Drosophila insulin release is triggered by adipose Stunted ligand to brain Methuselah receptor

Science

Volumn 353, Issue 6307, 2016, Pages 1553-1556

  Delanoue, Renald ^a   Meschi, Eleonora ^a   Agrawal, Neha ^a,c   Mauri, Alessandra ^a   Tsatskis, Yonit ^b   McNeill, Helen ^b   Léopold, Pierre ^a  

^a UNIVERSITÉ CÔTE D'AZUR   (France)

^b MOUNT SINAI HOSPITAL   (Canada)

^c UNIVERSITY OF CAMBRIDGE   (United Kingdom)

Author keywords

[No Author keywords available]

Indexed keywords

HORMONE RECEPTOR; INSULIN; LIGAND; METHUSELAH LIGAND STUNTED; METHUSELAH RECEPTOR; UNCLASSIFIED DRUG; DIAP2 PROTEIN, DROSOPHILA; DROSOPHILA PROTEIN; G PROTEIN COUPLED RECEPTOR; INCRETIN; INHIBITOR OF APOPTOSIS PROTEIN; MEMBRANE PROTEIN; METHUSELAH PROTEIN, DROSOPHILA; PGC PROTEIN, DROSOPHILA; POSITIVE TRANSCRIPTION ELONGATION FACTOR B; SECRETIN RECEPTOR; SUNGLASSES PROTEIN, DROSOPHILA; TARGET OF RAPAMYCIN KINASE; TARGET OF RAPAMYCIN PROTEIN, DROSOPHILA;

AMINO ACID; BODY SIZE; BRAIN; CELLS AND CELL COMPONENTS; FAT; FLY; GENETIC ANALYSIS; GROWTH RATE; HORMONE; LIGAND; NUTRIENT; PEPTIDE; PHYSIOLOGICAL RESPONSE; SECRETION;

ADIPOCYTE; ANIMAL EXPERIMENT; ARTICLE; CONTROLLED STUDY; DROSOPHILA MOJAVENSIS; GENOTYPE; INSULIN RELEASE; NONHUMAN; ORGAN CULTURE; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN SECRETION; ADIPOSE TISSUE; ANIMAL; BRAIN; DIET RESTRICTION; DROSOPHILA MELANOGASTER; EATING; FAT PAD; FOOD; GENETICS; GROWTH, DEVELOPMENT AND AGING; HEMOLYMPH; METABOLISM; ORGAN CULTURE TECHNIQUE; PUPA;

ANIMALIA;

ADIPOSE TISSUE; ANIMALS; BRAIN; DROSOPHILA MELANOGASTER; DROSOPHILA PROTEINS; EATING; FASTING; FAT BODY; FOOD; HEMOLYMPH; INCRETINS; INHIBITOR OF APOPTOSIS PROTEINS; INSULIN; LIGANDS; MEMBRANE PROTEINS; ORGAN CULTURE TECHNIQUES; POSITIVE TRANSCRIPTIONAL ELONGATION FACTOR B; PUPA; RECEPTORS, G-PROTEIN-COUPLED; RECEPTORS, GASTROINTESTINAL HORMONE; TOR SERINE-THREONINE KINASES;

EID: 84988984913     PISSN: 00368075     EISSN: 10959203     Source Type: Journal    
DOI: 10.1126/science.aaf8430     Document Type: Article

References (24)

1. D. S. Andersen, J. Colombani, P. Léopold, Trends Cell Biol. 23, 336-344 (2013).
2. J. S. Britton, B. A. Edgar, Development 125, 2149-2158 (1998).
3. J. Colombani et al., Cell 114, 739-749 (2003).
4. J. F. Martin, E. Hersperger, A. Simcox, A. Shearn, Mech. Dev. 92, 155-167 (2000).
5. A. Rajan, N. Perrimon, Cell 151, 123-137 (2012).
6. H. Sano et al., PLOS Genet. 11, e1005209 (2015).
7. C. Géminard, E. J. Rulifson, P. Léopold, Cell Metab. 10, 199-207 (2009).
8. T. Koyama, C. K. Mirth, PLOS Biol. 14, e1002392 (2016).
9. A. R. Araújo et al., PLOS ONE 8, e63747 (2013).
10. Y. J. Lin, L. Seroude, S. Benzer, Science 282, 943-946 (1998).
11. W. Song et al., Neuron 36, 105-119 (2002).
12. A. P. West Jr., L. L. Llamas, P. M. Snow, S. Benzer, P. J. Bjorkman, Proc. Natl. Acad. Sci. U.S.A. 98, 3744-3749 (2001).
13. L. E. Gimenez et al., Aging Cell 12, 121-129 (2013).
14. S. Cvejic, Z. Zhu, S. J. Felice, Y. Berman, X. Y. Huang, Nat. Cell Biol. 6, 540-546 (2004).
15. W. W. Ja, G. B. Carvalho, M. Madrigal, R. W. Roberts, S. Benzer, Protein Sci. 18, 2203-2208 (2009).
16. B. Gershman et al., Physiol. Genomics 29, 24-34 (2007).
17. T. Kidd et al., Genetics 170, 697-708 (2005).
18. L. L. Fruttero, D. R. Demartini, E. R. Rubiolo, C. R. Carlini, L. E. Canavoso, Insect Biochem. Mol. Biol. 52, 1-12 (2014).
19. L. Giot et al., Science 302, 1727-1736 (2003).
20. L. O. Martinez et al., Nature 421, 75-79 (2003).
21. M. Zalewska et al., Biochim. Biophys. Acta 1788, 1695-1705 (2009).
22. T. Osanai et al., Circulation 104, 3132-3136 (2001).
23. M. Brankatschk, S. Dunst, L. Nemetschke, S. Eaton, eLife 3, e02862 (2014).
24. N. Agrawal et al., Cell Metab. 23, 675-684 (2016).