메뉴 건너뛰기




Volumn 1783, Issue 9, 2008, Pages 1663-1672

Cell surface targeting of VPAC1 receptors: Evidence for implication of a quality control system and the proteasome

Author keywords

Cell surface expression; Glycosylation; GPCR; Proteasome; Trafficking; VIP receptor; VPAC1

Indexed keywords

G PROTEIN COUPLED RECEPTOR; PROTEASOME; VASOACTIVE INTESTINAL POLYPEPTIDE RECEPTOR 1; CHAPERONE; UBIQUITIN;

EID: 49149101395     PISSN: 01674889     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbamcr.2008.03.013     Document Type: Article
Times cited : (9)

References (33)
  • 2
    • 24344487961 scopus 로고    scopus 로고
    • The regulatory mechanisms of export trafficking of G protein-coupled receptors
    • Duvernay M.T., Filipeanu C.M., and Wu G. The regulatory mechanisms of export trafficking of G protein-coupled receptors. Cell. Signal. 17 (2005) 1457-1465
    • (2005) Cell. Signal. , vol.17 , pp. 1457-1465
    • Duvernay, M.T.1    Filipeanu, C.M.2    Wu, G.3
  • 3
  • 4
    • 0346655115 scopus 로고    scopus 로고
    • Regulated ubiquitination of proteins in GPCR-initiated signaling pathways
    • Wojcikiewicz R.J. Regulated ubiquitination of proteins in GPCR-initiated signaling pathways. Trends Pharmacol. Sci. 25 (2004) 35-41
    • (2004) Trends Pharmacol. Sci. , vol.25 , pp. 35-41
    • Wojcikiewicz, R.J.1
  • 5
    • 0034578389 scopus 로고    scopus 로고
    • Aggresomes, inclusion bodies and protein aggregation
    • Kopito R.R. Aggresomes, inclusion bodies and protein aggregation. Trends Cell Biol. 10 (2000) 524-530
    • (2000) Trends Cell Biol. , vol.10 , pp. 524-530
    • Kopito, R.R.1
  • 7
    • 0036499130 scopus 로고    scopus 로고
    • Arresting developments in heptahelical receptor signaling and regulation
    • Perry S.J., and Lefkowitz R.J. Arresting developments in heptahelical receptor signaling and regulation. Trends Cell Biol. 12 (2002) 130-138
    • (2002) Trends Cell Biol. , vol.12 , pp. 130-138
    • Perry, S.J.1    Lefkowitz, R.J.2
  • 8
    • 0038487327 scopus 로고    scopus 로고
    • The ins and outs of G protein-coupled receptor trafficking
    • Marchese A., Chen C., Kim Y.M., and Benovic J.L. The ins and outs of G protein-coupled receptor trafficking. Trends Biochem. Sci. 28 (2003) 369-376
    • (2003) Trends Biochem. Sci. , vol.28 , pp. 369-376
    • Marchese, A.1    Chen, C.2    Kim, Y.M.3    Benovic, J.L.4
  • 10
    • 0030051035 scopus 로고    scopus 로고
    • Mutagenesis of N-glycosylation sites in the human vasoactive intestinal peptide 1 receptor. Evidence that asparagine 58 or 69 is crucial for correct delivery of the receptor to plasma membrane
    • Couvineau A., Fabre C., Gaudin P., Maoret J.J., and Laburthe M. Mutagenesis of N-glycosylation sites in the human vasoactive intestinal peptide 1 receptor. Evidence that asparagine 58 or 69 is crucial for correct delivery of the receptor to plasma membrane. Biochemistry 35 (1996) 1745-1752
    • (1996) Biochemistry , vol.35 , pp. 1745-1752
    • Couvineau, A.1    Fabre, C.2    Gaudin, P.3    Maoret, J.J.4    Laburthe, M.5
  • 11
    • 0034751792 scopus 로고    scopus 로고
    • Vasoactive intestinal peptide (VIP) stimulates [Ca(2+)](i)and cyclic AMPin CHO cells expressing Galpha16
    • Langer I., Perret J., Vertongen P., Waelbroeck M., and Robberecht P. Vasoactive intestinal peptide (VIP) stimulates [Ca(2+)](i)and cyclic AMPin CHO cells expressing Galpha16. Cell Calcium 30 (2001) 229-234
    • (2001) Cell Calcium , vol.30 , pp. 229-234
    • Langer, I.1    Perret, J.2    Vertongen, P.3    Waelbroeck, M.4    Robberecht, P.5
  • 12
    • 0036252320 scopus 로고    scopus 로고
    • A small sequence in the third intracellular loop of the VPAC(1) receptor is responsible for its efficient coupling to the calcium effector
    • Langer I., Vertongen P., Perret J., Waelbroeck M., and Robberecht P. A small sequence in the third intracellular loop of the VPAC(1) receptor is responsible for its efficient coupling to the calcium effector. Mol. Endocrinol. 16 (2002) 1089-1096
    • (2002) Mol. Endocrinol. , vol.16 , pp. 1089-1096
    • Langer, I.1    Vertongen, P.2    Perret, J.3    Waelbroeck, M.4    Robberecht, P.5
  • 13
    • 11144230455 scopus 로고    scopus 로고
    • Immunocytochemical identification of VPAC1, VPAC2, and PAC1 receptors in normal and neoplastic human tissues with subtype-specific antibodies
    • Schulz S., Rocken C., Mawrin C., Weise W., Hollt V., and Schulz S. Immunocytochemical identification of VPAC1, VPAC2, and PAC1 receptors in normal and neoplastic human tissues with subtype-specific antibodies. Clin. Cancer Res. 10 (2004) 8235-8242
    • (2004) Clin. Cancer Res. , vol.10 , pp. 8235-8242
    • Schulz, S.1    Rocken, C.2    Mawrin, C.3    Weise, W.4    Hollt, V.5    Schulz, S.6
  • 14
    • 23044487654 scopus 로고    scopus 로고
    • Contribution of the carboxyl terminus of the VPAC1 receptor to agonist-induced receptor phosphorylation, internalization, and recycling
    • Langlet C., Langer I., Vertongen P., Gaspard N., Vanderwinden J.M., and Robberecht P. Contribution of the carboxyl terminus of the VPAC1 receptor to agonist-induced receptor phosphorylation, internalization, and recycling. J. Biol. Chem. 280 (2005) 28034-28043
    • (2005) J. Biol. Chem. , vol.280 , pp. 28034-28043
    • Langlet, C.1    Langer, I.2    Vertongen, P.3    Gaspard, N.4    Vanderwinden, J.M.5    Robberecht, P.6
  • 15
    • 0016374975 scopus 로고
    • A highly sensitive adenylate cyclase assay
    • Salomon Y., Londos C., and Rodbell M. A highly sensitive adenylate cyclase assay. Anal. Biochem. 58 (1974) 541-548
    • (1974) Anal. Biochem. , vol.58 , pp. 541-548
    • Salomon, Y.1    Londos, C.2    Rodbell, M.3
  • 18
    • 24944446266 scopus 로고    scopus 로고
    • Endoplasmic reticulum-associated degradation
    • Romisch K. Endoplasmic reticulum-associated degradation. Annu. Rev. Cell Dev. Biol. 21 (2005) 435-456
    • (2005) Annu. Rev. Cell Dev. Biol. , vol.21 , pp. 435-456
    • Romisch, K.1
  • 19
    • 0344393021 scopus 로고    scopus 로고
    • Quality control and protein folding in the secretory pathway
    • Trombetta E.S., and Parodi A.J. Quality control and protein folding in the secretory pathway. Annu. Rev. Cell Dev. Biol. 19 (2003) 649-676
    • (2003) Annu. Rev. Cell Dev. Biol. , vol.19 , pp. 649-676
    • Trombetta, E.S.1    Parodi, A.J.2
  • 20
    • 7244253015 scopus 로고    scopus 로고
    • Pharmacologic rescue of conformationally-defective proteins: implications for the treatment of human disease
    • Ulloa-Aguirre A., Janovick J.A., Brothers S.P., and Conn P.M. Pharmacologic rescue of conformationally-defective proteins: implications for the treatment of human disease. Traffic 5 (2004) 821-837
    • (2004) Traffic , vol.5 , pp. 821-837
    • Ulloa-Aguirre, A.1    Janovick, J.A.2    Brothers, S.P.3    Conn, P.M.4
  • 21
    • 33750314184 scopus 로고    scopus 로고
    • Asn229 in the third helix of VPAC1 receptor is essential for receptor activation but not for receptor phosphorylation and internalization: comparison with Asn216 in VPAC2 receptor
    • Nachtergael I., Gaspard N., Langlet C., Robberecht P., and Langer I. Asn229 in the third helix of VPAC1 receptor is essential for receptor activation but not for receptor phosphorylation and internalization: comparison with Asn216 in VPAC2 receptor. Cell. Signal. 18 (2006) 2121-2130
    • (2006) Cell. Signal. , vol.18 , pp. 2121-2130
    • Nachtergael, I.1    Gaspard, N.2    Langlet, C.3    Robberecht, P.4    Langer, I.5
  • 22
    • 30044441189 scopus 로고    scopus 로고
    • Constitutive formation of oligomeric complexes between family B G protein-coupled vasoactive intestinal polypeptide and secretin receptors
    • Harikumar K.G., Morfis M.M., Lisenbee C.S., Sexton P.M., and Miller L.J. Constitutive formation of oligomeric complexes between family B G protein-coupled vasoactive intestinal polypeptide and secretin receptors. Mol. Pharmacol. 69 (2006) 363-373
    • (2006) Mol. Pharmacol. , vol.69 , pp. 363-373
    • Harikumar, K.G.1    Morfis, M.M.2    Lisenbee, C.S.3    Sexton, P.M.4    Miller, L.J.5
  • 24
    • 4043125390 scopus 로고    scopus 로고
    • Homodimerization of the beta2-adrenergic receptor as a prerequisite for cell surface targeting
    • Salahpour A., Angers S., Mercier J.F., Lagace M., Marullo S., and Bouvier M. Homodimerization of the beta2-adrenergic receptor as a prerequisite for cell surface targeting. J. Biol. Chem. 279 (2004) 33390-33397
    • (2004) J. Biol. Chem. , vol.279 , pp. 33390-33397
    • Salahpour, A.1    Angers, S.2    Mercier, J.F.3    Lagace, M.4    Marullo, S.5    Bouvier, M.6
  • 25
    • 22544435246 scopus 로고    scopus 로고
    • Inefficient maturation of the rat luteinizing hormone receptor. A putative way to regulate receptor numbers at the cell surface
    • Pietila E.M., Tuusa J.T., Apaja P.M., Aatsinki J.T., Hakalahti A.E., Rajaniemi H.J., and Petaja-Repo U.E. Inefficient maturation of the rat luteinizing hormone receptor. A putative way to regulate receptor numbers at the cell surface. J. Biol. Chem. 280 (2005) 26622-26629
    • (2005) J. Biol. Chem. , vol.280 , pp. 26622-26629
    • Pietila, E.M.1    Tuusa, J.T.2    Apaja, P.M.3    Aatsinki, J.T.4    Hakalahti, A.E.5    Rajaniemi, H.J.6    Petaja-Repo, U.E.7
  • 26
    • 0034607918 scopus 로고    scopus 로고
    • Export from the endoplasmic reticulum represents the limiting step in the maturation and cell surface expression of the human delta opioid receptor
    • Petaja-Repo U.E., Hogue M., Laperriere A., Walker P., and Bouvier M. Export from the endoplasmic reticulum represents the limiting step in the maturation and cell surface expression of the human delta opioid receptor. J. Biol. Chem. 275 (2000) 13727-13736
    • (2000) J. Biol. Chem. , vol.275 , pp. 13727-13736
    • Petaja-Repo, U.E.1    Hogue, M.2    Laperriere, A.3    Walker, P.4    Bouvier, M.5
  • 27
    • 0034646876 scopus 로고    scopus 로고
    • Chaperone selection during glycoprotein translocation into the endoplasmic reticulum
    • Molinari M., and Helenius A. Chaperone selection during glycoprotein translocation into the endoplasmic reticulum. Science 288 (2000) 331-333
    • (2000) Science , vol.288 , pp. 331-333
    • Molinari, M.1    Helenius, A.2
  • 28
    • 33748751347 scopus 로고    scopus 로고
    • Serotonin 5-HT2C receptor homodimer biogenesis in the endoplasmic reticulum: real-time visualization with confocal fluorescence resonance energy transfer
    • Herrick-Davis K., Weaver B.A., Grinde E., and Mazurkiewicz J.E. Serotonin 5-HT2C receptor homodimer biogenesis in the endoplasmic reticulum: real-time visualization with confocal fluorescence resonance energy transfer. J. Biol. Chem. 281 (2006) 27109-27116
    • (2006) J. Biol. Chem. , vol.281 , pp. 27109-27116
    • Herrick-Davis, K.1    Weaver, B.A.2    Grinde, E.3    Mazurkiewicz, J.E.4
  • 29
    • 2442597256 scopus 로고    scopus 로고
    • Cell surface expression of alpha1D-adrenergic receptors is controlled by heterodimerization with alpha1B-adrenergic receptors
    • Hague C., Uberti M.A., Chen Z., Hall R.A., and Minneman K.P. Cell surface expression of alpha1D-adrenergic receptors is controlled by heterodimerization with alpha1B-adrenergic receptors. J. Biol. Chem. 279 (2004) 15541-15549
    • (2004) J. Biol. Chem. , vol.279 , pp. 15541-15549
    • Hague, C.1    Uberti, M.A.2    Chen, Z.3    Hall, R.A.4    Minneman, K.P.5
  • 30
    • 15744405558 scopus 로고    scopus 로고
    • Heterodimerization with beta2-adrenergic receptors promotes surface expression and functional activity of alpha1D-adrenergic receptors
    • Uberti M.A., Hague C., Oller H., Minneman K.P., and Hall R.A. Heterodimerization with beta2-adrenergic receptors promotes surface expression and functional activity of alpha1D-adrenergic receptors. J. Pharmacol. Exp. Ther. 313 (2005) 16-23
    • (2005) J. Pharmacol. Exp. Ther. , vol.313 , pp. 16-23
    • Uberti, M.A.1    Hague, C.2    Oller, H.3    Minneman, K.P.4    Hall, R.A.5
  • 31
    • 27844457541 scopus 로고    scopus 로고
    • Cell-surface targeting of alpha2-adrenergic receptors - inhibition by a transport deficient mutant through dimerization
    • Zhou F., Filipeanu C.M., Duvernay M.T., and Wu G. Cell-surface targeting of alpha2-adrenergic receptors - inhibition by a transport deficient mutant through dimerization. Cell. Signal. 18 (2006) 318-327
    • (2006) Cell. Signal. , vol.18 , pp. 318-327
    • Zhou, F.1    Filipeanu, C.M.2    Duvernay, M.T.3    Wu, G.4
  • 32
    • 0035834428 scopus 로고    scopus 로고
    • Regulation of receptor fate by ubiquitination of activated beta 2-adrenergic receptor and beta-arrestin
    • Shenoy S.K., McDonald P.H., Kohout T.A., and Lefkowitz R.J. Regulation of receptor fate by ubiquitination of activated beta 2-adrenergic receptor and beta-arrestin. Science 294 (2001) 1307-1313
    • (2001) Science , vol.294 , pp. 1307-1313
    • Shenoy, S.K.1    McDonald, P.H.2    Kohout, T.A.3    Lefkowitz, R.J.4
  • 33
    • 0037067693 scopus 로고    scopus 로고
    • Vasoactive intestinal polypeptide type-1 receptor regulation. desensitization, phosphorylation, and sequestration
    • Shetzline M.A., Walker J.K., Valenzano K.J., and Premont R.T. Vasoactive intestinal polypeptide type-1 receptor regulation. desensitization, phosphorylation, and sequestration. J. Biol. Chem. 277 (2002) 25519-25526
    • (2002) J. Biol. Chem. , vol.277 , pp. 25519-25526
    • Shetzline, M.A.1    Walker, J.K.2    Valenzano, K.J.3    Premont, R.T.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.