Hypothalamic mTOR signaling regulates food intake

Science

Volumn 312, Issue 5775, 2006, Pages 927-930

  Cota, Daniela ^a   Proulx, Karine ^a   Blake Smith, Kathi A ^a   Kozma, Sara C ^b   Thomas, George ^b   Woods, Stephen C ^a   Seeley, Randy J ^a  

^a UNIVERSITY OF CINCINNATI COLLEGE OF MEDICINE   (United States)

^b UNIVERSITY OF CINCINNATI   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

BIOMECHANICS; BRAIN; CELLS; ENZYMES; HORMONES; NEUROLOGY; SENSORS;

ANORECTIC EFFECT; CELL-CYCLE PROGRESSION; PROOPIOMELANOCORTIN NEURONS; TARGET OF RAPAMYCIN (MTOR) PROTEIN;

BIOELECTRIC POTENTIALS;

LEPTIN; LEUCINE; MAMMALIAN TARGET OF RAPAMYCIN; NEUROPEPTIDE Y; PROOPIOMELANOCORTIN;

BRAIN; ENERGY BALANCE; FOOD INTAKE; MAMMAL; NUTRIENT AVAILABILITY;

ANIMAL EXPERIMENT; ANIMAL TISSUE; ARCUATE NUCLEUS; ARTICLE; BODY WEIGHT; CALORIC INTAKE; CELL CYCLE PROGRESSION; CELL GROWTH; CONTROLLED STUDY; ENERGY; ENERGY BALANCE; ENZYME ACTIVITY; FOOD INTAKE; HYPOTHALAMUS; NERVE CELL; NONHUMAN; NUTRIENT AVAILABILITY; PRIORITY JOURNAL; PROTEIN LOCALIZATION; RAT; SATIETY; SIGNAL TRANSDUCTION;

ANIMALS; ARCUATE NUCLEUS; EATING; ENERGY INTAKE; ENERGY METABOLISM; FASTING; HYPOTHALAMUS; INJECTIONS, INTRAVENTRICULAR; LEPTIN; LEUCINE; NEURONS; NEUROPEPTIDE Y; PHOSPHORYLATION; PROTEIN KINASES; RATS; RATS, LONG-EVANS; RIBOSOMAL PROTEIN S6; RIBOSOMAL PROTEIN S6 KINASES; SIGNAL TRANSDUCTION; SIROLIMUS; STAT3 TRANSCRIPTION FACTOR; VALINE; WEIGHT LOSS;

MAMMALIA;

EID: 33646582664     PISSN: 00368075     EISSN: 10959203     Source Type: Journal    
DOI: 10.1126/science.1124147     Document Type: Article

References (29)

1. B. E. Levin, A. A. Dunn-Meynell, V. H. Routh, Int. Rev. Neurobiol. 51, 219 (2002).
2. S. Ritter, K. Bugarith, T. T. Dinh, J. Comp. Neurol. 432, 197 (2001).
3. R. J. Seeley, S. C. Woods, Nat. Rev. Neurosci. 4, 901 (2003).
4. D. M. Sabatini, H. Erdjument-Bromage, M. Lui, P. Tempst, S. H. Snyder, Cell 78, 35 (1994).
5. T. Schmelzle, M. N. Hall, Cell 103, 253 (2000).
6. E. Jacinto, M. N. Hall, Nat. Rev. Mol. Cell Biol. 4, 117 (2003).
7. P. B. Dennis et al., Science 294, 1102 (2001).
8. Y. G. Gangloff et al., Mol. Cell Biol. 24, 9508 (2004).
9. J. Montagne et al., Science 285, 2126 (1999).
10. B. D. Manning, J. Cell Biol. 167, 399 (2004).
11. K. Inoki, M. N. Corradetti, K. L. Guan, Nat. Genet. 37, 19 (2005).
12. L. Khamzina, A. Veilleux, S. Bergeron, A. Marette, Endocrinology 146, 1473 (2005).
13. S. H. Um et al., Nature 431, 200 (2004).
14. C. J. Sabers et al., J. Biol. Chem. 270, 815 (1995).
15. Materials and methods are available as supporting material on Science Online.
16. A. J. Meijer, P. F. Dubbelhuis, Biochem. Biophys. Res. Commun. 313, 397 (2004).
17. C. G. Proud, Eur. J. Biochem. 269, 5338 (2002).
18. M. A. Bjornsti, P. J. Houghton, Nat. Rev. Cancer 4, 335 (2004).
19. K. D. Niswender et al., Nature 413, 794 (2001).
20. K. D. Niswender et al., Diabetes 52, 227 (2003).
21. Q. Wu, Y. Zhang, J. Xu, P. Shen, Proc. Natl. Acad. Sci. U.S.A. 102, 13289 (2005).
22. T. K. Lam, G. J. Schwartz, L. Rossetti, Nat. Neurosci. 8, 579 (2005).
23. D. W. Gietzen, L. J. Magrum, J. Nutr. 131, 8515 (2001).
24. S. Pinto et al., Science 304, 110 (2004).
25. G. M. Schratt, E. A. Nigh, W. G. Chen, L. Hu, M. E. Greenberg, J. Neurosci. 24, 7366 (2004).
26. B. B. Kahn, T. Alquier, D. Carling, D. G. Hardie, Cell. Metab. 1, 15 (2005).
27. Y. Minokoshi et al., Nature 428, 569 (2004).
28. K. Inoki, T. Zhu, K. L. Guan, Cell 115, 577 (2003).
29. We thank L. De, E. Matter, K. Parks, J. Reed, E. Richer, D. Russell, J. Sorrell, and M. Toure for expert technical assistance; J. P. Herman and C. M. Padgett for assistance with artwork preparation; and H. Shi for assistance with the quantification of the immunohistochemistry. Supported by NIH grants DK 17844, DK 54080, and DK 54890. G.T. receives research support from Novartis.