메뉴 건너뛰기




Volumn 62, Issue , 2011, Pages 279-314

Role of PDZ Proteins in Regulating Trafficking, Signaling, and Function of GPCRs. Means, Motif, and Opportunity

Author keywords

Cell signaling; G protein coupled receptors; PDZ proteins; Protein protein interactions; Receptor endocytosis; Receptor trafficking

Indexed keywords

4 AMINOBUTYRIC ACID B RECEPTOR; ADENOSINE RECEPTOR; ADRENALIN; ALPHA ADRENERGIC RECEPTOR; BETA 1 ADRENERGIC RECEPTOR; BETA 2 ADRENERGIC RECEPTOR; BETA 3 ADRENERGIC RECEPTOR; BETA ARRESTIN; CHEMOKINE RECEPTOR CXCR2; CORTICOTROPIN RELEASING FACTOR RECEPTOR; CYCLIC AMP DEPENDENT PROTEIN KINASE; FRIZZLED PROTEIN; G PROTEIN COUPLED RECEPTOR; GUANOSINE TRIPHOSPHATASE; ISOPRENALINE; KAPPA OPIATE RECEPTOR; LUTEINIZING HORMONE RECEPTOR; LYSOPHOSPHATIDIC ACID RECEPTOR; NORADRENALIN; PDZ PROTEIN; PHOSPHOLIPASE C; PURINERGIC P2Y1 RECEPTOR; SCAFFOLD PROTEIN; SEROTONIN 1 RECEPTOR; SEROTONIN 2 RECEPTOR; SEROTONIN 3 RECEPTOR; SEROTONIN 4 RECEPTOR; SEROTONIN 5 RECEPTOR; SEROTONIN 6 RECEPTOR; SEROTONIN 7 RECEPTOR;

EID: 80052689122     PISSN: 10543589     EISSN: 15578925     Source Type: Book Series    
DOI: 10.1016/B978-0-12-385952-5.00003-8     Document Type: Chapter
Times cited : (136)

References (141)
  • 1
    • 0026598246 scopus 로고
    • Expression cloning of a common receptor for parathyroid hormone and parathyroid hormone-related peptide from rat osteoblast-like cells: A single receptor stimulates intracellular accumulation of both cAMP and inositol trisphosphates and increases intracellular free calcium
    • Abou-Samra A.B., Jüppner H., Force T., Freeman M.W., Kong X.F., Schipani E., et al. Expression cloning of a common receptor for parathyroid hormone and parathyroid hormone-related peptide from rat osteoblast-like cells: A single receptor stimulates intracellular accumulation of both cAMP and inositol trisphosphates and increases intracellular free calcium. Proceedings of the National Academy of Science of the United States of America 1992, 89(7):2732-2736.
    • (1992) Proceedings of the National Academy of Science of the United States of America , vol.89 , Issue.7 , pp. 2732-2736
    • Abou-Samra, A.B.1    Jüppner, H.2    Force, T.3    Freeman, M.W.4    Kong, X.F.5    Schipani, E.6
  • 3
    • 0023390229 scopus 로고
    • Parathyroid hormone stimulation of mitosis in rat thymic lymphocytes is independent of cyclic AMP
    • Atkinson M.J., Hesch R.D., Cade C., Wadwah M., Perris A.D. Parathyroid hormone stimulation of mitosis in rat thymic lymphocytes is independent of cyclic AMP. Journal of Bone and Mineral Research 1987, 2(4):303-309.
    • (1987) Journal of Bone and Mineral Research , vol.2 , Issue.4 , pp. 303-309
    • Atkinson, M.J.1    Hesch, R.D.2    Cade, C.3    Wadwah, M.4    Perris, A.D.5
  • 4
    • 0034604706 scopus 로고    scopus 로고
    • Deletion of the serotonin 5-HT2C receptor PDZ recognition motif prevents receptor phosphorylation and delays resensitization of receptor responses
    • Backstrom J.R., Price R.D., Reasoner D.T., Sanders-Bush E. Deletion of the serotonin 5-HT2C receptor PDZ recognition motif prevents receptor phosphorylation and delays resensitization of receptor responses. The Journal of Biological Chemistry 2000, 275(31):23620-23626.
    • (2000) The Journal of Biological Chemistry , vol.275 , Issue.31 , pp. 23620-23626
    • Backstrom, J.R.1    Price, R.D.2    Reasoner, D.T.3    Sanders-Bush, E.4
  • 5
    • 33947539044 scopus 로고    scopus 로고
    • GABAB receptor association with the PDZ scaffold Mupp 1 alters receptor stability and function
    • Balasubramanian S., Fam S.R., Hall R.A. GABAB receptor association with the PDZ scaffold Mupp 1 alters receptor stability and function. The Journal of Biological Chemistry 2007, 282(6):4162-4171.
    • (2007) The Journal of Biological Chemistry , vol.282 , Issue.6 , pp. 4162-4171
    • Balasubramanian, S.1    Fam, S.R.2    Hall, R.A.3
  • 6
    • 57649221137 scopus 로고    scopus 로고
    • The carboxyl-terminal PDZ ligand motif of chemokine receptor CXCR2 modulates post-endocytic sorting and cellular chemotaxis
    • Baugher P.J., Richmond A. The carboxyl-terminal PDZ ligand motif of chemokine receptor CXCR2 modulates post-endocytic sorting and cellular chemotaxis. The Journal of Biological Chemistry 2008, 283(45):30868-30878.
    • (2008) The Journal of Biological Chemistry , vol.283 , Issue.45 , pp. 30868-30878
    • Baugher, P.J.1    Richmond, A.2
  • 7
    • 0033679292 scopus 로고    scopus 로고
    • Structure of the Homer EVH1 domain-peptide complex reveals a new twist in polyproline recognition
    • Beneken J., Tu J.C., Xiao B., Nuriya M., Yuan J.P., Worley P.F., et al. Structure of the Homer EVH1 domain-peptide complex reveals a new twist in polyproline recognition. Neuron 2000, 26(1):143-154.
    • (2000) Neuron , vol.26 , Issue.1 , pp. 143-154
    • Beneken, J.1    Tu, J.C.2    Xiao, B.3    Nuriya, M.4    Yuan, J.P.5    Worley, P.F.6
  • 8
    • 33748689299 scopus 로고    scopus 로고
    • MacMARCKS interacts with the metabotropic glutamate receptor type 7 and modulates G protein-mediated constitutive inhibition of calcium channels
    • Bertaso F., Lill Y., Airas J.M., Espeut J., Blahos J., Bockaert J., et al. MacMARCKS interacts with the metabotropic glutamate receptor type 7 and modulates G protein-mediated constitutive inhibition of calcium channels. Journal of Neurochemistry 2006, 99(1):288-298.
    • (2006) Journal of Neurochemistry , vol.99 , Issue.1 , pp. 288-298
    • Bertaso, F.1    Lill, Y.2    Airas, J.M.3    Espeut, J.4    Blahos, J.5    Bockaert, J.6
  • 10
    • 17844390142 scopus 로고    scopus 로고
    • The post-endocytotic fate of the gonadotropin receptors is an important determinant of the desensitization of gonadotropin responses
    • Bhaskaran R.S., Ascoli M. The post-endocytotic fate of the gonadotropin receptors is an important determinant of the desensitization of gonadotropin responses. Journal of Molecular Endocrinology 2005, 34(2):447-457.
    • (2005) Journal of Molecular Endocrinology , vol.34 , Issue.2 , pp. 447-457
    • Bhaskaran, R.S.1    Ascoli, M.2
  • 13
    • 77950505396 scopus 로고    scopus 로고
    • Vangl2 directs the posterior tilting and asymmetric localization of motile primary cilia
    • Borovina A., Superina S., Voskas D., Ciruna B. Vangl2 directs the posterior tilting and asymmetric localization of motile primary cilia. Nature Cell Biology 2010, 12(4):407-412.
    • (2010) Nature Cell Biology , vol.12 , Issue.4 , pp. 407-412
    • Borovina, A.1    Superina, S.2    Voskas, D.3    Ciruna, B.4
  • 14
    • 0030970135 scopus 로고    scopus 로고
    • Homer: A protein that selectively binds metabotropic glutamate receptors
    • Brakeman P.R., Lanahan A.A., O'Brien R., Roche K., Barnes C.A., Huganir R.L., et al. Homer: A protein that selectively binds metabotropic glutamate receptors. Nature 1997, 386(6622):284-288.
    • (1997) Nature , vol.386 , Issue.6622 , pp. 284-288
    • Brakeman, P.R.1    Lanahan, A.A.2    O'Brien, R.3    Roche, K.4    Barnes, C.A.5    Huganir, R.L.6
  • 15
    • 13344277364 scopus 로고    scopus 로고
    • Interaction of nitric oxide synthase with the postsynaptic density protein PSD-95 and α1-syntrophin mediated by PDZ domains
    • Brenman J.E., Chao D.S., Gee S.H., McGee A.W., Craven S.E., Santillano D.R., et al. Interaction of nitric oxide synthase with the postsynaptic density protein PSD-95 and α1-syntrophin mediated by PDZ domains. Cell 1996, 84(5):757-767.
    • (1996) Cell , vol.84 , Issue.5 , pp. 757-767
    • Brenman, J.E.1    Chao, D.S.2    Gee, S.H.3    McGee, A.W.4    Craven, S.E.5    Santillano, D.R.6
  • 16
    • 0033575916 scopus 로고    scopus 로고
    • A kinase-regulated PDZ-domain interaction controls endocytic sorting of the ß2-adrenergic receptor
    • Cao T.T., Deacon H.W., Reczek D., Bretscher A., von Zastrow M. A kinase-regulated PDZ-domain interaction controls endocytic sorting of the ß2-adrenergic receptor. Nature 1999, 401(6750):286-290.
    • (1999) Nature , vol.401 , Issue.6750 , pp. 286-290
    • Cao, T.T.1    Deacon, H.W.2    Reczek, D.3    Bretscher, A.4    von Zastrow, M.5
  • 17
    • 0037126331 scopus 로고    scopus 로고
    • The DIX domain targets dishevelled to actin stress fibres and vesicular membranes
    • Capelluto D.G., Kutateladze T.G., Habas R., Finkielstein C.V., He X., Overduin M. The DIX domain targets dishevelled to actin stress fibres and vesicular membranes. Nature 2002, 419(6908):726-729.
    • (2002) Nature , vol.419 , Issue.6908 , pp. 726-729
    • Capelluto, D.G.1    Kutateladze, T.G.2    Habas, R.3    Finkielstein, C.V.4    He, X.5    Overduin, M.6
  • 18
    • 0029844904 scopus 로고    scopus 로고
    • A human exchange factor for ARF contains Sec7- and pleckstrin-homology domains
    • Chardin P., Paris S., Antonny B., Robineau S., Beraud-Dufour S., Jackson C.L., et al. A human exchange factor for ARF contains Sec7- and pleckstrin-homology domains. Nature 1996, 384(6608):481-484.
    • (1996) Nature , vol.384 , Issue.6608 , pp. 481-484
    • Chardin, P.1    Paris, S.2    Antonny, B.3    Robineau, S.4    Beraud-Dufour, S.5    Jackson, C.L.6
  • 19
    • 0036479131 scopus 로고    scopus 로고
    • A Golgi-associated PDZ domain protein modulates cystic fibrosis transmembrane regulator plasma membrane expression
    • Cheng J., Moyer B.D., Milewski M., Loffing J., Ikeda M., Mickle J.E., et al. A Golgi-associated PDZ domain protein modulates cystic fibrosis transmembrane regulator plasma membrane expression. The Journal of Biological Chemistry 2002, 277(5):3520-3529.
    • (2002) The Journal of Biological Chemistry , vol.277 , Issue.5 , pp. 3520-3529
    • Cheng, J.1    Moyer, B.D.2    Milewski, M.3    Loffing, J.4    Ikeda, M.5    Mickle, J.E.6
  • 20
    • 0347717877 scopus 로고    scopus 로고
    • Modulation of mature cystic fibrosis transmembrane regulator protein by the PDZ domain protein CAL
    • Cheng J., Wang H., Guggino W.B. Modulation of mature cystic fibrosis transmembrane regulator protein by the PDZ domain protein CAL. The Journal of Biological Chemistry 2004, 279(3):1892-1898.
    • (2004) The Journal of Biological Chemistry , vol.279 , Issue.3 , pp. 1892-1898
    • Cheng, J.1    Wang, H.2    Guggino, W.B.3
  • 21
    • 0036225314 scopus 로고    scopus 로고
    • Dapper, a Dishevelled-associated antagonist of ß-catenin and JNK signaling, is required for notochord formation
    • Cheyette B.N., Waxman J.S., Miller J.R., Takemaru K., Sheldahl L.C., Khlebtsova N., et al. Dapper, a Dishevelled-associated antagonist of ß-catenin and JNK signaling, is required for notochord formation. Developmental Cell 2002, 2(4):449-461.
    • (2002) Developmental Cell , vol.2 , Issue.4 , pp. 449-461
    • Cheyette, B.N.1    Waxman, J.S.2    Miller, J.R.3    Takemaru, K.4    Sheldahl, L.C.5    Khlebtsova, N.6
  • 22
    • 0034307444 scopus 로고    scopus 로고
    • Phosphorylation of the AMPA receptor subunit GluR2 differentially regulates its interaction with PDZ domain-containing proteins
    • Chung H.J., Xia J., Scannevin R.H., Zhang X., Huganir R.L. Phosphorylation of the AMPA receptor subunit GluR2 differentially regulates its interaction with PDZ domain-containing proteins. The Journal of Neuroscience 2000, 20(19):7258-7267.
    • (2000) The Journal of Neuroscience , vol.20 , Issue.19 , pp. 7258-7267
    • Chung, H.J.1    Xia, J.2    Scannevin, R.H.3    Zhang, X.4    Huganir, R.L.5
  • 23
    • 0035977051 scopus 로고    scopus 로고
    • Binding of the ß2 adrenergic receptor to N-ethylmaleimide-sensitive factor regulates receptor recycling
    • Cong M., Perry S.J., Hu L.A., Hanson P.I., Claing A., Lefkowitz R.J. Binding of the ß2 adrenergic receptor to N-ethylmaleimide-sensitive factor regulates receptor recycling. The Journal of Biological Chemistry 2001, 276(48):45145-45152.
    • (2001) The Journal of Biological Chemistry , vol.276 , Issue.48 , pp. 45145-45152
    • Cong, M.1    Perry, S.J.2    Hu, L.A.3    Hanson, P.I.4    Claing, A.5    Lefkowitz, R.J.6
  • 24
    • 8444223093 scopus 로고    scopus 로고
    • Wnt signals across the plasma membrane to activate the ß-catenin pathway by forming oligomers containing its receptors, Frizzled and LRP
    • Cong F., Schweizer L., Varmus H. Wnt signals across the plasma membrane to activate the ß-catenin pathway by forming oligomers containing its receptors, Frizzled and LRP. Development 2004, 131(20):5103-5115.
    • (2004) Development , vol.131 , Issue.20 , pp. 5103-5115
    • Cong, F.1    Schweizer, L.2    Varmus, H.3
  • 25
    • 33748146106 scopus 로고    scopus 로고
    • The role of protein interaction motifs in regulating the polarity and clustering of the metabotropic glutamate receptor mGluR1a
    • Das S.S., Banker G.A. The role of protein interaction motifs in regulating the polarity and clustering of the metabotropic glutamate receptor mGluR1a. The Journal of Neuroscience 2006, 26(31):8115-8125.
    • (2006) The Journal of Neuroscience , vol.26 , Issue.31 , pp. 8115-8125
    • Das, S.S.1    Banker, G.A.2
  • 28
    • 15444362814 scopus 로고    scopus 로고
    • Receptors specific for the carboxyl-terminal region of parathyroid hormone on bone-derived cells: Determinants of ligand binding and bioactivity
    • Divieti P., Geller A.I., Suliman G., Juppner H., Bringhurst F.R. Receptors specific for the carboxyl-terminal region of parathyroid hormone on bone-derived cells: Determinants of ligand binding and bioactivity. Endocrinology 2005, 146(4):1863-1870.
    • (2005) Endocrinology , vol.146 , Issue.4 , pp. 1863-1870
    • Divieti, P.1    Geller, A.I.2    Suliman, G.3    Juppner, H.4    Bringhurst, F.R.5
  • 29
    • 0030604722 scopus 로고    scopus 로고
    • Crystal structures of a complexed and peptide-free membrane protein-binding domain: Molecular basis of peptide recognition by PDZ
    • Doyle D.A., Lee A., Lewis J., Kim E., Sheng M., MacKinnon R. Crystal structures of a complexed and peptide-free membrane protein-binding domain: Molecular basis of peptide recognition by PDZ. Cell 1996, 85(7):1067-1076.
    • (1996) Cell , vol.85 , Issue.7 , pp. 1067-1076
    • Doyle, D.A.1    Lee, A.2    Lewis, J.3    Kim, E.4    Sheng, M.5    MacKinnon, R.6
  • 30
    • 33745771673 scopus 로고    scopus 로고
    • Biologic actions and therapeutic potential of the proglucagon-derived peptides
    • Drucker D.J. Biologic actions and therapeutic potential of the proglucagon-derived peptides. Nature Clinical Practice. Endocrinology & Metabolism 2005, 1(1):22-31.
    • (2005) Nature Clinical Practice. Endocrinology & Metabolism , vol.1 , Issue.1 , pp. 22-31
    • Drucker, D.J.1
  • 31
    • 0037101776 scopus 로고    scopus 로고
    • G-protein-coupled receptors for neurotransmitter amino acids: C-terminal tails, crowded signalosomes
    • El Far O., Betz H. G-protein-coupled receptors for neurotransmitter amino acids: C-terminal tails, crowded signalosomes. The Biochemical Journal 2002, 365(Pt 2):329-336.
    • (2002) The Biochemical Journal , vol.365 , Issue.PART 2 , pp. 329-336
    • El Far, O.1    Betz, H.2
  • 32
    • 20444477139 scopus 로고    scopus 로고
    • The glucagon-like peptide-2 Receptor C terminus modulates ß-Arrestin-2 association but is dispensable for ligand-induced desensitization, endocytosis, and G-protein-dependent effector activation
    • Estall J.L., Koehler J.A., Yusta B., Drucker D.J. The glucagon-like peptide-2 Receptor C terminus modulates ß-Arrestin-2 association but is dispensable for ligand-induced desensitization, endocytosis, and G-protein-dependent effector activation. The Journal of Biological Chemistry 2005, 280(23):22124-22134.
    • (2005) The Journal of Biological Chemistry , vol.280 , Issue.23 , pp. 22124-22134
    • Estall, J.L.1    Koehler, J.A.2    Yusta, B.3    Drucker, D.J.4
  • 34
    • 57249086450 scopus 로고    scopus 로고
    • Developmental roles for Homer: More than just a pretty scaffold
    • Foa L., Gasperini R. Developmental roles for Homer: More than just a pretty scaffold. Journal of Neurochemistry 2009, 108(1):1-10.
    • (2009) Journal of Neurochemistry , vol.108 , Issue.1 , pp. 1-10
    • Foa, L.1    Gasperini, R.2
  • 35
    • 0030044881 scopus 로고    scopus 로고
    • Parathyroid hormone stimulation of calcium transport is mediated by dual signaling mechanisms involving PKA and PKC
    • Friedman P.A., Coutermarsh B.A., Kennedy S.M., Gesek F.A. Parathyroid hormone stimulation of calcium transport is mediated by dual signaling mechanisms involving PKA and PKC. Endocrinology 1996, 137(1):13-20.
    • (1996) Endocrinology , vol.137 , Issue.1 , pp. 13-20
    • Friedman, P.A.1    Coutermarsh, B.A.2    Kennedy, S.M.3    Gesek, F.A.4
  • 37
    • 33947547544 scopus 로고    scopus 로고
    • Assembly of an SAP97-AKAP79-cAMP-dependent protein kinase scaffold at the type 1 PSD-95/DLG/ZO1 motif of the human ß1-adrenergic receptor generates a receptosome involved in receptor recycling and networking
    • Gardner L.A., Naren A.P., Bahouth S.W. Assembly of an SAP97-AKAP79-cAMP-dependent protein kinase scaffold at the type 1 PSD-95/DLG/ZO1 motif of the human ß1-adrenergic receptor generates a receptosome involved in receptor recycling and networking. The Journal of Biological Chemistry 2007, 282(7):5085-5099.
    • (2007) The Journal of Biological Chemistry , vol.282 , Issue.7 , pp. 5085-5099
    • Gardner, L.A.1    Naren, A.P.2    Bahouth, S.W.3
  • 38
    • 33750501125 scopus 로고    scopus 로고
    • Opposite effects of PSD-95 and MPP3 PDZ proteins on serotonin 5-hydroxytryptamine2C receptor desensitization and membrane stability
    • Gavarini S., Becamel C., Altier C., Lory P., Poncet J., Wijnholds J., et al. Opposite effects of PSD-95 and MPP3 PDZ proteins on serotonin 5-hydroxytryptamine2C receptor desensitization and membrane stability. Molecular Biology of the Cell 2006, 17(11):4619-4631.
    • (2006) Molecular Biology of the Cell , vol.17 , Issue.11 , pp. 4619-4631
    • Gavarini, S.1    Becamel, C.2    Altier, C.3    Lory, P.4    Poncet, J.5    Wijnholds, J.6
  • 39
    • 67650266967 scopus 로고    scopus 로고
    • Discovery and characterization of a small molecule inhibitor of the PDZ domain of dishevelled
    • Grandy D., Shan J., Zhang X., Rao S., Akunuru S., Li H., et al. Discovery and characterization of a small molecule inhibitor of the PDZ domain of dishevelled. The Journal of Biological Chemistry 2009, 284(24):16256-16263.
    • (2009) The Journal of Biological Chemistry , vol.284 , Issue.24 , pp. 16256-16263
    • Grandy, D.1    Shan, J.2    Zhang, X.3    Rao, S.4    Akunuru, S.5    Li, H.6
  • 41
    • 0032555156 scopus 로고    scopus 로고
    • A C-terminal motif found in the ß2-adrenergic receptor, P2Y1 receptor and cystic fibrosis transmembrane conductance regulator determines binding to the Na+/H+ exchanger regulatory factor family of PDZ proteins
    • Hall R.A., Ostedgaard L.S., Premont R.T., Blitzer J.T., Rahman N., Welsh M.J., et al. A C-terminal motif found in the ß2-adrenergic receptor, P2Y1 receptor and cystic fibrosis transmembrane conductance regulator determines binding to the Na+/H+ exchanger regulatory factor family of PDZ proteins. Proceedings of the National Academy of Science of the United States of America 1998, 95(15):8496-8501.
    • (1998) Proceedings of the National Academy of Science of the United States of America , vol.95 , Issue.15 , pp. 8496-8501
    • Hall, R.A.1    Ostedgaard, L.S.2    Premont, R.T.3    Blitzer, J.T.4    Rahman, N.5    Welsh, M.J.6
  • 42
    • 0032498963 scopus 로고    scopus 로고
    • The ß2-adrenergic receptor interacts with the Na+/H+-exchanger regulatory factor to control Na+/H+ exchange
    • Hall R.A., Premont R.T., Chow C.W., Blitzer J.T., Pitcher J.A., Claing A., et al. The ß2-adrenergic receptor interacts with the Na+/H+-exchanger regulatory factor to control Na+/H+ exchange. Nature (London) 1998, 392(6676):626-630.
    • (1998) Nature (London) , vol.392 , Issue.6676 , pp. 626-630
    • Hall, R.A.1    Premont, R.T.2    Chow, C.W.3    Blitzer, J.T.4    Pitcher, J.A.5    Claing, A.6
  • 43
    • 0033588029 scopus 로고    scopus 로고
    • G protein-coupled receptor kinase 6A phosphorylates the Na+/H+ exchanger regulatory factor via a PDZ domain-mediated interaction
    • Hall R.A., Spurney R.F., Premont R.T., Rahman N., Blitzer J.T., Pitcher J.A., et al. G protein-coupled receptor kinase 6A phosphorylates the Na+/H+ exchanger regulatory factor via a PDZ domain-mediated interaction. The Journal of Biological Chemistry 1999, 274(34):24328-24334.
    • (1999) The Journal of Biological Chemistry , vol.274 , Issue.34 , pp. 24328-24334
    • Hall, R.A.1    Spurney, R.F.2    Premont, R.T.3    Rahman, N.4    Blitzer, J.T.5    Pitcher, J.A.6
  • 44
    • 22744455819 scopus 로고    scopus 로고
    • Essential role of Hrs in a recycling mechanism mediating functional resensitization of cell signaling
    • Hanyaloglu A.C., McCullagh E., von Zastrow M. Essential role of Hrs in a recycling mechanism mediating functional resensitization of cell signaling. The EMBO Journal 2005, 24(13):2265-2283.
    • (2005) The EMBO Journal , vol.24 , Issue.13 , pp. 2265-2283
    • Hanyaloglu, A.C.1    McCullagh, E.2    von Zastrow, M.3
  • 45
    • 33646346138 scopus 로고    scopus 로고
    • Proteomic analysis of ß1-adrenergic receptor interactions with PDZ scaffold proteins
    • He J., Bellini M., Inuzuka H., Xu J., Xiong Y., Yang X., et al. Proteomic analysis of ß1-adrenergic receptor interactions with PDZ scaffold proteins. The Journal of Biological Chemistry 2006, 281(5):2820-2827.
    • (2006) The Journal of Biological Chemistry , vol.281 , Issue.5 , pp. 2820-2827
    • He, J.1    Bellini, M.2    Inuzuka, H.3    Xu, J.4    Xiong, Y.5    Yang, X.6
  • 46
    • 0037134787 scopus 로고    scopus 로고
    • Direct interaction of Frizzled-1, -2, -4, and -7 with PDZ domains of PSD-95
    • Hering H., Sheng M. Direct interaction of Frizzled-1, -2, -4, and -7 with PDZ domains of PSD-95. FEBS Letters 2002, 521(1-3):185-189.
    • (2002) FEBS Letters , vol.521 , Issue.1-3 , pp. 185-189
    • Hering, H.1    Sheng, M.2
  • 47
    • 0033617473 scopus 로고    scopus 로고
    • Unexpected modes of PDZ domain scaffolding revealed by structure of nNOS-syntrophin complex
    • Hillier B.J., Christopherson K.S., Prehoda K.E., Bredt D.S., Lim W.A. Unexpected modes of PDZ domain scaffolding revealed by structure of nNOS-syntrophin complex. Science 1999, 284(5415):812-815.
    • (1999) Science , vol.284 , Issue.5415 , pp. 812-815
    • Hillier, B.J.1    Christopherson, K.S.2    Prehoda, K.E.3    Bredt, D.S.4    Lim, W.A.5
  • 49
    • 0842292006 scopus 로고    scopus 로고
    • GIPC binds to the human lutropin receptor (hLHR) through an unusual PDZ domain binding motif, and it regulates the sorting of the internalized human choriogonadotropin and the density of cell surface hLHR
    • Hirakawa T., Galet C., Kishi M., Ascoli M. GIPC binds to the human lutropin receptor (hLHR) through an unusual PDZ domain binding motif, and it regulates the sorting of the internalized human choriogonadotropin and the density of cell surface hLHR. The Journal of Biological Chemistry 2003, 278(49):49348-49357.
    • (2003) The Journal of Biological Chemistry , vol.278 , Issue.49 , pp. 49348-49357
    • Hirakawa, T.1    Galet, C.2    Kishi, M.3    Ascoli, M.4
  • 51
    • 2942588535 scopus 로고    scopus 로고
    • κ Opioid receptor interacts with Na+/H+-exchanger regulatory factor-1/Ezrin-radixin-moesin-binding phosphoprotein-50 (NHERF-1/EBP50) to stimulate Na+/H+ exchange independent of Gi/Go proteins
    • Huang P., Steplock D., Weinman E.J., Hall R.A., Ding Z., Li J., et al. κ Opioid receptor interacts with Na+/H+-exchanger regulatory factor-1/Ezrin-radixin-moesin-binding phosphoprotein-50 (NHERF-1/EBP50) to stimulate Na+/H+ exchange independent of Gi/Go proteins. The Journal of Biological Chemistry 2004, 279(24):25002-25009.
    • (2004) The Journal of Biological Chemistry , vol.279 , Issue.24 , pp. 25002-25009
    • Huang, P.1    Steplock, D.2    Weinman, E.J.3    Hall, R.A.4    Ding, Z.5    Li, J.6
  • 52
    • 16844362568 scopus 로고    scopus 로고
    • The interaction of phospholipase C-ß3 with Shank2 regulates mGluR-mediated calcium signal
    • Hwang J.I., Kim H.S., Lee J.R., Kim E., Ryu S.H., Suh P.G. The interaction of phospholipase C-ß3 with Shank2 regulates mGluR-mediated calcium signal. The Journal of Biological Chemistry 2005, 280(13):12467-12473.
    • (2005) The Journal of Biological Chemistry , vol.280 , Issue.13 , pp. 12467-12473
    • Hwang, J.I.1    Kim, H.S.2    Lee, J.R.3    Kim, E.4    Ryu, S.H.5    Suh, P.G.6
  • 53
    • 0242384221 scopus 로고    scopus 로고
    • Physiological actions of regulators of G-protein signaling (RGS) proteins
    • Ishii M., Kurachi Y. Physiological actions of regulators of G-protein signaling (RGS) proteins. Life Sciences 2003, 74(2-3):163-171.
    • (2003) Life Sciences , vol.74 , Issue.2-3 , pp. 163-171
    • Ishii, M.1    Kurachi, Y.2
  • 54
    • 0742270638 scopus 로고    scopus 로고
    • Interactions of GIPC with dopamine D2, D3 but not D4 receptors define a novel mode of regulation of G protein-coupled receptors
    • Jeanneteau F., Diaz J., Sokoloff P., Griffon N. Interactions of GIPC with dopamine D2, D3 but not D4 receptors define a novel mode of regulation of G protein-coupled receptors. Molecular Biology of the Cell 2004, 15(2):696-705.
    • (2004) Molecular Biology of the Cell , vol.15 , Issue.2 , pp. 696-705
    • Jeanneteau, F.1    Diaz, J.2    Sokoloff, P.3    Griffon, N.4
  • 55
    • 0005169503 scopus 로고    scopus 로고
    • GABA(B) receptors function as a heteromeric assembly of the subunits GABA(B)R1 and GABA(B)R2
    • Jones K.A., Borowsky B., Tamm J.A., Craig D.A., Durkin M.M., Dai M., et al. GABA(B) receptors function as a heteromeric assembly of the subunits GABA(B)R1 and GABA(B)R2. Nature 1998, 396(6712):674-679.
    • (1998) Nature , vol.396 , Issue.6712 , pp. 674-679
    • Jones, K.A.1    Borowsky, B.2    Tamm, J.A.3    Craig, D.A.4    Durkin, M.M.5    Dai, M.6
  • 58
    • 0035906714 scopus 로고    scopus 로고
    • Crystal structure of the PDZ1 domain of human Na+/H+ exchanger regulatory factor provides insights into the mechanism of carboxyl-terminal leucine recognition by class I PDZ domains
    • Karthikeyan S., Leung T., Birrane G., Webster G., Ladias J.A. Crystal structure of the PDZ1 domain of human Na+/H+ exchanger regulatory factor provides insights into the mechanism of carboxyl-terminal leucine recognition by class I PDZ domains. Journal of Molecular Biology 2001, 308(5):963-973.
    • (2001) Journal of Molecular Biology , vol.308 , Issue.5 , pp. 963-973
    • Karthikeyan, S.1    Leung, T.2    Birrane, G.3    Webster, G.4    Ladias, J.A.5
  • 59
    • 0037083370 scopus 로고    scopus 로고
    • Tamalin, a PDZ domain-containing protein, links a protein complex formation of group 1 metabotropic glutamate receptors and the guanine nucleotide exchange factor cytohesins
    • Kitano J., Kimura K., Yamazaki Y., Soda T., Shigemoto R., Nakajima Y., et al. Tamalin, a PDZ domain-containing protein, links a protein complex formation of group 1 metabotropic glutamate receptors and the guanine nucleotide exchange factor cytohesins. The Journal of Neuroscience 2002, 22(4):1280-1289.
    • (2002) The Journal of Neuroscience , vol.22 , Issue.4 , pp. 1280-1289
    • Kitano, J.1    Kimura, K.2    Yamazaki, Y.3    Soda, T.4    Shigemoto, R.5    Nakajima, Y.6
  • 60
    • 0038013863 scopus 로고    scopus 로고
    • Tamalin is a scaffold protein that interacts with multiple neuronal proteins in distinct modes of protein-protein association
    • Kitano J., Yamazaki Y., Kimura K., Masukado T., Nakajima Y., Nakanishi S. Tamalin is a scaffold protein that interacts with multiple neuronal proteins in distinct modes of protein-protein association. The Journal of Biological Chemistry 2003, 278(17):14762-14768.
    • (2003) The Journal of Biological Chemistry , vol.278 , Issue.17 , pp. 14762-14768
    • Kitano, J.1    Yamazaki, Y.2    Kimura, K.3    Masukado, T.4    Nakajima, Y.5    Nakanishi, S.6
  • 61
    • 0030975196 scopus 로고    scopus 로고
    • Signaling by phosphoinositide-3,4,5-trisphosphate through proteins containing pleckstrin and Sec7 homology domains
    • Klarlund J.K., Guilherme A., Holik J.J., Virbasius J.V., Chawla A., Czech M.P. Signaling by phosphoinositide-3,4,5-trisphosphate through proteins containing pleckstrin and Sec7 homology domains. Science 1997, 275(5308):1927-1930.
    • (1997) Science , vol.275 , Issue.5308 , pp. 1927-1930
    • Klarlund, J.K.1    Guilherme, A.2    Holik, J.J.3    Virbasius, J.V.4    Chawla, A.5    Czech, M.P.6
  • 64
    • 79952292419 scopus 로고    scopus 로고
    • MAGI-3 competes with NHERF-2 to negatively regulate LPA(2) receptor signaling in colon cancer cells
    • Lee S.J., Ritter S.L., Zhang H., Shim H., Hall R.A., Yun C.C. MAGI-3 competes with NHERF-2 to negatively regulate LPA(2) receptor signaling in colon cancer cells. Gastroenterology 2011, 140(3):924-934.
    • (2011) Gastroenterology , vol.140 , Issue.3 , pp. 924-934
    • Lee, S.J.1    Ritter, S.L.2    Zhang, H.3    Shim, H.4    Hall, R.A.5    Yun, C.C.6
  • 65
    • 0344310763 scopus 로고    scopus 로고
    • Mechanisms of ß-adrenergic receptor desensitization and resensitization
    • Lefkowitz R.J., Pitcher J., Krueger K., Daaka Y. Mechanisms of ß-adrenergic receptor desensitization and resensitization. Advances in Pharmacology 1998, 42(2):416-420.
    • (1998) Advances in Pharmacology , vol.42 , Issue.2 , pp. 416-420
    • Lefkowitz, R.J.1    Pitcher, J.2    Krueger, K.3    Daaka, Y.4
  • 66
    • 33646681494 scopus 로고    scopus 로고
    • Deletions of genes encoding calcitonin/alpha-CGRP, amylin and calcitonin receptor have given new and unexpected insights into the function of calcitonin receptors and calcitonin receptor-like receptors in bone
    • Lerner U.H. Deletions of genes encoding calcitonin/alpha-CGRP, amylin and calcitonin receptor have given new and unexpected insights into the function of calcitonin receptors and calcitonin receptor-like receptors in bone. Journal of Musculoskeletal and Neuronal Interaction 2006, 6(1):87-95.
    • (2006) Journal of Musculoskeletal and Neuronal Interaction , vol.6 , Issue.1 , pp. 87-95
    • Lerner, U.H.1
  • 67
    • 68949167656 scopus 로고    scopus 로고
    • Ezrin induces long-range interdomain allostery in the scaffolding protein NHERF1
    • Li J., Callaway D.J.E., Bu Z. Ezrin induces long-range interdomain allostery in the scaffolding protein NHERF1. Journal of Molecular Biology 2009, 392(1):166-180.
    • (2009) Journal of Molecular Biology , vol.392 , Issue.1 , pp. 166-180
    • Li, J.1    Callaway, D.J.E.2    Bu, Z.3
  • 68
    • 0037178820 scopus 로고    scopus 로고
    • Ezrin-radixin-moesin-binding phosphoprotein-50/Na+/H+ exchanger regulatory factor (EBP50/NHERF) blocks U50,488H-induced down-regulation of the human kappa opioid receptor by enhancing its recycling rate
    • Li J.G., Chen C., Liu-Chen L.Y. Ezrin-radixin-moesin-binding phosphoprotein-50/Na+/H+ exchanger regulatory factor (EBP50/NHERF) blocks U50,488H-induced down-regulation of the human kappa opioid receptor by enhancing its recycling rate. The Journal of Biological Chemistry 2002, 277(30):27545-27552.
    • (2002) The Journal of Biological Chemistry , vol.277 , Issue.30 , pp. 27545-27552
    • Li, J.G.1    Chen, C.2    Liu-Chen, L.Y.3
  • 69
    • 0037077301 scopus 로고    scopus 로고
    • Selectivity and promiscuity of the first and second PDZ domains of PSD-95 and synapse-associated protein 102
    • Lim I.A., Hall D.D., Hell J.W. Selectivity and promiscuity of the first and second PDZ domains of PSD-95 and synapse-associated protein 102. The Journal of Biological Chemistry 2002, 277(24):21697-21711.
    • (2002) The Journal of Biological Chemistry , vol.277 , Issue.24 , pp. 21697-21711
    • Lim, I.A.1    Hall, D.D.2    Hell, J.W.3
  • 72
    • 0029895294 scopus 로고    scopus 로고
    • Cell-specific signal transduction of parathyroid hormone (PTH)-related protein through stably expressed recombinant PTH/PTHrP receptors in vascular smooth muscle cells
    • Maeda S., Wu S., Jüppner H., Green J., Aragay A.M., Fagin J.A., et al. Cell-specific signal transduction of parathyroid hormone (PTH)-related protein through stably expressed recombinant PTH/PTHrP receptors in vascular smooth muscle cells. Endocrinology 1996, 137(8):3154-3162.
    • (1996) Endocrinology , vol.137 , Issue.8 , pp. 3154-3162
    • Maeda, S.1    Wu, S.2    Jüppner, H.3    Green, J.4    Aragay, A.M.5    Fagin, J.A.6
  • 73
    • 77951667861 scopus 로고    scopus 로고
    • CRF receptor 1 regulates anxiety behavior via sensitization of 5-HT2 receptor signaling
    • Magalhaes A.C., Holmes K.D., Dale L.B., Comps-Agrar L., Lee D., Yadav P.N., et al. CRF receptor 1 regulates anxiety behavior via sensitization of 5-HT2 receptor signaling. Nature Neuroscience 2010, 13(5):622-629.
    • (2010) Nature Neuroscience , vol.13 , Issue.5 , pp. 622-629
    • Magalhaes, A.C.1    Holmes, K.D.2    Dale, L.B.3    Comps-Agrar, L.4    Lee, D.5    Yadav, P.N.6
  • 74
    • 38749090547 scopus 로고    scopus 로고
    • Indole-2-amide based biochemical antagonist of Dishevelled PDZ domain interaction down-regulates Dishevelled-driven Tcf transcriptional activity
    • Mahindroo N., Punchihewa C., Bail A.M., Fujii N. Indole-2-amide based biochemical antagonist of Dishevelled PDZ domain interaction down-regulates Dishevelled-driven Tcf transcriptional activity. Bioorganic & Medicinal Chemistry Letters 2008, 18(3):946-949.
    • (2008) Bioorganic & Medicinal Chemistry Letters , vol.18 , Issue.3 , pp. 946-949
    • Mahindroo, N.1    Punchihewa, C.2    Bail, A.M.3    Fujii, N.4
  • 75
    • 0037142080 scopus 로고    scopus 로고
    • Na+/H+ exchanger regulatory factor 2 directs parathyroid hormone 1 receptor signalling
    • Mahon M.J., Donowitz M., Yun C.C., Segre G.V. Na+/H+ exchanger regulatory factor 2 directs parathyroid hormone 1 receptor signalling. Nature 2002, 417(6891):858-861.
    • (2002) Nature , vol.417 , Issue.6891 , pp. 858-861
    • Mahon, M.J.1    Donowitz, M.2    Yun, C.C.3    Segre, G.V.4
  • 76
    • 2542420098 scopus 로고    scopus 로고
    • Stimulation by parathyroid hormone of a NHERF-1-assembled complex consisting of the parathyroid hormone I receptor, PLCß, and actin increases intracellular calcium in opossum kidney cells
    • Mahon M.J., Segre G.V. Stimulation by parathyroid hormone of a NHERF-1-assembled complex consisting of the parathyroid hormone I receptor, PLCß, and actin increases intracellular calcium in opossum kidney cells. The Journal of Biological Chemistry 2004, 279(22):23550-23558.
    • (2004) The Journal of Biological Chemistry , vol.279 , Issue.22 , pp. 23550-23558
    • Mahon, M.J.1    Segre, G.V.2
  • 78
    • 14944372499 scopus 로고    scopus 로고
    • The scaffold protein Homer1b/c links metabotropic glutamate receptor 5 to extracellular signal-regulated protein kinase cascades in neurons
    • Mao L., Yang L., Tang Q., Samdani S., Zhang G., Wang J.Q. The scaffold protein Homer1b/c links metabotropic glutamate receptor 5 to extracellular signal-regulated protein kinase cascades in neurons. The Journal of Neuroscience 2005, 25(10):2741-2752.
    • (2005) The Journal of Neuroscience , vol.25 , Issue.10 , pp. 2741-2752
    • Mao, L.1    Yang, L.2    Tang, Q.3    Samdani, S.4    Zhang, G.5    Wang, J.Q.6
  • 79
    • 28144441697 scopus 로고    scopus 로고
    • Wingless signaling at synapses is through cleavage and nuclear import of receptor DFrizzled2
    • Mathew D., Ataman B., Chen J., Zhang Y., Cumberledge S., Budnik V. Wingless signaling at synapses is through cleavage and nuclear import of receptor DFrizzled2. Science 2005, 310(5752):1344-1347.
    • (2005) Science , vol.310 , Issue.5752 , pp. 1344-1347
    • Mathew, D.1    Ataman, B.2    Chen, J.3    Zhang, Y.4    Cumberledge, S.5    Budnik, V.6
  • 80
    • 0033755880 scopus 로고    scopus 로고
    • Platelet-derived growth factor receptor association with Na+/H+ exchanger regulatory factor potentiates receptor activity
    • Maudsley S., Zamah A.M., Rahman N., Blitzer J.T., Luttrell L.M., Lefkowitz R.J., et al. Platelet-derived growth factor receptor association with Na+/H+ exchanger regulatory factor potentiates receptor activity. Molecular and Cellular Biology 2000, 20(22):8352-8363.
    • (2000) Molecular and Cellular Biology , vol.20 , Issue.22 , pp. 8352-8363
    • Maudsley, S.1    Zamah, A.M.2    Rahman, N.3    Blitzer, J.T.4    Luttrell, L.M.5    Lefkowitz, R.J.6
  • 81
    • 0032574982 scopus 로고    scopus 로고
    • RAMPs regulate the transport and ligand specificity of the calcitonin-receptor-like receptor
    • McLatchie L.M., Fraser N.J., Main M.J., Wise A., Brown J., Thompson N., et al. RAMPs regulate the transport and ligand specificity of the calcitonin-receptor-like receptor. Nature 1998, 393(6683):333-339.
    • (1998) Nature , vol.393 , Issue.6683 , pp. 333-339
    • McLatchie, L.M.1    Fraser, N.J.2    Main, M.J.3    Wise, A.4    Brown, J.5    Thompson, N.6
  • 83
    • 33646941288 scopus 로고    scopus 로고
    • Asymmetric localization of Vangl2 and Fz3 indicate novel mechanisms for planar cell polarity in mammals
    • Montcouquiol M., Sans N., Huss D., Kach J., Dickman J.D., Forge A., et al. Asymmetric localization of Vangl2 and Fz3 indicate novel mechanisms for planar cell polarity in mammals. The Journal of Neuroscience 2006, 26(19):5265-5275.
    • (2006) The Journal of Neuroscience , vol.26 , Issue.19 , pp. 5265-5275
    • Montcouquiol, M.1    Sans, N.2    Huss, D.3    Kach, J.4    Dickman, J.D.5    Forge, A.6
  • 86
    • 13444260744 scopus 로고    scopus 로고
    • Parathyroid hormone secretion and action: Evidence for discrete receptors for the carboxyl-terminal region and related biological actions of carboxyl-terminal ligands
    • Murray T.M., Rao L.G., Divieti P., Bringhurst F.R. Parathyroid hormone secretion and action: Evidence for discrete receptors for the carboxyl-terminal region and related biological actions of carboxyl-terminal ligands. Endocrine Reviews 2005, 26(1):78-113.
    • (2005) Endocrine Reviews , vol.26 , Issue.1 , pp. 78-113
    • Murray, T.M.1    Rao, L.G.2    Divieti, P.3    Bringhurst, F.R.4
  • 87
    • 78751578854 scopus 로고    scopus 로고
    • Pharmacological inhibition of Frizzled-7 displays anti-tumor properties in hepatocellular carcinoma
    • Nambotin S.B., Lefrancois L., Sainsily X., Berthillon P., Kim M., Wands J.R., et al. Pharmacological inhibition of Frizzled-7 displays anti-tumor properties in hepatocellular carcinoma. Journal of Hepatology 2011, 54(2):288-299.
    • (2011) Journal of Hepatology , vol.54 , Issue.2 , pp. 288-299
    • Nambotin, S.B.1    Lefrancois, L.2    Sainsily, X.3    Berthillon, P.4    Kim, M.5    Wands, J.R.6
  • 88
    • 0033777931 scopus 로고    scopus 로고
    • Localization of BAI-associated protein1/membrane-associated guanylate kinase-1 at adherens junctions in normal rat kidney cells: Polarized targeting mediated by the carboxyl-terminal PDZ domains
    • Nishimura W., Iizuka T., Hirabayashi S., Tanaka N., Hata Y. Localization of BAI-associated protein1/membrane-associated guanylate kinase-1 at adherens junctions in normal rat kidney cells: Polarized targeting mediated by the carboxyl-terminal PDZ domains. Journal of Cellular Physiology 2000, 185(3):358-365.
    • (2000) Journal of Cellular Physiology , vol.185 , Issue.3 , pp. 358-365
    • Nishimura, W.1    Iizuka, T.2    Hirabayashi, S.3    Tanaka, N.4    Hata, Y.5
  • 89
  • 90
    • 2442676625 scopus 로고    scopus 로고
    • NHERF2 specifically interacts with LPA2 receptor and defines the specificity and efficiency of receptor-mediated phospholipase C-ß3 activation
    • Oh Y.S., Jo N.W., Choi J.W., Kim H.S., Seo S.W., Kang K.O., et al. NHERF2 specifically interacts with LPA2 receptor and defines the specificity and efficiency of receptor-mediated phospholipase C-ß3 activation. Molecular and Cellular Biology 2004, 24(11):5069-5079.
    • (2004) Molecular and Cellular Biology , vol.24 , Issue.11 , pp. 5069-5079
    • Oh, Y.S.1    Jo, N.W.2    Choi, J.W.3    Kim, H.S.4    Seo, S.W.5    Kang, K.O.6
  • 91
    • 0029042451 scopus 로고
    • Further evidence for a novel receptor for amino-terminal parathyroid hormone-related protein on keratinocytes and squamous carcinoma cell lines
    • Orloff J.J., Kats Y., Urena P., Schipani E., Vasavada R.C., Philbrick W.M., et al. Further evidence for a novel receptor for amino-terminal parathyroid hormone-related protein on keratinocytes and squamous carcinoma cell lines. Endocrinology 1995, 136(7):3016-3023.
    • (1995) Endocrinology , vol.136 , Issue.7 , pp. 3016-3023
    • Orloff, J.J.1    Kats, Y.2    Urena, P.3    Schipani, E.4    Vasavada, R.C.5    Philbrick, W.M.6
  • 92
    • 17844375640 scopus 로고    scopus 로고
    • Subtype-specific sorting of the ETA endothelin receptor by a novel endocytic recycling signal for G protein-coupled receptors
    • Paasche J.D., Attramadal T., Kristiansen K., Oksvold M.P., Johansen H.K., Huitfeldt H.S., et al. Subtype-specific sorting of the ETA endothelin receptor by a novel endocytic recycling signal for G protein-coupled receptors. Molecular Pharmacology 2005, 67(5):1581-1590.
    • (2005) Molecular Pharmacology , vol.67 , Issue.5 , pp. 1581-1590
    • Paasche, J.D.1    Attramadal, T.2    Kristiansen, K.3    Oksvold, M.P.4    Johansen, H.K.5    Huitfeldt, H.S.6
  • 93
    • 77955024111 scopus 로고    scopus 로고
    • GABAB receptor coupling to G-proteins and ion channels
    • Padgett C.L., Slesinger P.A. GABAB receptor coupling to G-proteins and ion channels. Advances in Pharmacology 2010, 58:123-147.
    • (2010) Advances in Pharmacology , vol.58 , pp. 123-147
    • Padgett, C.L.1    Slesinger, P.A.2
  • 94
    • 16644386504 scopus 로고    scopus 로고
    • Characterization of function of three domains in Dishevelled-1: DEP domain is responsible for membrane translocation of Dishevelled-1
    • Pan W.J., Pang S.Z., Huang T., Guo H.Y., Wu D., Li L. Characterization of function of three domains in Dishevelled-1: DEP domain is responsible for membrane translocation of Dishevelled-1. Cell Research 2004, 14(4):324-330.
    • (2004) Cell Research , vol.14 , Issue.4 , pp. 324-330
    • Pan, W.J.1    Pang, S.Z.2    Huang, T.3    Guo, H.Y.4    Wu, D.5    Li, L.6
  • 96
    • 0037124377 scopus 로고    scopus 로고
    • PICK1 is required for the control of synaptic transmission by the metabotropic glutamate receptor 7
    • Perroy J., El Far O., Bertaso F., Pin J.P., Betz H., Bockaert J., et al. PICK1 is required for the control of synaptic transmission by the metabotropic glutamate receptor 7. The EMBO Journal 2002, 21(12):2990-2999.
    • (2002) The EMBO Journal , vol.21 , Issue.12 , pp. 2990-2999
    • Perroy, J.1    El Far, O.2    Bertaso, F.3    Pin, J.P.4    Betz, H.5    Bockaert, J.6
  • 97
    • 0035824541 scopus 로고    scopus 로고
    • The C terminus of the metabotropic glutamate receptor subtypes 2 and 7 specifies the receptor signaling pathways
    • Perroy J., Gutierrez G.J., Coulon V., Bockaert J., Pin J.P., Fagni L. The C terminus of the metabotropic glutamate receptor subtypes 2 and 7 specifies the receptor signaling pathways. The Journal of Biological Chemistry 2001, 276(49):45800-45805.
    • (2001) The Journal of Biological Chemistry , vol.276 , Issue.49 , pp. 45800-45805
    • Perroy, J.1    Gutierrez, G.J.2    Coulon, V.3    Bockaert, J.4    Pin, J.P.5    Fagni, L.6
  • 99
    • 61449210006 scopus 로고    scopus 로고
    • Identification of a novel region of the GABA(B2) C-terminus that regulates surface expression and neuronal targeting of the GABA(B) receptor
    • Pooler A.M., Gray A.G., McIlhinney R.A. Identification of a novel region of the GABA(B2) C-terminus that regulates surface expression and neuronal targeting of the GABA(B) receptor. The European Journal of Neuroscience 2009, 29(5):869-878.
    • (2009) The European Journal of Neuroscience , vol.29 , Issue.5 , pp. 869-878
    • Pooler, A.M.1    Gray, A.G.2    McIlhinney, R.A.3
  • 100
    • 68849124264 scopus 로고    scopus 로고
    • Sequence requirement and subtype specificity in the high-affinity interaction between human frizzled and Dishevelled proteins
    • Punchihewa C., Ferreira A.M., Cassell R., Rodrigues P., Fujii N. Sequence requirement and subtype specificity in the high-affinity interaction between human frizzled and Dishevelled proteins. Protein Science 2009, 18(5):994-1002.
    • (2009) Protein Science , vol.18 , Issue.5 , pp. 994-1002
    • Punchihewa, C.1    Ferreira, A.M.2    Cassell, R.3    Rodrigues, P.4    Fujii, N.5
  • 101
    • 2642583318 scopus 로고    scopus 로고
    • Interaction of neuronal nitric oxide synthase with alpha1-adrenergic receptor subtypes in transfected HEK-293 cells
    • Pupo A.S., Minneman K.P. Interaction of neuronal nitric oxide synthase with alpha1-adrenergic receptor subtypes in transfected HEK-293 cells. BMC Pharmacology 2002, 2:17.
    • (2002) BMC Pharmacology , vol.2 , pp. 17
    • Pupo, A.S.1    Minneman, K.P.2
  • 102
    • 33749079184 scopus 로고    scopus 로고
    • Cargo regulates clathrin-coated pit dynamics
    • Puthenveedu M.A., von Zastrow M. Cargo regulates clathrin-coated pit dynamics. Cell 2006, 127(1):113-124.
    • (2006) Cell , vol.127 , Issue.1 , pp. 113-124
    • Puthenveedu, M.A.1    von Zastrow, M.2
  • 103
  • 104
    • 43049083994 scopus 로고    scopus 로고
    • 5-HT2C and GABAB receptors influence handling-induced convulsion severity in chromosome 4 congenic and DBA/2J background strain mice
    • Reilly M.T., Milner L.C., Shirley R.L., Crabbe J.C., Buck K.J. 5-HT2C and GABAB receptors influence handling-induced convulsion severity in chromosome 4 congenic and DBA/2J background strain mice. Brain Research 2008, 1198:124-131.
    • (2008) Brain Research , vol.1198 , pp. 124-131
    • Reilly, M.T.1    Milner, L.C.2    Shirley, R.L.3    Crabbe, J.C.4    Buck, K.J.5
  • 105
    • 0037175055 scopus 로고    scopus 로고
    • Regulation of GTP-binding protein αq (Gαq) signaling by the ezrin-radixin-moesin-binding phosphoprotein-50 (EBP50)
    • Rochdi M.D., Watier V., La Madeleine C., Nakata H., Kozasa T., Parent J.L. Regulation of GTP-binding protein αq (Gαq) signaling by the ezrin-radixin-moesin-binding phosphoprotein-50 (EBP50). The Journal of Biological Chemistry 2002, 277(43):40751-40759.
    • (2002) The Journal of Biological Chemistry , vol.277 , Issue.43 , pp. 40751-40759
    • Rochdi, M.D.1    Watier, V.2    La Madeleine, C.3    Nakata, H.4    Kozasa, T.5    Parent, J.L.6
  • 106
    • 77952004118 scopus 로고    scopus 로고
    • Parathyroid hormone receptor directly interacts with Dishevelled to regulate β-catenin signaling and osteoclastogenesis
    • Romero G., Sneddon W.B., Yang Y., Wheeler D., Blair H.C., Friedman P.A. Parathyroid hormone receptor directly interacts with Dishevelled to regulate β-catenin signaling and osteoclastogenesis. The Journal of Biological Chemistry 2010, 285(19):14756-14763.
    • (2010) The Journal of Biological Chemistry , vol.285 , Issue.19 , pp. 14756-14763
    • Romero, G.1    Sneddon, W.B.2    Yang, Y.3    Wheeler, D.4    Blair, H.C.5    Friedman, P.A.6
  • 107
    • 18244374184 scopus 로고    scopus 로고
    • Key role of the postsynaptic density scaffold proteins Shank and Homer in the functional architecture of Ca2+ homeostasis at dendritic spines in hippocampal neurons
    • Sala C., Roussignol G., Meldolesi J., Fagni L. Key role of the postsynaptic density scaffold proteins Shank and Homer in the functional architecture of Ca2+ homeostasis at dendritic spines in hippocampal neurons. The Journal of Neuroscience 2005, 25(18):4587-4592.
    • (2005) The Journal of Neuroscience , vol.25 , Issue.18 , pp. 4587-4592
    • Sala, C.1    Roussignol, G.2    Meldolesi, J.3    Fagni, L.4
  • 108
    • 33645109501 scopus 로고    scopus 로고
    • The effect of RGS12 on PDGFß receptor signalling to p42/p44 mitogen activated protein kinase in mammalian cells
    • Sambi B.S., Hains M.D., Waters C.M., Connell M.C., Willard F.S., Kimple A.J., et al. The effect of RGS12 on PDGFß receptor signalling to p42/p44 mitogen activated protein kinase in mammalian cells. Cellular Signalling 2006, 18(7):971-981.
    • (2006) Cellular Signalling , vol.18 , Issue.7 , pp. 971-981
    • Sambi, B.S.1    Hains, M.D.2    Waters, C.M.3    Connell, M.C.4    Willard, F.S.5    Kimple, A.J.6
  • 109
    • 0030995719 scopus 로고    scopus 로고
    • The neuronal nitric oxide synthase PDZ motif binds to -G(D, E)XV* carboxyterminal sequences
    • Schepens J., Cuppen E., Wieringa B., Hendriks W. The neuronal nitric oxide synthase PDZ motif binds to -G(D, E)XV* carboxyterminal sequences. FEBS Letters 1997, 409(1):53-56.
    • (1997) FEBS Letters , vol.409 , Issue.1 , pp. 53-56
    • Schepens, J.1    Cuppen, E.2    Wieringa, B.3    Hendriks, W.4
  • 110
    • 0029029862 scopus 로고
    • Parathyroid hormone induces PKC but not adenylate cyclase in adult cardiomyocytes and regulates cyclic AMP levels via PKC-dependent phosphodiesterase activity
    • Schlüter K.D., Weber M., Piper H.M. Parathyroid hormone induces PKC but not adenylate cyclase in adult cardiomyocytes and regulates cyclic AMP levels via PKC-dependent phosphodiesterase activity. The Biochemical Journal 1995, 310(Pt 2):439-444.
    • (1995) The Biochemical Journal , vol.310 , Issue.PART 2 , pp. 439-444
    • Schlüter, K.D.1    Weber, M.2    Piper, H.M.3
  • 111
    • 34748812548 scopus 로고    scopus 로고
    • The Frizzled family of unconventional G-protein-coupled receptors
    • Schulte G., Bryja V. The Frizzled family of unconventional G-protein-coupled receptors. Trends in Pharmacological Sciences 2007, 28(10):518-525.
    • (2007) Trends in Pharmacological Sciences , vol.28 , Issue.10 , pp. 518-525
    • Schulte, G.1    Bryja, V.2
  • 112
    • 28244496603 scopus 로고    scopus 로고
    • Identification of a specific inhibitor of the Dishevelled PDZ domain
    • Shan J., Shi D.L., Wang J., Zheng J. Identification of a specific inhibitor of the Dishevelled PDZ domain. Biochemistry 2005, 44(47):15495-15503.
    • (2005) Biochemistry , vol.44 , Issue.47 , pp. 15495-15503
    • Shan, J.1    Shi, D.L.2    Wang, J.3    Zheng, J.4
  • 115
    • 0037031938 scopus 로고    scopus 로고
    • The adenosine 2b receptor is recruited to the plasma membrane and associates with E3KARP and ezrin upon agonist stimulation
    • Sitaraman S.V., Wang L., Bruewer M., Hobert M., Wong M., Yun C.H., et al. The adenosine 2b receptor is recruited to the plasma membrane and associates with E3KARP and ezrin upon agonist stimulation. The Journal of Biological Chemistry 2002, 277(36):33188-33195.
    • (2002) The Journal of Biological Chemistry , vol.277 , Issue.36 , pp. 33188-33195
    • Sitaraman, S.V.1    Wang, L.2    Bruewer, M.3    Hobert, M.4    Wong, M.5    Yun, C.H.6
  • 117
    • 15644373915 scopus 로고    scopus 로고
    • GTPase activating specificity of RGS12 and binding specificity of an alternatively spliced PDZ (PSD-95/Dlg/ZO-1) domain
    • Snow B.E., Hall R.A., Krumins A.M., Brothers G.M., Bouchard D., Brothers C.A., et al. GTPase activating specificity of RGS12 and binding specificity of an alternatively spliced PDZ (PSD-95/Dlg/ZO-1) domain. The Journal of Biological Chemistry 1998, 273(28):17749-17755.
    • (1998) The Journal of Biological Chemistry , vol.273 , Issue.28 , pp. 17749-17755
    • Snow, B.E.1    Hall, R.A.2    Krumins, A.M.3    Brothers, G.M.4    Bouchard, D.5    Brothers, C.A.6
  • 118
    • 15644379801 scopus 로고    scopus 로고
    • Recognition of unique carboxyl-terminal motifs by distinct PDZ domains
    • Songyang Z., Fanning A.S., Fu C., Xu J., Marfatia S.M., Chishti A.H., et al. Recognition of unique carboxyl-terminal motifs by distinct PDZ domains. Science 1997, 275(5296):73-77.
    • (1997) Science , vol.275 , Issue.5296 , pp. 73-77
    • Songyang, Z.1    Fanning, A.S.2    Fu, C.3    Xu, J.4    Marfatia, S.M.5    Chishti, A.H.6
  • 119
    • 44649149583 scopus 로고    scopus 로고
    • Corequirement of PICK1 binding and PKC phosphorylation for stable surface expression of the metabotropic glutamate receptor mGluR7
    • Suh Y.H., Pelkey K.A., Lavezzari G., Roche P.A., Huganir R.L., McBain C.J., et al. Corequirement of PICK1 binding and PKC phosphorylation for stable surface expression of the metabotropic glutamate receptor mGluR7. Neuron 2008, 58(5):736-748.
    • (2008) Neuron , vol.58 , Issue.5 , pp. 736-748
    • Suh, Y.H.1    Pelkey, K.A.2    Lavezzari, G.3    Roche, P.A.4    Huganir, R.L.5    McBain, C.J.6
  • 120
    • 0034721943 scopus 로고    scopus 로고
    • Formation of nNOS/PSD-95 PDZ dimer requires a preformed ß-finger structure from the nNOS PDZ domain
    • Tochio H., Mok Y.K., Zhang Q., Kan H.M., Bredt D.S., Zhang M. Formation of nNOS/PSD-95 PDZ dimer requires a preformed ß-finger structure from the nNOS PDZ domain. Journal of Molecular Biology 2000, 303(3):359-370.
    • (2000) Journal of Molecular Biology , vol.303 , Issue.3 , pp. 359-370
    • Tochio, H.1    Mok, Y.K.2    Zhang, Q.3    Kan, H.M.4    Bredt, D.S.5    Zhang, M.6
  • 122
    • 0033166537 scopus 로고    scopus 로고
    • Coupling of mGluR/Homer and PSD-95 complexes by the Shank family of postsynaptic density proteins
    • Tu J.C., Xiao B., Naisbitt S., Yuan J.P., Petralia R.S., Brakeman P., et al. Coupling of mGluR/Homer and PSD-95 complexes by the Shank family of postsynaptic density proteins. Neuron 1999, 23(3):583-592.
    • (1999) Neuron , vol.23 , Issue.3 , pp. 583-592
    • Tu, J.C.1    Xiao, B.2    Naisbitt, S.3    Yuan, J.P.4    Petralia, R.S.5    Brakeman, P.6
  • 123
    • 0032192487 scopus 로고    scopus 로고
    • Homer binds a novel proline-rich motif and links group 1 metabotropic glutamate receptors with IP3 receptors
    • Tu J.C., Xiao B., Yuan J.P., Lanahan A.A., Leoffert K., Li M., et al. Homer binds a novel proline-rich motif and links group 1 metabotropic glutamate receptors with IP3 receptors. Neuron 1998, 21(4):717-726.
    • (1998) Neuron , vol.21 , Issue.4 , pp. 717-726
    • Tu, J.C.1    Xiao, B.2    Yuan, J.P.3    Lanahan, A.A.4    Leoffert, K.5    Li, M.6
  • 124
    • 0034665045 scopus 로고    scopus 로고
    • The C-terminal cytoplasmic Lys-Thr-X-X-X-Trp motif in frizzled receptors mediates Wnt/ß-catenin signalling
    • Umbhauer M., Djiane A., Goisset C., Penzo-Mendez A., Riou J.F., Boucaut J.C., et al. The C-terminal cytoplasmic Lys-Thr-X-X-X-Trp motif in frizzled receptors mediates Wnt/ß-catenin signalling. The EMBO Journal 2000, 19(18):4944-4954.
    • (2000) The EMBO Journal , vol.19 , Issue.18 , pp. 4944-4954
    • Umbhauer, M.1    Djiane, A.2    Goisset, C.3    Penzo-Mendez, A.4    Riou, J.F.5    Boucaut, J.C.6
  • 125
    • 77956247356 scopus 로고    scopus 로고
    • Na/H exchanger regulatory factors control PTH receptor signaling by differential activation of Gα protein subunits
    • Wang B., Ardura J.A., Romero G., Yang Y., Hall R.A., Friedman P.A. Na/H exchanger regulatory factors control PTH receptor signaling by differential activation of Gα protein subunits. The Journal of Biological Chemistry 2010, 285(35):26976-26986.
    • (2010) The Journal of Biological Chemistry , vol.285 , Issue.35 , pp. 26976-26986
    • Wang, B.1    Ardura, J.A.2    Romero, G.3    Yang, Y.4    Hall, R.A.5    Friedman, P.A.6
  • 126
    • 66149096210 scopus 로고    scopus 로고
    • NHERF1 regulates parathyroid hormone receptor desensitization; interference with ß-arrestin binding
    • Wang B., Yang Y., Abou-Samra A.B., Friedman P.A. NHERF1 regulates parathyroid hormone receptor desensitization; interference with ß-arrestin binding. Molecular Pharmacology 2009, 75(5):1189-1197.
    • (2009) Molecular Pharmacology , vol.75 , Issue.5 , pp. 1189-1197
    • Wang, B.1    Yang, Y.2    Abou-Samra, A.B.3    Friedman, P.A.4
  • 127
    • 36048958880 scopus 로고    scopus 로고
    • Parathyroid hormone inhibits renal phosphate transport by phosphorylation of serine 77 of sodium-hydrogen exchanger regulatory factor-1
    • Weinman E.J., Biswas R.S., Peng Q., Shen L., Turner C.L., Steplock E.X., et al. Parathyroid hormone inhibits renal phosphate transport by phosphorylation of serine 77 of sodium-hydrogen exchanger regulatory factor-1. The Journal of Clinical Investigation 2007, 117(11):3412-3420.
    • (2007) The Journal of Clinical Investigation , vol.117 , Issue.11 , pp. 3412-3420
    • Weinman, E.J.1    Biswas, R.S.2    Peng, Q.3    Shen, L.4    Turner, C.L.5    Steplock, E.X.6
  • 131
    • 0015179028 scopus 로고
    • The roles of calcium and cyclic AMP in the stimulatory action of parathyroid hormone on thymic lymphocyte proliferation
    • Whitfield J.F., MacManus J.P., Youdale T., Franks D.J. The roles of calcium and cyclic AMP in the stimulatory action of parathyroid hormone on thymic lymphocyte proliferation. Journal of Cellular Physiology 1971, 78(3):355-368.
    • (1971) Journal of Cellular Physiology , vol.78 , Issue.3 , pp. 355-368
    • Whitfield, J.F.1    MacManus, J.P.2    Youdale, T.3    Franks, D.J.4
  • 132
    • 0344413477 scopus 로고    scopus 로고
    • Direct binding of the PDZ domain of Dishevelled to a conserved internal sequence in the C-terminal region of Frizzled
    • Wong H.C., Bourdelas A., Krauss A., Lee H.J., Shao Y., Wu D., et al. Direct binding of the PDZ domain of Dishevelled to a conserved internal sequence in the C-terminal region of Frizzled. Molecular Cell 2003, 12(5):1251-1260.
    • (2003) Molecular Cell , vol.12 , Issue.5 , pp. 1251-1260
    • Wong, H.C.1    Bourdelas, A.2    Krauss, A.3    Lee, H.J.4    Shao, Y.5    Wu, D.6
  • 133
    • 51449094916 scopus 로고    scopus 로고
    • The frizzled extracellular domain is a ligand for Van Gogh/Stbm during nonautonomous planar cell polarity signaling
    • Wu J., Mlodzik M. The frizzled extracellular domain is a ligand for Van Gogh/Stbm during nonautonomous planar cell polarity signaling. Developmental Cell 2008, 15(3):462-469.
    • (2008) Developmental Cell , vol.15 , Issue.3 , pp. 462-469
    • Wu, J.1    Mlodzik, M.2
  • 134
    • 0027138650 scopus 로고
    • Effects of N-terminal, midregion, and C-terminal parathyroid hormone-related peptides on adenosine 3',5'-monophosphate and cytoplasmic free calcium in rat aortic smooth muscle cells and UMR-106 osteoblast-like cells
    • Wu S., Pirola C.J., Green J., Yamaguchi D.T., Okano K., Jueppner H., et al. Effects of N-terminal, midregion, and C-terminal parathyroid hormone-related peptides on adenosine 3',5'-monophosphate and cytoplasmic free calcium in rat aortic smooth muscle cells and UMR-106 osteoblast-like cells. Endocrinology 1993, 133(6):2437-2444.
    • (1993) Endocrinology , vol.133 , Issue.6 , pp. 2437-2444
    • Wu, S.1    Pirola, C.J.2    Green, J.3    Yamaguchi, D.T.4    Okano, K.5    Jueppner, H.6
  • 135
    • 18544393408 scopus 로고    scopus 로고
    • Homer regulates the association of group 1 metabotropic glutamate receptors with multivalent complexes of homer-related, synaptic proteins
    • Xiao B., Tu J.C., Petralia R.S., Yuan J.P., Doan A., Breder C.D., et al. Homer regulates the association of group 1 metabotropic glutamate receptors with multivalent complexes of homer-related, synaptic proteins. Neuron 1998, 21(4):707-716.
    • (1998) Neuron , vol.21 , Issue.4 , pp. 707-716
    • Xiao, B.1    Tu, J.C.2    Petralia, R.S.3    Yuan, J.P.4    Doan, A.5    Breder, C.D.6
  • 136
    • 21444444299 scopus 로고    scopus 로고
    • Physical and functional interactions of the lysophosphatidic acid receptors with PDZ domain-containing Rho guanine nucleotide exchange factors (RhoGEFs)
    • Yamada T., Ohoka Y., Kogo M., Inagaki S. Physical and functional interactions of the lysophosphatidic acid receptors with PDZ domain-containing Rho guanine nucleotide exchange factors (RhoGEFs). The Journal of Biological Chemistry 2005, 280(19):19358-19363.
    • (2005) The Journal of Biological Chemistry , vol.280 , Issue.19 , pp. 19358-19363
    • Yamada, T.1    Ohoka, Y.2    Kogo, M.3    Inagaki, S.4
  • 137
    • 0034812092 scopus 로고    scopus 로고
    • Identification of a PDZ domain containing Golgi protein, GOPC, as an interaction partner of frizzled
    • Yao R., Maeda T., Takada S., Noda T. Identification of a PDZ domain containing Golgi protein, GOPC, as an interaction partner of frizzled. Biochemical and Biophysical Research Communications 2001, 286(4):771-778.
    • (2001) Biochemical and Biophysical Research Communications , vol.286 , Issue.4 , pp. 771-778
    • Yao, R.1    Maeda, T.2    Takada, S.3    Noda, T.4
  • 138
    • 4444262013 scopus 로고    scopus 로고
    • MAGI-3 is involved in the regulation of the JNK signaling pathway as a scaffold protein for frizzled and Ltap
    • Yao R., Natsume Y., Noda T. MAGI-3 is involved in the regulation of the JNK signaling pathway as a scaffold protein for frizzled and Ltap. Oncogene 2004, 23(36):6023-6030.
    • (2004) Oncogene , vol.23 , Issue.36 , pp. 6023-6030
    • Yao, R.1    Natsume, Y.2    Noda, T.3
  • 139
    • 49849093718 scopus 로고    scopus 로고
    • Evaluation of a chemical library of small-molecule Dishevelled antagonists that suppress tumor growth by down-regulating T-cell factor-mediated transcription
    • You L., Xu Z., Punchihewa C., Jablons D.M., Fujii N. Evaluation of a chemical library of small-molecule Dishevelled antagonists that suppress tumor growth by down-regulating T-cell factor-mediated transcription. Molecular Cancer Therapeutics 2008, 7(6):1633-1638.
    • (2008) Molecular Cancer Therapeutics , vol.7 , Issue.6 , pp. 1633-1638
    • You, L.1    Xu, Z.2    Punchihewa, C.3    Jablons, D.M.4    Fujii, N.5
  • 140
    • 33845788234 scopus 로고    scopus 로고
    • MAGI-3 regulates LPA-induced activation of Erk and RhoA
    • Zhang H., Wang D., Sun H., Hall R.A., Yun C.C. MAGI-3 regulates LPA-induced activation of Erk and RhoA. Cellular Signalling 2007, 19(2):261-268.
    • (2007) Cellular Signalling , vol.19 , Issue.2 , pp. 261-268
    • Zhang, H.1    Wang, D.2    Sun, H.3    Hall, R.A.4    Yun, C.C.5
  • 141
    • 33746819780 scopus 로고    scopus 로고
    • Convergent and divergent ligand specificity among PDZ domains of the LAP and zonula occludens (ZO) families
    • Zhang Y., Yeh S., Appleton B.A., Held H.A., Kausalya P.J., Phua D.C., et al. Convergent and divergent ligand specificity among PDZ domains of the LAP and zonula occludens (ZO) families. The Journal of Biological Chemistry 2006, 281(31):22299-22311.
    • (2006) The Journal of Biological Chemistry , vol.281 , Issue.31 , pp. 22299-22311
    • Zhang, Y.1    Yeh, S.2    Appleton, B.A.3    Held, H.A.4    Kausalya, P.J.5    Phua, D.C.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.