Evidence for leptin receptor isoforms heteromerization at the cell surface

FEBS Letters

Volumn 584, Issue 11, 2010, Pages 2213-2217

  Bacart, Johan ^a   Leloire, Audrey ^a   Levoye, Angélique ^b   Froguel, Philippe ^a,c   Jockers, Ralf ^d,e   Couturier, Cyril ^a  

^a Institut Pasteur de Lille   (France)

^b INSTITUT PASTEUR   (France)

^c HAMMERSMITH HOSPITAL   (United Kingdom)

^d INSTITUT COCHIN   (France)

^e INSERM   (France)

Author keywords

Bioluminescence resonance energy transfer; Heteromerization; LEPR; Obesity; Protein protein interaction; Yellow fluorescent Protein for energy transfer

Indexed keywords

LEPTIN; LEPTIN RECEPTOR; LEPTIN RECEPTOR A; LEPTIN RECEPTOR B; LEPTIN RECEPTOR C; UNCLASSIFIED DRUG;

ARTICLE; BIOLUMINESCENCE RESONANCE ENERGY TRANSFER; CELL MEMBRANE; CELL SURFACE; CELLULAR DISTRIBUTION; CONTROLLED STUDY; HUMAN; HUMAN CELL; IMMUNOPRECIPITATION; PRIORITY JOURNAL; PROTEIN EXPRESSION; PROTEIN LOCALIZATION;

EID: 77952956961     PISSN: 00145793     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.febslet.2010.03.033     Document Type: Article

References (22)

1. Tartaglia L.A. The leptin receptor. J. Biol. Chem. 1997, 272:6093-6096.
2. Ahima R.S., Flier J.S. Leptin. Annu. Rev. Physiol. 2000, 62:413-437.
3. Fruhbeck G. Intracellular signalling pathways activated by leptin. Biochem. J. 2006, 393:7-20.
4. Nakashima K., Narazaki M., Taga T. Leptin receptor (OB-R) oligomerizes with itself but not with its closely related cytokine signal transducer gp130. FEBS Lett. 1997, 403:79-82.
5. Devos R., Guisez Y., Van der Heyden J., White D.W., Kalai M., Fountoulakis M., Plaetinck G. Ligand-independent dimerization of the extracellular domain of the leptin receptor and determination of the stoichiometry of leptin binding. J. Biol. Chem. 1997, 272:18304-18310.
6. White D.W., Tartaglia L.A. Evidence for ligand-independent homo-oligomerization of leptin receptor (OB-R) isoforms: a proposed mechanism permitting productive long-form signaling in the presence of excess short-form expression. J. Cell. Biochem. 1999, 73:278-288.
7. Couturier C., Jockers R. Activation of the leptin receptor by a ligand-induced conformational change of constitutive receptor dimers. J. Biol. Chem. 2003, 278:26604-26611.
8. Biener E., et al. Quantitative FRET imaging of leptin receptor oligomerization kinetics in single cells. Biol. Cell 2005, 97:905-919.
9. Zabeau L., Defeau D., Iserentant H., Vandekerckhove J., Peelman F., Tavernier J. Leptin receptor activation depends on critical cysteine residues in its fibronectin type III subdomains. J. Biol. Chem. 2005, 280:22632-22640.
10. Chen H., et al. Evidence that the diabetes gene encodes the leptin receptor: identification of a mutation in the leptin receptor gene in db/db mice. Cell 1996, 84:491-495.
11. Fei H., Okano H.J., Li C., Lee G.H., Zhao C., Darnell R., Friedman J.M. Anatomic localization of alternatively spliced leptin receptors (Ob-R) in mouse brain and other tissues. Proc. Natl. Acad. Sci. USA 1997, 94:7001-7005.
12. Lollmann B., Gruninger S., Stricker-Krongrad A., Chiesi M. Detection and quantification of the leptin receptor splice variants Ob-Ra, b, and, e in different mouse tissues. Biochem. Biophys. Res. Commun. 1997, 238:648-652.
13. Ayoub M.A., Couturier C., Lucas-Meunier E., Angers S., Fossier P., Bouvier M., Jockers R. Monitoring of ligand-independent dimerization and ligand-induced conformational changes of melatonin receptors in living cells by bioluminescence resonance energy transfer. J. Biol. Chem. 2002, 277:21522-21528.
14. Bacart J., Corbel C., Jockers R., Bach S., Couturier C. The BRET technology and its application to screening assays. Biotechnol. J. 2008, 3:311-324.
15. Kamal M., Marquez M., Vauthier V., Leloire A., Froguel P., Jockers R., Couturier C. Improved donor/acceptor BRET couples for monitoring beta-arrestin recruitment to G protein-coupled receptors. Biotechnol. J. 2009, 4:1337-1344.
16. Couturier C., et al. Silencing of OB-RGRP in mouse hypothalamic arcuate nucleus increases leptin receptor signaling and prevents diet-induced obesity. Proc. Natl. Acad. Sci. USA 2007, 104:19476-19481.
17. Belouzard S., Delcroix D., Rouille Y. Low levels of expression of leptin receptor at the cell surface result from constitutive endocytosis and intracellular retention in the biosynthetic pathway. J. Biol. Chem. 2004, 279:28499-28508.
18. White D.W., Kuropatwinski K.K., Devos R., Baumann H., Tartaglia L.A. Leptin receptor (OB-R) signaling. Cytoplasmic domain mutational analysis and evidence for receptor homo-oligomerization. J. Biol. Chem. 1997, 272:4065-4071.
19. Peelman F., Couturier C., Dam J., Zabeau L., Tavernier J., Jockers R. Techniques: new pharmacological perspectives for the leptin receptor. Trends Pharmacol. Sci. 2006, 27:218-225.
20. Bahrenberg G., Behrmann I., Barthel A., Hekerman P., Heinrich P.C., Joost H.G., Becker W. Identification of the critical sequence elements in the cytoplasmic domain of leptin receptor isoforms required for Janus kinase/signal transducer and activator of transcription activation by receptor heterodimers. Mol. Endocrinol. 2002, 16:859-872.
21. Kloek C., Haq A.K., Dunn S.L., Lavery H.J., Banks A.S., Myers M.G. Regulation of Jak kinases by intracellular leptin receptor sequences. J. Biol. Chem. 2002, 277:41547-41555.
22. Belouzard S., Rouille Y. Ubiquitylation of leptin receptor OB-Ra regulates its clathrin-mediated endocytosis. EMBO J. 2006, 25:932-942.