K. E. Mayo, L. J. Miller, D. Bataille, S. Dalle, B. Gö-ke et al., International Union of Pharmacology. XXXV. The Glucagon Receptor Family, Pharmacological Reviews, vol.55, issue.1, pp.167-194, 2003.
DOI : 10.1124/pr.55.1.6

K. L. Pierce, R. T. Premont, and R. J. Lefkowitz, Signalling: Seven-transmembrane receptors, Nature Reviews Molecular Cell Biology, vol.70, issue.9, pp.639-650, 2002.
DOI : 10.1038/nrm908

F. Authier, B. Desbuquois, D. Galle, and B. , Ligandmediated internalization of glucagon receptors in intact rat liver, Endocrinology, vol.131, pp.447-457, 1992.

J. J. Buggy, R. O. Heurich, M. Macdougall, K. A. Kelley, J. N. Livingston et al., Role of the Glucagon Receptor COOH-Terminal Domain in Glucagon-Mediated Signaling and Receptor Internalization, Diabetes, vol.46, issue.9, pp.1400-1405, 1997.
DOI : 10.2337/diab.46.9.1400

F. Authier, M. Janicot, F. Lederer, and B. Desbuquois, . Degradation of internalized ligand in the endosomal compartment, Biochemical Journal, vol.272, issue.3, pp.703-712, 1990.
DOI : 10.1042/bj2720703

F. Authier and B. Desbuquois, Degradation of glucagon in isolated liver endosomes. ATP-dependence and partial characterization of degradation products, Biochemical Journal, vol.280, issue.1, pp.211-218, 1991.
DOI : 10.1042/bj2800211

F. Authier, J. S. Mort, A. W. Bell, B. I. Posner, and J. J. Bergeron, Proteolysis of Glucagon within Hepatic Endosomes by Membrane-associated Cathepsins B and D, Journal of Biological Chemistry, vol.270, issue.26, pp.15798-15807, 1995.
DOI : 10.1074/jbc.270.26.15798

F. Authier, P. H. Cameron, C. Merlen, M. Kouach, and G. Briand, Endosomal Proteolysis of Glucagon at Neutral pH Generates the Bioactive Degradation Product Miniglucagon-(19???29), Endocrinology, vol.144, issue.12, pp.5353-5364, 2003.
DOI : 10.1210/en.2003-0543

B. Desbuquois, Iodoglucagon. Preparation and Characterization, European Journal of Biochemistry, vol.56, issue.2, pp.569-580, 1975.
DOI : 10.1016/0005-2795(68)90014-7

C. G. Unson, A. M. Cypess, C. Wu, P. K. Goldsmith, R. B. Merrifield et al., Antibodies against specific extracellular epitopes of the glucagon receptor block glucagon binding., Proc. Natl. Acad. Sci. USA 93, pp.310-315, 1996.
DOI : 10.1073/pnas.93.1.310

O. H. Lowry, N. J. Rosebrough, A. L. Farr, and R. J. Randall, Protein measurement with the Folin phenol reagent, J. Biol. Chem, vol.193, pp.265-275, 1951.

H. Beaufay, A. Amar-costesec, E. Feytmans, D. Thinès-sempoux, M. Wibo et al., ANALYTICAL STUDY OF MICROSOMES AND ISOLATED SUBCELLULAR MEMBRANES FROM RAT LIVER: I. Biochemical Methods, The Journal of Cell Biology, vol.61, issue.1, pp.188-200, 1974.
DOI : 10.1083/jcb.61.1.188

A. Trouet, [31] Isolation of modified liver lysosomes, Methods Enzymol, vol.31, pp.323-329, 1974.
DOI : 10.1016/0076-6879(74)31034-8

F. Authier, R. A. Rachubinski, B. I. Posner, and J. J. Bergeron, Endosomal proteolysis of insulin by an acidic thiol metalloprotease unrelated to insulin degrading enzyme, J. Biol. Chem, vol.269, pp.3010-3016, 1994.

D. M. Neville, Isolation of an organ specific protein antigen from cell-surface membrane rat liver, Biochimica et Biophysica Acta (BBA) - Protein Structure, vol.154, issue.3, pp.540-552, 1968.
DOI : 10.1016/0005-2795(68)90014-7

F. Authier, D. Guglielmo, G. M. Danielsen, G. M. Bergeron, and J. J. , Uptake and metabolic fate of [HisA8,HisB4,GluB10,HisB27]insulin in rat liver in vivo, Biochemical Journal, vol.332, issue.2, pp.421-430, 1998.
DOI : 10.1042/bj3320421

F. Authier, M. Métioui, A. W. Bell, and J. S. Mort, Negative Regulation of Epidermal Growth Factor Signaling by Selective Proteolytic Mechanisms in the Endosome Mediated by Cathepsin B, Journal of Biological Chemistry, vol.274, issue.47, pp.33723-33731, 1999.
DOI : 10.1074/jbc.274.47.33723

G. Chauvet, K. Tahiri, F. Authier, and B. Desbuquois, Endosome-lysosome transfer of insulin and glucagon in a liver cell-free system, European Journal of Biochemistry, vol.254, issue.3, pp.527-537, 1998.
DOI : 10.1046/j.1432-1327.1998.2540527.x

F. Authier and G. Chauvet, In vitro endosome-lysosome transfer of dephosphorylated EGF receptor and Shc in rat liver, FEBS Letters, vol.315, issue.1-2, pp.25-31, 1999.
DOI : 10.1016/S0014-5793(99)01413-1

R. W. Van-dyke, Heterotrimeric G protein subunits are located on rat liver endosomes, BMC Physiology, vol.4, issue.1, pp.1-16, 2004.
DOI : 10.1186/1472-6793-4-1

C. G. Unson, D. Andreu, E. M. Gurzenda, and R. B. Merrifield, Synthetic peptide antagonists of glucagon., Proc. Natl. Acad. Sci. USA, pp.4083-4087, 1987.
DOI : 10.1073/pnas.84.12.4083

C. G. Unson, E. M. Gurzenda, and R. B. Merrifield, Biological activities of des-His1[Glu9]glucagon amide, a glucagon antagonist, Peptides, vol.10, issue.6, pp.1171-1177, 1989.
DOI : 10.1016/0196-9781(89)90010-7

M. C. Lin, S. Nicosia, and M. Rodbell, Effects of iodination of tyrosyl residues on the binding and action of glucagon at its receptor, Biochemistry, vol.15, issue.20, pp.4537-4540, 1976.
DOI : 10.1021/bi00665a031

S. S. Ferguson, Evolving concepts in G protein-coupled receptor endocytosis: the role in receptor desensitization and signaling, Pharmacol. Rev, vol.53, pp.1-24, 2001.

R. O. Heurich, J. J. Buggy, M. T. Vandenberg, and A. J. Rossomando, Glucagon Induces a Rapid and Sustained Phosphorylation of the Human Glucagon Receptor in Chinese Hamster Ovary Cells, Biochemical and Biophysical Research Communications, vol.220, issue.3, pp.905-910, 1996.
DOI : 10.1006/bbrc.1996.0504

E. S. Tobias, E. Rozengurt, J. M. Connell, and M. D. Houslay, Co-transfection with protein kinase D confers phorbol-ester-mediated inhibition on glucagon-stimulated cAMP accumulation in COS cells transfected to overexpress glucagon receptors, Biochemical Journal, vol.326, issue.2, pp.545-551, 1997.
DOI : 10.1042/bj3260545

H. Attramadal, J. L. Arriza, C. Aoki, T. M. Dawson, J. Codina et al., ) b-arrestin 2, a novel member of the arrestin/b-arrestin gene family, J. Biol. Chem, vol.267, pp.17882-17890, 1992.

J. L. Estall, B. Yusta, and D. J. Drucker, Lipid Raft-dependent Glucagon-like Peptide-2 Receptor Trafficking Occurs Independently of Agonist-induced Desensitization, Molecular Biology of the Cell, vol.15, issue.8, pp.3673-3687, 2004.
DOI : 10.1091/mbc.E03-11-0825

P. Svoboda and J. Novotny, Hormone-induced subcellular redistribution of trimeric G proteins, Cellular and Molecular Life Sciences (CMLS), vol.59, issue.3, pp.501-512, 2002.
DOI : 10.1007/s00018-002-8441-7

K. Haraguchi and M. Rodbell, Isoproterenol stimulates shift of G proteins from plasma membrane to pinocytotic vesicles in rat adipocytes: a possible means of signal dissemination., Proc. Natl. Acad. Sci. USA, pp.1208-1212, 1990.
DOI : 10.1073/pnas.87.3.1208

P. Kvapil, J. Novotny, P. Svoboda, and L. A. Ransnas, The short and long forms of the a subunit of the stimulatory guanine nucleotide-binding protein are unequally redistributed during isoproterenol-mediated desensitization of intact S49 lymphoma cells, Eur. J. Biochem, vol.226, pp.193-199, 1994.

P. B. Wedegaertner, H. R. Bourne, and M. Von-zastrow, Activation-induced subcellular redistribution of Gs alpha., Molecular Biology of the Cell, vol.7, issue.8, pp.1225-1233, 1996.
DOI : 10.1091/mbc.7.8.1225

H. Cheng and M. G. Farquhar, Presence of adenylate cyclase activity in Golgi and other fractions from rat liver. I. Biochemical determination, The Journal of Cell Biology, vol.70, issue.3, pp.660-670, 1976.
DOI : 10.1083/jcb.70.3.660

M. Janicot, F. Fouque, and B. Desbuquois, Activation of rat liver adenylate cyclase by cholera toxin requires toxin internalization and processing in endosomes, J. Biol. Chem, vol.266, pp.12858-12865, 1991.

C. G. Unson, D. Macdonald, K. Ray, T. L. Durrah, and R. B. Merrifield, Position 9 replacement analogs of glucagon uncouple biological activity and receptor binding, J. Biol. Chem, vol.266, pp.2763-2766, 1991.