메뉴 건너뛰기




Volumn 275, Issue 1 38-1, 1998, Pages

Identification of a domain in the carboxy terminus of CCK receptor that affects its intracellular trafficking

Author keywords

Cholecystokinin; Endocytosis; G protein coupled receptor; Receptor internalization; Receptor trafficking

Indexed keywords

CHOLECYSTOKININ; CHOLECYSTOKININ A RECEPTOR; INOSITOL 1,4,5 TRISPHOSPHATE;

EID: 0031859218     PISSN: 01931857     EISSN: None     Source Type: Journal    
DOI: 10.1152/ajpgi.1998.275.1.g56     Document Type: Article
Times cited : (16)

References (41)
  • 1
    • 0024997853 scopus 로고
    • Receptor-mediated internalization of insulin requires a 12-amino acid sequence in the juxtamembrane region of the insulin receptor beta-subunit
    • Backer, J. M., C. R. Kahn, D. A. Cahill, A. Ullrich, and M. F. White. Receptor-mediated internalization of insulin requires a 12-amino acid sequence in the juxtamembrane region of the insulin receptor beta-subunit. J. Biol. Chem. 265: 16450-16454, 1990.
    • (1990) J. Biol. Chem. , vol.265 , pp. 16450-16454
    • Backer, J.M.1    Kahn, C.R.2    Cahill, D.A.3    Ullrich, A.4    White, M.F.5
  • 3
    • 0027239858 scopus 로고
    • Serines and threonines in the gastrin-releasing peptide receptor carboxyl terminus mediate internalization
    • Benya, R. V., Z. Fathi, J. F. Battey, and R. T. Jensen. Serines and threonines in the gastrin-releasing peptide receptor carboxyl terminus mediate internalization. J. Biol. Chem. 268: 20285-20290, 1993.
    • (1993) J. Biol. Chem. , vol.268 , pp. 20285-20290
    • Benya, R.V.1    Fathi, Z.2    Battey, J.F.3    Jensen, R.T.4
  • 4
    • 0028815948 scopus 로고
    • Chronic desensitization and down-regulation of the gastrin-releasing peptide receptor are mediated by a protein kinase C-dependent mechanism
    • Benya, R. V., T. Kusui, J. F. Battey, and R. T. Jensen. Chronic desensitization and down-regulation of the gastrin-releasing peptide receptor are mediated by a protein kinase C-dependent mechanism. J. Biol. Chem. 270: 3346-3352, 1995.
    • (1995) J. Biol. Chem. , vol.270 , pp. 3346-3352
    • Benya, R.V.1    Kusui, T.2    Battey, J.F.3    Jensen, R.T.4
  • 5
    • 0024519834 scopus 로고
    • A simple, sensitive, and specific radioreceptor assay for inositol 1,4,5-trisphosphate in biological tissues
    • Bredt, D. S., R. J. Mourey, and S. H. Snyder. A simple, sensitive, and specific radioreceptor assay for inositol 1,4,5-trisphosphate in biological tissues. Biochem. Biophys. Res. Commun. 159: 976-982, 1989.
    • (1989) Biochem. Biophys. Res. Commun. , vol.159 , pp. 976-982
    • Bredt, D.S.1    Mourey, R.J.2    Snyder, S.H.3
  • 6
    • 0025250145 scopus 로고
    • NPXY, a sequence often found in cytoplasmic tails, is required for coated pit-mediated internalization of the low density lipoprotein receptor
    • Chen, W. J., J. L. Goldstein, and M. S. Brown. NPXY, a sequence often found in cytoplasmic tails, is required for coated pit-mediated internalization of the low density lipoprotein receptor. J. Biol. Chem. 265: 3116-3123, 1990.
    • (1990) J. Biol. Chem. , vol.265 , pp. 3116-3123
    • Chen, W.J.1    Goldstein, J.L.2    Brown, M.S.3
  • 7
    • 0030993001 scopus 로고    scopus 로고
    • Cellular handling of unoccupied and agonist-stimulated cholecystokinin receptor determined by immunolocalization
    • Gastrointest. Liver Physiol. 35
    • De Toledo, C. F., B. F. Roettger, C. Morys-Wortmann, W. E. Schmidt, and L. J. Miller. Cellular handling of unoccupied and agonist-stimulated cholecystokinin receptor determined by immunolocalization. Am. J. Physiol. 272 (Gastrointest. Liver Physiol. 35): G488-G497, 1997.
    • (1997) Am. J. Physiol. , vol.272
    • De Toledo, C.F.1    Roettger, B.F.2    Morys-Wortmann, C.3    Schmidt, W.E.4    Miller, L.J.5
  • 9
    • 0030593035 scopus 로고    scopus 로고
    • Role of β-arrestin in mediating agonist-promoted G protein-coupled receptor internalization
    • Ferguson, S. S. G., W. E. Downey III, A. M. Colapietro, L. S. Barak, L. Ménard, and M. G. Caron. Role of β-arrestin in mediating agonist-promoted G protein-coupled receptor internalization. Science 271: 363-366, 1996.
    • (1996) Science , vol.271 , pp. 363-366
    • Ferguson, S.S.G.1    Downey III, W.E.2    Colapietro, A.M.3    Barak, L.S.4    Ménard, L.5    Caron, M.G.6
  • 10
    • 0027243579 scopus 로고
    • Multiple kinases phosphorylate the pancreatic cholecystokinin receptor in an agonist-dependent manner
    • Gastrointest. Liver Physiol. 27
    • Gates, L. K., C. D. Ulrich, and L. J. Miller. Multiple kinases phosphorylate the pancreatic cholecystokinin receptor in an agonist-dependent manner. Am. J. Physiol. 264 (Gastrointest. Liver Physiol. 27): G840-G847, 1993.
    • (1993) Am. J. Physiol. , vol.264
    • Gates, L.K.1    Ulrich, C.D.2    Miller, L.J.3
  • 11
    • 0031149660 scopus 로고    scopus 로고
    • Quantitative dynamic multicompartmental analysis of cholecystokinin receptor movement in a living cell using dual fluorophores and reconstruction of confocal images
    • Go, W. Y., B. F. Roettger, E. L. Holicky, E. M. Hadac, and L. J. Miller. Quantitative dynamic multicompartmental analysis of cholecystokinin receptor movement in a living cell using dual fluorophores and reconstruction of confocal images. Anal. Biochem. 247: 210-215, 1997.
    • (1997) Anal. Biochem. , vol.247 , pp. 210-215
    • Go, W.Y.1    Roettger, B.F.2    Holicky, E.L.3    Hadac, E.M.4    Miller, L.J.5
  • 13
    • 0029791442 scopus 로고    scopus 로고
    • Relationship between native and recombinant cholecystokinin receptors: Role of differential glycosylation
    • Hadac, E. M., D. V. Ghanekar, E. L. Holicky, D. I. Pinon, R. W. Dougherty, and L. J. Miller. Relationship between native and recombinant cholecystokinin receptors: role of differential glycosylation. Pancreas 13: 130-139, 1996.
    • (1996) Pancreas , vol.13 , pp. 130-139
    • Hadac, E.M.1    Ghanekar, D.V.2    Holicky, E.L.3    Pinon, D.I.4    Dougherty, R.W.5    Miller, L.J.6
  • 14
    • 0029790078 scopus 로고    scopus 로고
    • Role of receptor phosphorylation in desensitization and internalization of the secretin receptor
    • Holtmann, M. H., B. F. Roettger, D. I. Pinon, and L. J. Miller. Role of receptor phosphorylation in desensitization and internalization of the secretin receptor. J. Biol. Chem. 271: 23566-23571, 1996.
    • (1996) J. Biol. Chem. , vol.271 , pp. 23566-23571
    • Holtmann, M.H.1    Roettger, B.F.2    Pinon, D.I.3    Miller, L.J.4
  • 16
    • 0029017353 scopus 로고
    • A conserved NPLFY sequence contributes to agonist binding and signal transduction but is not an internalization signal for the type 1 angiotensin II receptor
    • Hunyady, L., M. Bor, A. J. Baukal, T. Balla, and K. J. Catt. A conserved NPLFY sequence contributes to agonist binding and signal transduction but is not an internalization signal for the type 1 angiotensin II receptor. J. Biol. Chem. 270: 16602-16609, 1995.
    • (1995) J. Biol. Chem. , vol.270 , pp. 16602-16609
    • Hunyady, L.1    Bor, M.2    Baukal, A.J.3    Balla, T.4    Catt, K.J.5
  • 17
    • 0027999333 scopus 로고
    • Palmitoylation of luteinizing hormone/human choriogonadotropin receptors in transfected cells. Abolition of palmitoylation by mutation of Cys-621 and Cys-622 residues in the cytoplasmic tail increases ligand-induced internalization of the receptor
    • Kawate, N., and K. M. J. Menon. Palmitoylation of luteinizing hormone/human choriogonadotropin receptors in transfected cells. Abolition of palmitoylation by mutation of Cys-621 and Cys-622 residues in the cytoplasmic tail increases ligand-induced internalization of the receptor. J. Biol. Chem. 269: 30651-30658, 1994.
    • (1994) J. Biol. Chem. , vol.269 , pp. 30651-30658
    • Kawate, N.1    Menon, K.M.J.2
  • 18
    • 0027401994 scopus 로고
    • 2A-adrenergic receptor that eliminate detectable palmitoylation do not perturb receptor-G-protein coupling
    • 2A-adrenergic receptor that eliminate detectable palmitoylation do not perturb receptor-G-protein coupling. J. Biol. Chem. 268: 8003-8011, 1993.
    • (1993) J. Biol. Chem. , vol.268 , pp. 8003-8011
    • Kennedy, M.E.1    Limbird, L.E.2
  • 19
    • 0025834131 scopus 로고
    • Agonist-regulated phosphorylation of the pancreatic cholecystokinin receptor
    • Klueppelberg, U. G., L. K. Gates, F. S. Gorelick, and L. J. Miller. Agonist-regulated phosphorylation of the pancreatic cholecystokinin receptor. J. Biol. Chem. 266: 2403-2408, 1991.
    • (1991) J. Biol. Chem. , vol.266 , pp. 2403-2408
    • Klueppelberg, U.G.1    Gates, L.K.2    Gorelick, F.S.3    Miller, L.J.4
  • 20
    • 0027196424 scopus 로고
    • Control of cholecystokinin receptor dephosphorylation in pancreatic acinar cells
    • Lutz, M. P., D. I. Pinon, L. K. Gates, S. Shenolikar, and L. J. Miller. Control of cholecystokinin receptor dephosphorylation in pancreatic acinar cells. J. Biol. Chem. 268: 12136-12142, 1993.
    • (1993) J. Biol. Chem. , vol.268 , pp. 12136-12142
    • Lutz, M.P.1    Pinon, D.I.2    Gates, L.K.3    Shenolikar, S.4    Miller, L.J.5
  • 21
    • 0027265077 scopus 로고
    • A role for cholecystokinin-stimulated protein tyrosine phosphorylation in regulated secretion by the pancreatic acinar cell
    • Lutz, M. P., S. L. Sutor, R. T. Abraham, and L. J. Miller. A role for cholecystokinin-stimulated protein tyrosine phosphorylation in regulated secretion by the pancreatic acinar cell. J. Biol. Chem. 268: 11119-11124, 1993.
    • (1993) J. Biol. Chem. , vol.268 , pp. 11119-11124
    • Lutz, M.P.1    Sutor, S.L.2    Abraham, R.T.3    Miller, L.J.4
  • 22
    • 0028307839 scopus 로고
    • Fluorescence studies of the location and membrane accessibility of the palmitoylation sites of rhodopsin
    • Moench, S. J., J. Moreland, D. H. Stewart, and T. G. Dewey. Fluorescence studies of the location and membrane accessibility of the palmitoylation sites of rhodopsin. Biochemistry 33: 5791-5796, 1994.
    • (1994) Biochemistry , vol.33 , pp. 5791-5796
    • Moench, S.J.1    Moreland, J.2    Stewart, D.H.3    Dewey, T.G.4
  • 24
    • 0019061918 scopus 로고
    • LIGAND: A versatile computerized approach for characterization of ligand-binding systems
    • Munson, P. J., and D. Rodbard. LIGAND: a versatile computerized approach for characterization of ligand-binding systems. Anal. Biochem. 107: 220-239, 1980.
    • (1980) Anal. Biochem. , vol.107 , pp. 220-239
    • Munson, P.J.1    Rodbard, D.2
  • 25
    • 0003111499 scopus 로고
    • Cholecystokinin: Isolation, structure, and functions
    • edited by G. B. J. Glass. New York: Raven
    • Mutt, V. Cholecystokinin: isolation, structure, and functions. In: Gastrointestinal Hormones, edited by G. B. J. Glass. New York: Raven, 1980, p. 169-221.
    • (1980) Gastrointestinal Hormones , pp. 169-221
    • Mutt, V.1
  • 26
    • 0027258001 scopus 로고
    • Alternative splicing of C-terminal tail of prostaglandin e receptor subtype EP3 determines G-protein specificity
    • Namba, T., Y. Sugimoto, M. Negishi, A. Irie, F. Ushikubi, A. Kakizuka, S. Ito, A. Ichikawa, and S. Narumiya. Alternative splicing of C-terminal tail of prostaglandin E receptor subtype EP3 determines G-protein specificity. Nature 365: 166-170, 1993.
    • (1993) Nature , vol.365 , pp. 166-170
    • Namba, T.1    Sugimoto, Y.2    Negishi, M.3    Irie, A.4    Ushikubi, F.5    Kakizuka, A.6    Ito, S.7    Ichikawa, A.8    Narumiya, S.9
  • 28
    • 0028795221 scopus 로고
    • Phosphopeptide mapping of cholecystokinin receptors on agonist-stimulated native pancreatic acinar cells
    • Ozcelebi, F., and L. J. Miller. Phosphopeptide mapping of cholecystokinin receptors on agonist-stimulated native pancreatic acinar cells. J. Biol. Chem. 270: 3435-3441, 1995.
    • (1995) J. Biol. Chem. , vol.270 , pp. 3435-3441
    • Ozcelebi, F.1    Miller, L.J.2
  • 29
    • 0030067449 scopus 로고    scopus 로고
    • Phosphorylation of cholecystokinin receptors expressed on Chinese hamster ovary cells: Similarities and differences relative to native pancreatic acinar cells
    • Ozcelebi, F., R. V. Rao, E. Holicky, B. J. Madden, D. J. McCormick, and L. J. Miller. Phosphorylation of cholecystokinin receptors expressed on Chinese hamster ovary cells: similarities and differences relative to native pancreatic acinar cells. J. Biol. Chem. 271: 3750-3755, 1996.
    • (1996) J. Biol. Chem. , vol.271 , pp. 3750-3755
    • Ozcelebi, F.1    Rao, R.V.2    Holicky, E.3    Madden, B.J.4    McCormick, D.J.5    Miller, L.J.6
  • 30
    • 0030789693 scopus 로고    scopus 로고
    • Ligand-induced internalization of cholecystokinin receptors. Demonstration of the importance of the carboxyl terminus for ligand-induced internalization of the rat cholecystokinin type B receptor but not the type A receptor
    • Pohl, M., S. Silvente-Poirot, J. R. Pisegna, N. I. Tarasova, and S. A. Wank. Ligand-induced internalization of cholecystokinin receptors. Demonstration of the importance of the carboxyl terminus for ligand-induced internalization of the rat cholecystokinin type B receptor but not the type A receptor. J. Biol. Chem. 272: 18179-18184, 1997.
    • (1997) J. Biol. Chem. , vol.272 , pp. 18179-18184
    • Pohl, M.1    Silvente-Poirot, S.2    Pisegna, J.R.3    Tarasova, N.I.4    Wank, S.A.5
  • 32
    • 0024009303 scopus 로고
    • Use of N,O-bis-FMOC-D-Tyr-ONSu for introduction of an oxidative iodination site into cholecystokinin family peptides
    • Powers, S. P., D. I. Pinon, and L. J. Miller. Use of N,O-bis-FMOC-D-Tyr-ONSu for introduction of an oxidative iodination site into cholecystokinin family peptides. Int. J. Pept. Protein Res. 31: 429-434, 1988.
    • (1988) Int. J. Pept. Protein Res. , vol.31 , pp. 429-434
    • Powers, S.P.1    Pinon, D.I.2    Miller, L.J.3
  • 33
    • 0031016848 scopus 로고    scopus 로고
    • Roles of cholecystokinin receptor phosphorylation in agonist-stimulated desensitization of pancreatic acinar cells and receptor-bearing Chinese hamster ovary cholecystokinin receptor cells
    • Rao, R. V., B. F. Roettger, E. M. Hadac, and L. J. Miller. Roles of cholecystokinin receptor phosphorylation in agonist-stimulated desensitization of pancreatic acinar cells and receptor-bearing Chinese hamster ovary cholecystokinin receptor cells. Mol. Pharmacol. 51: 185-192, 1997.
    • (1997) Mol. Pharmacol. , vol.51 , pp. 185-192
    • Rao, R.V.1    Roettger, B.F.2    Hadac, E.M.3    Miller, L.J.4
  • 34
    • 0029122636 scopus 로고
    • Insulation of a G protein-coupled receptor on the plasmalemmal surface of the pancreatic acinar cell
    • Roettger, B. F., R. U. Rentsch, E. M. Hadac, E. H. Hellen, T. P. Burghardt, and L. J. Miller. Insulation of a G protein-coupled receptor on the plasmalemmal surface of the pancreatic acinar cell. J. Cell Biol. 130: 579-590, 1995.
    • (1995) J. Cell Biol. , vol.130 , pp. 579-590
    • Roettger, B.F.1    Rentsch, R.U.2    Hadac, E.M.3    Hellen, E.H.4    Burghardt, T.P.5    Miller, L.J.6
  • 38
    • 0025338137 scopus 로고
    • A domain of the insulin receptor required for endocytosis in rat fibroblasts
    • Thies, R. S., N. J. Webster, and D. A. McClain. A domain of the insulin receptor required for endocytosis in rat fibroblasts. J. Biol. Chem. 265: 10132-10137, 1990.
    • (1990) J. Biol. Chem. , vol.265 , pp. 10132-10137
    • Thies, R.S.1    Webster, N.J.2    McClain, D.A.3
  • 40
    • 0028284289 scopus 로고
    • Multisite interactions of receptors and G proteins: Enhanced potency of dimeric receptor peptides in modifying G protein function
    • Wade, S. M., H. M. Dalman, S.-Z. Yang, and R. R. Neubig. Multisite interactions of receptors and G proteins: enhanced potency of dimeric receptor peptides in modifying G protein function. Mol. Pharmacol. 45: 1191-1197, 1994.
    • (1994) Mol. Pharmacol. , vol.45 , pp. 1191-1197
    • Wade, S.M.1    Dalman, H.M.2    Yang, S.-Z.3    Neubig, R.R.4
  • 41
    • 0029010308 scopus 로고
    • The phosphotyrosine interaction domain of SHC recognizes tyrosine-phosphorylated NPXY motif
    • Zhou, S., B. Margolis, M. Chaudhuri, S. E. Shoelson, and L. C. Cantley. The phosphotyrosine interaction domain of SHC recognizes tyrosine-phosphorylated NPXY motif. J. Biol. Chem. 270: 14863-14866, 1995.
    • (1995) J. Biol. Chem. , vol.270 , pp. 14863-14866
    • Zhou, S.1    Margolis, B.2    Chaudhuri, M.3    Shoelson, S.E.4    Cantley, L.C.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.