Text Molecular and cellular basis of lysosomal transmembrane protein dysfunction
by Ruivo, Raquel and Anne, Christine and Sagné, Corinne and Gasnier, Bruno
BBA - Molecular Cell Research, ISSN 0167-4889, 2009, Volume 1793, Issue 4, pp. 636 - 649
Lysosomal membrane proteins act at several crucial steps of the lysosome life cycle, including lumen acidification, metabolite export, molecular motor... 
TRPML1 | HGSNAT | ClC-7 | Lysosomal storage disorder | Channel | Sanfilippo C syndrome | Infantile sialic acid disorder | Mucopolysaccharidosis | Danon disease | Cystinosis | Mucolipidosis type IV | Sialin | Mucolipin | Cobalamin F type disease | Osteopetrosis | LAMP2 | Lysosomal membrane | Salla disease | Ostm1 | Transporter | Cystinosin | AUTOSOMAL RECESSIVE OSTEOPETROSIS | CELL BIOLOGY | ACID-STORAGE DISEASES | CIC-7 | MUCOLIPIDOSIS TYPE-IV | BIOCHEMISTRY & MOLECULAR BIOLOGY | ACETYL-COENZYME-A | GLUCOSAMINIDE N-ACETYLTRANSFERASE | CLC CL-CHANNELS | VARITINT-WADDLER PHENOTYPE | PICK C1 DISEASE | RECEPTOR POTENTIAL CHANNEL | INTEGRAL MEMBRANE-PROTEIN | Animals | Lysosomes - metabolism | Proteins - metabolism | Biological Transport | Lysosomal Storage Diseases - physiopathology | Humans | Lysosomal Storage Diseases - metabolism | Membrane Proteins - metabolism | Autophagy | Lysosomal Storage Diseases - pathology | Cysteine | Sugars | Dynein | Monosaccharides | Membrane proteins | Membrane Proteins | Proteins | Life Sciences | Lysosomal Storage Diseases | Biochemistry, Molecular Biology | Lysosomes
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5. Full Text Severe Serotonin Depletion after Conditional Deletion of the Vesicular Monoamine Transporter 2 Gene in Serotonin Neurons: Neural and Behavioral Consequences
by Narboux-Nême, Nicolas and Sagné, Corinne and Doly, Stephane and Diaz, Silvina L and Martin, Cédric B P and Angenard, Gaelle and Martres, Marie-Pascale and Giros, Bruno and Hamon, Michel and Lanfumey, Laurence and Gaspar, Patricia and Mongeau, Raymond
Neuropsychopharmacology, ISSN 0893-133X, 11/2011, Volume 36, Issue 12, pp. 2538 - 2550
The vesicular monoamine transporter type 2 gene (VMAT2) has a crucial role in the storage and synaptic release of all monoamines, including serotonin (5-HT).... 
anxiety | conditional knockout mice | raphe | depression | serotonin transporter | defense behaviors | PSYCHIATRY | DORSAL RAPHE | RELEASE | NEUROSCIENCES | MICE LACKING | OXIDASE-A | EXPERIMENTAL-MODEL | DOPAMINE | RECEPTOR ACTIVATION | PHARMACOLOGY & PHARMACY | RAT-BRAIN | 5-HT | ANXIETY-LIKE | Severity of Illness Index | Serotonin - genetics | Mice, Inbred C57BL | Male | Mice, Transgenic | Escape Reaction - physiology | Serotonergic Neurons - metabolism | Animals | Vesicular Monoamine Transport Proteins - deficiency | Gene Deletion | Vesicular Monoamine Transport Proteins - genetics | Mice | Serotonergic Neurons - pathology | Serotonin - deficiency | Life Sciences | Pharmacology | Pharmaceutical sciences | biological psychiatry | vesicular monoamine transporter | animal models | knockout mice | mood | stress disorders | 5-HT1a receptors | serotonin | Original
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6. Full Text Mechanism of proton/substrate coupling in the heptahelical lysosomal transporter cystinosin
by Raquel Ruivo and Gian Carlo Bellenchi and Xiong Chen and Giovanni Zifarelli and Corinne Sagné and Cécile Debacker and Michael Pusch and Stéphane Supplisson and Bruno Gasnier
Proceedings of the National Academy of Sciences, ISSN 0027-8424, 01/2012, Volume 109, Issue 5, pp. E210 - E217
Secondary active transporters use electrochemical gradients provided by primary ion pumps to translocate metabolites or drugs “uphill” across membranes. Here... 
MULTIDISCIPLINARY SCIENCES | GLUTAMATE TRANSPORTER | VOLTAGE-DEPENDENCE | CL-COTRANSPORT FUNCTION | CONGENITAL DISORDER | PROTON CHANNELS | CHLORIDE CHANNEL | ION PERMEATION | MUTATIONS | ELECTROGENIC PROPERTIES | PUMP | Protons | Amino Acid Sequence | Amino Acid Transport Systems, Neutral - chemistry | Humans | Molecular Sequence Data | Substrate Specificity | Amino Acid Transport Systems, Neutral - metabolism | Amino Acid Transport Systems, Neutral - genetics | Sequence Homology, Amino Acid | Animals | Lysosomes - metabolism | Mutagenesis | Binding Sites | Index Medicus | PNAS Plus | Biological Sciences
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7. Full Text Identification of a putative lysosomal cobalamin exporter altered in the cblF defect of vitamin B12 metabolism
by Rutsch, Frank and Gailus, Susann and Miousse, Isabelle R and Suormala, Terttu and Sagné, Corinne and Toliat, Mohammad Reza and Nürnberg, Gudrun and Wittkampf, Tanja and Buers, Insa and Sharifi, Azita and Stucki, Martin and Becker, Christian and Baumgartner, Matthias and Robenek, Horst and Marquardt, Thorsten and Höhne, Wolfgang and Gasnier, Bruno and Rosenblatt, David S and Fowler, Brian and Nürnberg, Peter
Nature Genetics, ISSN 1061-4036, 02/2009, Volume 41, Issue 2, pp. 234 - 239
Vitamin B(12) (cobalamin) is essential in animals for metabolism of branched chain amino acids and odd chain fatty acids, and for remethylation of homocysteine... 
Vitamin B 12 Deficiency - etiology | Transcobalamins - genetics | Humans | Male | Methylmalonic Acid - metabolism | Proteins - isolation & purification | Tissue Distribution | Membrane Transport Proteins - deficiency | Membrane Transport Proteins - genetics | Transcobalamins - isolation & purification | Female | Membrane Transport Proteins - metabolism | Vitamin B 12 Deficiency - metabolism | Child | Methylmalonic Acid - urine | Chromosome Deletion | Lysosome-Associated Membrane Glycoproteins - metabolism | Nucleocytoplasmic Transport Proteins - physiology | Chromosome Mapping | Chromosomes, Human, Pair 6 | Nucleocytoplasmic Transport Proteins - genetics | Polymorphism, Genetic | Proteins - genetics | Nucleocytoplasmic Transport Proteins - metabolism | Proteins - metabolism | Transcobalamins - metabolism | Vitamin B 12 Deficiency - genetics | Hyperhomocysteinemia - genetics | HeLa Cells | Hyperhomocysteinemia - complications | Vitamin B 12 - metabolism | Medical research | Heart surgery | Genes | Vitamin B | Genetics | Medical screening | Chromosomes | Nucleocytoplasmic Transport Proteins | Biochemistry, Molecular Biology | Vitamin B 12 Deficiency | Proteins | Life Sciences | Membrane Transport Proteins | Transcobalamins | Vitamin B 12 | Hyperhomocysteinemia | Methylmalonic Acid | Lysosome-Associated Membrane Glycoproteins | Hela Cells
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8. Full Text Functional characterization of wild-type and mutant human sialin
by Gasnier, Bruno and Sagné, Corinne and Morin, Pierre
The EMBO Journal, ISSN 0261-4189, 11/2004, Volume 23, Issue 23, pp. 4560 - 4570
The modification of cell surface lipids or proteins with sialic acid is essential for many biological processes and several diseases are caused by defective... 
storage disease | sialin | sialic acid | lysosome | transporter | Storage disease | Sialin | Sialic acid | Transporter | Lysosome | ACID STORAGE DISEASE | PROTEIN | BIOCHEMISTRY & MOLECULAR BIOLOGY | GANGLIOSIDES | SALLA-DISEASE | MYELIN-ASSOCIATED GLYCOPROTEIN | FIBROBLASTS | CELL BIOLOGY | TRANSPORT | LYSOSOMES | MONOSACCHARIDES | DISORDER | Cell Line | Humans | Sialic Acids - metabolism | Sialic Acid Storage Disease - genetics | Organic Anion Transporters - metabolism | Symporters - metabolism | Amino Acid Motifs | Protein Transport | Endocytosis | Organic Anion Transporters - genetics | Symporters - genetics | Cloning, Molecular | Cell Membrane - metabolism | Mutation | Hydrogen-Ion Concentration
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9. Full Text Identification and Characterization of a Lysosomal Transporter for Small Neutral Amino Acids
by Corinne Sagné and Cendra Agulhon and Philippe Ravassard and Michele Darmon and Michel Hamon and Salah El Mestikawy and Bruno Gasnier and Bruno Giros
Proceedings of the National Academy of Sciences of the United States of America, ISSN 0027-8424, 6/2001, Volume 98, Issue 13, pp. 7206 - 7211
In eukaryotic cells, lysosomes represent a major site for macromolecule degradation. Hydrolysis products are eventually exported from this acidic organelle... 
COS cells | Brain | Biological Sciences | Messenger RNA | Neurons | Neuroglia | Lysosomes | Amino acids | Neutral amino acids | Hippocampus | FIBROBLAST LYSOSOMES | VESICULAR GABA | ARABIDOPSIS-THALIANA | CLONING | MEMBRANE | MULTIDISCIPLINARY SCIENCES | PERMEASE | DISORDERS | EXPRESSION | N-ACETYLNEURAMINIC ACID | MOLECULAR ANALYSIS | Proline - metabolism | gamma-Aminobutyric Acid - metabolism | Molecular Sequence Data | Male | Phylogeny | Cerebral Cortex - metabolism | Brain - metabolism | Lysosomes - metabolism | Transfection | Symporters | Cloning, Molecular | Carrier Proteins - chemistry | Recombinant Proteins - metabolism | Amino Acid Sequence | Cell Line | Amino Acid Transport Systems | Rats | Recombinant Proteins - chemistry | Alanine - metabolism | Rats, Sprague-Dawley | Sequence Homology, Amino Acid | Caenorhabditis elegans | Carrier Proteins - genetics | Hippocampus - metabolism | Sequence Alignment | Animals | Carrier Proteins - metabolism | Amino Acid Transport Systems, Neutral | Amino Acids, Neutral - metabolism | Kinetics | Drosophila melanogaster | Saccharomyces cerevisiae | Evolution, Molecular | Research | Eukaryotic cells | Macromolecules | Cellular control mechanisms
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10. Full Text Heptahelical protein PQLC2 is a lysosomal cationic amino acid exporter underlying the action of cysteamine in cystinosis therapy
by Adrien Jézégou and Elisa Llinares and Christine Anne and Sylvie Kieffer-Jaquinod and Seana O’Regan and Joëlle Aupetit and Allel Chabli and Corinne Sagné and Cécile Debacker and Bernadette Chadefaux-Vekemans and Agnès Journet and Bruno André and Bruno Gasnier
Proceedings of the National Academy of Sciences, ISSN 0027-8424, 12/2012, Volume 109, Issue 50, pp. E3434 - E3443
Cystinosin, the lysosomal cystine exporter defective in cystinosis, is the founding member of a family of heptahelical membrane proteins related to... 
Lysosomal storage disease | Secondary active transporter | lysosomal storage disease | SHOTGUN PROTEOMICS | secondary active transporter | MULTIDISCIPLINARY SCIENCES | FUNCTIONAL-CHARACTERIZATION | CONGENITAL DISORDER | NEPHROPATHIC CYSTINOSIS | SACCHAROMYCES-CEREVISIAE | MITOCHONDRIAL PYRUVATE CARRIER | GENE | ARGININE TRANSPORT | BATTEN-DISEASE | L-CANAVANINE | Amino Acid Transport Systems, Basic - genetics | Species Specificity | Saccharomyces cerevisiae - genetics | Caenorhabditis elegans Proteins - chemistry | Humans | DNA, Complementary - genetics | Caenorhabditis elegans Proteins - metabolism | Molecular Sequence Data | Cystinosis - drug therapy | Saccharomyces cerevisiae - metabolism | Base Sequence | Female | Genes, Fungal | Membrane Proteins - metabolism | Recombinant Proteins - metabolism | Amino Acid Sequence | Drosophila Proteins | DEAD-box RNA Helicases | Amino Acid Transport Systems, Basic - chemistry | Protein Structure, Secondary | Membrane Proteins - genetics | Oocytes - metabolism | Xenopus laevis | Rats | Recombinant Proteins - chemistry | Recombinant Proteins - genetics | Saccharomyces cerevisiae Proteins - genetics | Cystinosis - metabolism | Canavanine - metabolism | Amino Acid Motifs | Animals | Membrane Proteins - chemistry | Cysteamine - therapeutic use | Saccharomyces cerevisiae Proteins - metabolism | Vacuoles - metabolism | Electrophysiological Phenomena | Amino Acid Transport Systems, Basic - metabolism | Caenorhabditis elegans Proteins - genetics | Saccharomyces cerevisiae Proteins - chemistry | Life Sciences | Biochemistry, Molecular Biology | Genomics | Biological Sciences | PNAS Plus
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11. Full Text Clinical or ATPase domain mutations in ABCD4 disrupt the interaction between the vitamin B-12-trafficking proteins ABCD4 and LMBD1
by Fettelschoss, V and Burda, P and Sagne, C and Coelho, D and De Laet, C and Lutz, S and Suormala, T and Fowler, B and Pietrancosta, N and Gasnier, B and Bornhauser, B and Froese, DS and Baumgartner, MR
JOURNAL OF BIOLOGICAL CHEMISTRY, ISSN 0021-9258, 07/2017, Volume 292, Issue 28, pp. 11980 - 11991
Vitamin B-12 (cobalamin (Cbl)), in the cofactor forms methyl-Cbl and adenosyl-Cbl, is required for the function of the essential enzymes methionine synthase... 
ABCD4 | fluorescence resonance energy transfer (FRET) | BIOCHEMISTRY & MOLECULAR BIOLOGY | SUBCELLULAR-LOCALIZATION | FOLLOW-UP | inborn error of metabolism | BINDING CASSETTE PROTEIN | INBORN ERROR | GREEN FLUORESCENT PROTEIN | homology modeling | cblJ | vitamin B-12 | cblF | COENZYME B-12 | PEROXISOMAL MEMBRANE-PROTEIN | protein-protein interaction | ENDOPLASMIC-RETICULUM | LMBD1 | ABC transporter | METHYLMALONIC ACIDURIA | LIVING CELLS | Humans | Protein Multimerization | Lysosomes - enzymology | Recombinant Fusion Proteins - metabolism | ATP-Binding Cassette Transporters - deficiency | ATP-Binding Cassette Transporters - chemistry | Amino Acid Metabolism, Inborn Errors - metabolism | Lysosomes - metabolism | ATP-Binding Cassette Transporters - genetics | Amino Acid Metabolism, Inborn Errors - genetics | Nucleocytoplasmic Transport Proteins - chemistry | ATP-Binding Cassette Transporters - metabolism | Lysosomes - pathology | Protein Interaction Domains and Motifs | Amino Acid Metabolism, Inborn Errors - pathology | Catalytic Domain | Cells, Cultured | Metabolism, Inborn Errors - metabolism | Models, Molecular | Recombinant Fusion Proteins - chemistry | Metabolism, Inborn Errors - genetics | Nucleocytoplasmic Transport Proteins - genetics | Protein Transport | Nucleocytoplasmic Transport Proteins - metabolism | Luminescent Proteins - genetics | Protein Conformation | Molecular Docking Simulation | Nucleocytoplasmic Transport Proteins - deficiency | Structural Homology, Protein | HeLa Cells | Mutation | Metabolism, Inborn Errors - pathology | Vitamin B 12 - metabolism | Cell Line, Transformed | Amino Acid Substitution | Luminescent Proteins - metabolism | Life Sciences | Chemical Sciences
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12. SNAT7 is the primary lysosomal glutamine exporter required for extracellular protein-dependent growth of cancer cells
by Quentin Verdon and Marielle Boonen and Christopher Ribes and Michel Jadot and Bruno Gasnier and Corinne Sagné
Proceedings of the National Academy of Sciences of the United States of America, ISSN 0027-8424, 05/2017, Volume 114, Issue 18, p. E3602
Lysosomes degrade cellular components sequestered by autophagy or extracellular material internalized by endocytosis and phagocytosis. The macromolecule... 
Biodegradation | Fractionation | Lysosomes | Amino acids | Biosynthesis | Selectivity | pH effects | Autophagy | Cytosol | Proteins | Degradation | Hydrolysis | Molecules | Gene silencing | Endocytosis | Sodium | Asparagine | Localization | Transporter | Phagocytosis | Cancer | Glutamine
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13. Full Text Successful prediction of substrate-binding pocket in SLC17 transporter sialin
by Pietrancosta, Nicolas and Anne, Christine and Prescher, Horst and Ruivo, Raquel and Sagné, Corinne and Debacker, Cécile and Bertrand, Hugues-Olivier and Brossmer, Reinhard and Acher, Francine and Gasnier, Bruno
Journal of Biological Chemistry, ISSN 0021-9258, 03/2012, Volume 287, Issue 14, pp. 11489 - 11497
Secondary active transporters from the SLC17 protein family are required for excitatory and purinergic synaptic transmission, sialic acid metabolism, and renal... 
CELLS | PROTEIN | VESICULAR GLUTAMATE TRANSPORTERS | MECHANISM | ANALOGS | BIOCHEMISTRY & MOLECULAR BIOLOGY | ESCHERICHIA-COLI | BIOLOGICAL PROPERTIES | STORAGE DISORDERS | MAJOR FACILITATOR SUPERFAMILY