메뉴 건너뛰기




Volumn 62, Issue , 2011, Pages 349-380

GPCR-Interacting Proteins, Major Players of GPCR Function

Author keywords

Biosynthesis; Desensitization; G protein coupled receptor; Protein complexes; Recycling; Signaling

Indexed keywords

BETA ARRESTIN 1; BETA ARRESTIN 2; CALCITONIN RECEPTOR LIKE RECEPTOR; CALNEXIN; CALRETICULIN; CHAPERONE; CYTOSKELETON PROTEIN; DOPAMINE RECEPTOR INTERACTING PROTEIN 78; G PROTEIN COUPLED RECEPTOR; G PROTEIN COUPLED RECEPTOR INTERACTING PROTEIN; GONADORELIN; GUANINE NUCLEOTIDE BINDING PROTEIN; MEMBRANE PROTEIN; MU OPIATE RECEPTOR; PDZ PROTEIN; RAB PROTEIN; RECEPTOR ACTIVITY MODIFYING PROTEIN; RGS PROTEIN; RIBOPHORIN I; UNCLASSIFIED DRUG;

EID: 80052690010     PISSN: 10543589     EISSN: 15578925     Source Type: Book Series    
DOI: 10.1016/B978-0-12-385952-5.00001-4     Document Type: Chapter
Times cited : (55)

References (177)
  • 1
    • 77952955746 scopus 로고    scopus 로고
    • Identification and biological significance of G protein-coupled receptor associated sorting proteins (GASPs)
    • Abu-Helo A., Simonin F. Identification and biological significance of G protein-coupled receptor associated sorting proteins (GASPs). Pharmacology and Therapeutics 2010, 126:244-250.
    • (2010) Pharmacology and Therapeutics , vol.126 , pp. 244-250
    • Abu-Helo, A.1    Simonin, F.2
  • 2
    • 0033555946 scopus 로고    scopus 로고
    • Src-mediated tyrosine phosphorylation of dynamin is required for beta(2)-adrenergic receptor internalization and mitogen-activated protein kinase signaling
    • Ahn S., Maudsley S., Luttrell L.M., Lefkowitz R.J., Daaka Y. Src-mediated tyrosine phosphorylation of dynamin is required for beta(2)-adrenergic receptor internalization and mitogen-activated protein kinase signaling. The Journal of Biological Chemistry 1999, 274:1185-1188.
    • (1999) The Journal of Biological Chemistry , vol.274 , pp. 1185-1188
    • Ahn, S.1    Maudsley, S.2    Luttrell, L.M.3    Lefkowitz, R.J.4    Daaka, Y.5
  • 3
    • 0035815417 scopus 로고    scopus 로고
    • PKC phosphorylation of a conserved serine residue in the C-terminus of group III metabotropic glutamate receptors inhibits calmodulin binding
    • Airas J.M., Betz H., El Far O. PKC phosphorylation of a conserved serine residue in the C-terminus of group III metabotropic glutamate receptors inhibits calmodulin binding. FEBS Letters 2001, 494:60-63.
    • (2001) FEBS Letters , vol.494 , pp. 60-63
    • Airas, J.M.1    Betz, H.2    El Far, O.3
  • 4
    • 77951731676 scopus 로고    scopus 로고
    • Regulation of G-protein coupled receptor traffic by an evolutionary conserved hydrophobic signal
    • Angelotti T., Daunt D., Shcherbakova O.G., Kobilka B., Hurt C.M. Regulation of G-protein coupled receptor traffic by an evolutionary conserved hydrophobic signal. Traffic 2010, 11:560-578.
    • (2010) Traffic , vol.11 , pp. 560-578
    • Angelotti, T.1    Daunt, D.2    Shcherbakova, O.G.3    Kobilka, B.4    Hurt, C.M.5
  • 7
    • 0035860795 scopus 로고    scopus 로고
    • Interaction of the calcium-sensing receptor and filamin, a potential scaffolding protein
    • Awata H., Huang C., Handlogten M.E., Miller R.T. Interaction of the calcium-sensing receptor and filamin, a potential scaffolding protein. The Journal of Biological Chemistry 2001, 276:34871-34879.
    • (2001) The Journal of Biological Chemistry , vol.276 , pp. 34871-34879
    • Awata, H.1    Huang, C.2    Handlogten, M.E.3    Miller, R.T.4
  • 8
    • 74049099496 scopus 로고    scopus 로고
    • Protein disulfide isomerase chaperone ERP-57 decreases plasma membrane expression of the human GnRH receptor
    • Ayala Yanez R., Conn P.M. Protein disulfide isomerase chaperone ERP-57 decreases plasma membrane expression of the human GnRH receptor. Cell Biochemistry and Function 2010, 28:66-73.
    • (2010) Cell Biochemistry and Function , vol.28 , pp. 66-73
    • Ayala Yanez, R.1    Conn, P.M.2
  • 9
    • 34247511554 scopus 로고    scopus 로고
    • Real-time analysis of agonist-induced activation of protease-activated receptor 1/Galphai1 protein complex measured by bioluminescence resonance energy transfer in living cells
    • Ayoub M.A., Maurel D., Binet V., Fink M., Prezeau L., Ansanay H., Pin J.P. Real-time analysis of agonist-induced activation of protease-activated receptor 1/Galphai1 protein complex measured by bioluminescence resonance energy transfer in living cells. Molecular Pharmacology 2007, 71:1329-1340.
    • (2007) Molecular Pharmacology , vol.71 , pp. 1329-1340
    • Ayoub, M.A.1    Maurel, D.2    Binet, V.3    Fink, M.4    Prezeau, L.5    Ansanay, H.6    Pin, J.P.7
  • 10
    • 15044353649 scopus 로고    scopus 로고
    • Arrestin times for compartmentalised cAMP signalling and phosphodiesterase-4 enzymes
    • Baillie G.S., Houslay M.D. Arrestin times for compartmentalised cAMP signalling and phosphodiesterase-4 enzymes. Current Opinion in Cell Biology 2005, 17:129-134.
    • (2005) Current Opinion in Cell Biology , vol.17 , pp. 129-134
    • Baillie, G.S.1    Houslay, M.D.2
  • 13
    • 0028143610 scopus 로고
    • The cyclophilin homolog NinaA functions as a chaperone, forming a stable complex in vivo with its protein target rhodopsin
    • Baker E.K., Colley N.J., Zuker C.S. The cyclophilin homolog NinaA functions as a chaperone, forming a stable complex in vivo with its protein target rhodopsin. The EMBO Journal 1994, 13:4886-4895.
    • (1994) The EMBO Journal , vol.13 , pp. 4886-4895
    • Baker, E.K.1    Colley, N.J.2    Zuker, C.S.3
  • 14
    • 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, 282:4162-4171.
    • (2007) The Journal of Biological Chemistry , vol.282 , pp. 4162-4171
    • Balasubramanian, S.1    Fam, S.R.2    Hall, R.A.3
  • 18
    • 0035011489 scopus 로고    scopus 로고
    • Regulation of transport of the dopamine D1 receptor by a new membrane-associated ER protein
    • Bermak J.C., Li M., Bullock C., Zhou Q.Y. Regulation of transport of the dopamine D1 receptor by a new membrane-associated ER protein. Nature Cell Biology 2001, 3:492-498.
    • (2001) Nature Cell Biology , vol.3 , pp. 492-498
    • Bermak, J.C.1    Li, M.2    Bullock, C.3    Zhou, Q.Y.4
  • 19
    • 2442717874 scopus 로고    scopus 로고
    • RGS2 binds directly and selectively to the M1 muscarinic acetylcholine receptor third intracellular loop to modulate Gq/11alpha signaling
    • Bernstein L.S., Ramineni S., Hague C., Cladman W., Chidiac P., Levey A.I., Hepler J.R. RGS2 binds directly and selectively to the M1 muscarinic acetylcholine receptor third intracellular loop to modulate Gq/11alpha signaling. The Journal of Biological Chemistry 2004, 279:21248-21256.
    • (2004) The Journal of Biological Chemistry , vol.279 , pp. 21248-21256
    • Bernstein, L.S.1    Ramineni, S.2    Hague, C.3    Cladman, W.4    Chidiac, P.5    Levey, A.I.6    Hepler, J.R.7
  • 22
    • 0036765857 scopus 로고    scopus 로고
    • D2 and D3 dopamine receptor cell surface localization mediated by interaction with protein 4.1N
    • Binda A.V., Kabbani N., Lin R., Levenson R. D2 and D3 dopamine receptor cell surface localization mediated by interaction with protein 4.1N. Molecular Pharmacology 2002, 62:507-513.
    • (2002) Molecular Pharmacology , vol.62 , pp. 507-513
    • Binda, A.V.1    Kabbani, N.2    Lin, R.3    Levenson, R.4
  • 26
    • 0034692687 scopus 로고    scopus 로고
    • Binding of calmodulin to the D-2-dopamine receptor reduces receptor signaling by arresting the G protein activation switch
    • Bofill-Cardona E., Kudlacek O., Yang Q., Ahorn H., Freissmuth M., Nanoff C. Binding of calmodulin to the D-2-dopamine receptor reduces receptor signaling by arresting the G protein activation switch. The Journal of Biological Chemistry 2000, 275:32672-32680.
    • (2000) The Journal of Biological Chemistry , vol.275 , pp. 32672-32680
    • Bofill-Cardona, E.1    Kudlacek, O.2    Yang, Q.3    Ahorn, H.4    Freissmuth, M.5    Nanoff, C.6
  • 29
    • 27844496106 scopus 로고    scopus 로고
    • Receptor-activity-modifying proteins are required for forward trafficking of the calcium-sensing receptor to the plasma membrane
    • Bouschet T., Martin S., Henley J.M. Receptor-activity-modifying proteins are required for forward trafficking of the calcium-sensing receptor to the plasma membrane. Journal of Cell Science 2005, 118:4709-4720.
    • (2005) Journal of Cell Science , vol.118 , pp. 4709-4720
    • Bouschet, T.1    Martin, S.2    Henley, J.M.3
  • 31
    • 78649740904 scopus 로고    scopus 로고
    • Combining resonance energy transfer methods reveals a complex between the {alpha}2A-adrenergic receptor, G{alpha}i1{beta}1{gamma}2, and GRK2
    • Breton B., Lagace M., Bouvier M. Combining resonance energy transfer methods reveals a complex between the {alpha}2A-adrenergic receptor, G{alpha}i1{beta}1{gamma}2, and GRK2. The FASEB Journal 2010.
    • (2010) The FASEB Journal
    • Breton, B.1    Lagace, M.2    Bouvier, M.3
  • 32
    • 14644387575 scopus 로고    scopus 로고
    • Emerging role of homo- and heterodimerization in G-protein-coupled receptor biosynthesis and maturation
    • Bulenger S., Marullo S., Bouvier M. Emerging role of homo- and heterodimerization in G-protein-coupled receptor biosynthesis and maturation. Trends in Pharmacological Sciences 2005, 26:131-137.
    • (2005) Trends in Pharmacological Sciences , vol.26 , pp. 131-137
    • Bulenger, S.1    Marullo, S.2    Bouvier, M.3
  • 34
    • 79953141982 scopus 로고    scopus 로고
    • AKAP-LBC anchors a PKN-based signaling complex involved in alpha1-adrenergic receptor-induced p38 activation
    • Cariolato L., Cavin S., Diviani D. AKAP-LBC anchors a PKN-based signaling complex involved in alpha1-adrenergic receptor-induced p38 activation. The Journal of Biological Chemistry 2011, 286:7925-7937.
    • (2011) The Journal of Biological Chemistry , vol.286 , pp. 7925-7937
    • Cariolato, L.1    Cavin, S.2    Diviani, D.3
  • 35
    • 0038819926 scopus 로고    scopus 로고
    • The chaperone environment at the cytoplasmic face of the endoplasmic reticulum can modulate rhodopsin processing and inclusion formation
    • Chapple J.P., Cheetham M.E. The chaperone environment at the cytoplasmic face of the endoplasmic reticulum can modulate rhodopsin processing and inclusion formation. The Journal of Biological Chemistry 2003, 278:19087-19094.
    • (2003) The Journal of Biological Chemistry , vol.278 , pp. 19087-19094
    • Chapple, J.P.1    Cheetham, M.E.2
  • 38
    • 70349255916 scopus 로고    scopus 로고
    • PI3K/Akt signalling-mediated protein surface expression sensed by 14-3-3 interacting motif
    • Chung J.J., Okamoto Y., Coblitz B., Li M., Qiu Y., Shikano S. PI3K/Akt signalling-mediated protein surface expression sensed by 14-3-3 interacting motif. The FEBS Journal 2009, 276:5547-5558.
    • (2009) The FEBS Journal , vol.276 , pp. 5547-5558
    • Chung, J.J.1    Okamoto, Y.2    Coblitz, B.3    Li, M.4    Qiu, Y.5    Shikano, S.6
  • 40
    • 0030613761 scopus 로고    scopus 로고
    • Switching of the coupling of the beta2-adrenergic receptor to different G proteins by protein kinase A
    • Daaka Y., Luttrell L.M., Lefkowitz R.J. Switching of the coupling of the beta2-adrenergic receptor to different G proteins by protein kinase A. Nature 1997, 390:88-91.
    • (1997) Nature , vol.390 , pp. 88-91
    • Daaka, Y.1    Luttrell, L.M.2    Lefkowitz, R.J.3
  • 42
    • 59549102113 scopus 로고    scopus 로고
    • Recent methodological advances in the discovery of GPCR-associated protein complexes
    • Daulat A.M., Maurice P., Jockers R. Recent methodological advances in the discovery of GPCR-associated protein complexes. Trends in Pharmacological Sciences 2009, 30:72-78.
    • (2009) Trends in Pharmacological Sciences , vol.30 , pp. 72-78
    • Daulat, A.M.1    Maurice, P.2    Jockers, R.3
  • 45
    • 40349108549 scopus 로고    scopus 로고
    • Beta-arrestins and heterotrimeric G-proteins: Collaborators and competitors in signal transduction
    • Defea K. Beta-arrestins and heterotrimeric G-proteins: Collaborators and competitors in signal transduction. British Journal of Pharmacology 2008, 153(Suppl. 1):S298-S309.
    • (2008) British Journal of Pharmacology , vol.153 , Issue.SUPPL. 1
    • Defea, K.1
  • 47
    • 38349025530 scopus 로고    scopus 로고
    • Plectin regulates the signaling and trafficking of the HIV-1 co-receptor CXCR4 and plays a role in HIV-1 infection
    • Ding Y., Zhang L., Goodwin J.S., Wang Z., Liu B., Zhang J., Fan G.H. Plectin regulates the signaling and trafficking of the HIV-1 co-receptor CXCR4 and plays a role in HIV-1 infection. Experimental Cell Research 2008, 314:590-602.
    • (2008) Experimental Cell Research , vol.314 , pp. 590-602
    • Ding, Y.1    Zhang, L.2    Goodwin, J.S.3    Wang, Z.4    Liu, B.5    Zhang, J.6    Fan, G.H.7
  • 48
    • 0027537009 scopus 로고
    • Mechanochemistry of the alternatively spliced spectrin-actin binding domain in membrane skeletal protein 4.1
    • Discher D., Parra M., Conboy J.G., Mohandas N. Mechanochemistry of the alternatively spliced spectrin-actin binding domain in membrane skeletal protein 4.1. The Journal of Biological Chemistry 1993, 268:7186-7195.
    • (1993) The Journal of Biological Chemistry , vol.268 , pp. 7186-7195
    • Discher, D.1    Parra, M.2    Conboy, J.G.3    Mohandas, N.4
  • 49
    • 71949124790 scopus 로고    scopus 로고
    • Olfactory receptor signaling is regulated by the post-synaptic density 95, Drosophila discs large, zona-occludens 1 (PDZ) scaffold multi-PDZ domain protein 1
    • Dooley R., Baumgart S., Rasche S., Hatt H., Neuhaus E.M. Olfactory receptor signaling is regulated by the post-synaptic density 95, Drosophila discs large, zona-occludens 1 (PDZ) scaffold multi-PDZ domain protein 1. The FEBS Journal 2009, 276:7279-7290.
    • (2009) The FEBS Journal , vol.276 , pp. 7279-7290
    • Dooley, R.1    Baumgart, S.2    Rasche, S.3    Hatt, H.4    Neuhaus, E.M.5
  • 50
    • 68749105852 scopus 로고    scopus 로고
    • Enhancement of the surface expression of G protein-coupled receptors
    • Dunham J.H., Hall R.A. Enhancement of the surface expression of G protein-coupled receptors. Trends in Biotechnology 2009, 27:541-545.
    • (2009) Trends in Biotechnology , vol.27 , pp. 541-545
    • Dunham, J.H.1    Hall, R.A.2
  • 51
    • 33747120931 scopus 로고    scopus 로고
    • Biosynthesis and trafficking of seven transmembrane receptor signalling complexes
    • Dupre D.J., Hebert T.E. Biosynthesis and trafficking of seven transmembrane receptor signalling complexes. Cellular Signalling 2006, 18:1549-1559.
    • (2006) Cellular Signalling , vol.18 , pp. 1549-1559
    • Dupre, D.J.1    Hebert, T.E.2
  • 53
    • 0034517551 scopus 로고    scopus 로고
    • Interaction of the C-terminal tail region of the metabotropic glutamate receptor 7 with the protein kinase C substrate PICK1
    • El Far O., Airas J., Wischmeyer E., Nehring R.B., Karschin A., Betz H. Interaction of the C-terminal tail region of the metabotropic glutamate receptor 7 with the protein kinase C substrate PICK1. The European Journal of Neuroscience 2000, 12:4215-4221.
    • (2000) The European Journal of Neuroscience , vol.12 , pp. 4215-4221
    • El Far, O.1    Airas, J.2    Wischmeyer, E.3    Nehring, R.B.4    Karschin, A.5    Betz, H.6
  • 54
    • 0037070641 scopus 로고    scopus 로고
    • The actin-binding protein Filamin-A interacts with the metabotropic glutamate receptor type 7
    • Enz R. The actin-binding protein Filamin-A interacts with the metabotropic glutamate receptor type 7. FEBS Letters 2002, 514:184-188.
    • (2002) FEBS Letters , vol.514 , pp. 184-188
    • Enz, R.1
  • 55
    • 78651295086 scopus 로고    scopus 로고
    • Rab GTPases bind at a common site within the angiotensin II type I receptor carboxyl-terminal tail: Evidence that Rab4 regulates receptor phosphorylation, desensitization, and resensitization
    • Esseltine J.L., Dale L.B., Ferguson S.S. Rab GTPases bind at a common site within the angiotensin II type I receptor carboxyl-terminal tail: Evidence that Rab4 regulates receptor phosphorylation, desensitization, and resensitization. Molecular Pharmacology 2011, 79:175-184.
    • (2011) Molecular Pharmacology , vol.79 , pp. 175-184
    • Esseltine, J.L.1    Dale, L.B.2    Ferguson, S.S.3
  • 57
    • 0035918269 scopus 로고    scopus 로고
    • C-Src tyrosine kinase binds the beta 2-adrenergic receptor via phospho-Tyr-350, phosphorylates G-protein-linked receptor kinase 2, and mediates agonist-induced receptor desensitization
    • Fan G., Shumay E., Malbon C.C., Wang H. c-Src tyrosine kinase binds the beta 2-adrenergic receptor via phospho-Tyr-350, phosphorylates G-protein-linked receptor kinase 2, and mediates agonist-induced receptor desensitization. The Journal of Biological Chemistry 2001, 276:13240-13247.
    • (2001) The Journal of Biological Chemistry , vol.276 , pp. 13240-13247
    • Fan, G.1    Shumay, E.2    Malbon, C.C.3    Wang, H.4
  • 58
    • 0035968196 scopus 로고    scopus 로고
    • The scaffold protein gravin (cAMP-dependent protein kinase-anchoring protein 250) binds the beta(2)-adrenergic receptor via the receptor cytoplasmic Arg-329 to Leu-413 domain and provides a mobile scaffold during desensitization
    • Fan G.F., Shumay E., Wang H.Y., Malbon C.C. The scaffold protein gravin (cAMP-dependent protein kinase-anchoring protein 250) binds the beta(2)-adrenergic receptor via the receptor cytoplasmic Arg-329 to Leu-413 domain and provides a mobile scaffold during desensitization. The Journal of Biological Chemistry 2001, 276:24005-24014.
    • (2001) The Journal of Biological Chemistry , vol.276 , pp. 24005-24014
    • Fan, G.F.1    Shumay, E.2    Wang, H.Y.3    Malbon, C.C.4
  • 59
    • 0042357127 scopus 로고    scopus 로고
    • Selective interactions between helix VIII of the human mu-opioid receptors and the C terminus of periplakin disrupt G protein activation
    • Feng G.J., Kellett E., Scorer C.A., Wilde J., White J.H., Milligan G. Selective interactions between helix VIII of the human mu-opioid receptors and the C terminus of periplakin disrupt G protein activation. The Journal of Biological Chemistry 2003, 278:33400-33407.
    • (2003) The Journal of Biological Chemistry , vol.278 , pp. 33400-33407
    • Feng, G.J.1    Kellett, E.2    Scorer, C.A.3    Wilde, J.4    White, J.H.5    Milligan, G.6
  • 60
    • 0029859847 scopus 로고    scopus 로고
    • Cyclophilin-related protein RanBP2 acts as chaperone for red/green opsin
    • Ferreira P.A., Nakayama T.A., Pak W.L., Travis G.H. Cyclophilin-related protein RanBP2 acts as chaperone for red/green opsin. Nature 1996, 383:637-640.
    • (1996) Nature , vol.383 , pp. 637-640
    • Ferreira, P.A.1    Nakayama, T.A.2    Pak, W.L.3    Travis, G.H.4
  • 61
    • 33845955161 scopus 로고    scopus 로고
    • Interaction of neurochondrin with the melanin-concentrating hormone receptor 1 interferes with G protein-coupled signal transduction but not agonist-mediated internalization
    • Francke F., Ward R.J., Jenkins L., Kellett E., Richter D., Milligan G., Bachner D. Interaction of neurochondrin with the melanin-concentrating hormone receptor 1 interferes with G protein-coupled signal transduction but not agonist-mediated internalization. The Journal of Biological Chemistry 2006, 281:32496-32507.
    • (2006) The Journal of Biological Chemistry , vol.281 , pp. 32496-32507
    • Francke, F.1    Ward, R.J.2    Jenkins, L.3    Kellett, E.4    Richter, D.5    Milligan, G.6    Bachner, D.7
  • 62
    • 0034611757 scopus 로고    scopus 로고
    • Assembly of an A kinase-anchoring protein-2-adrenergic receptor complex facilitates receptor phosphorylation and signaling
    • Fraser I.D.C., Cong M., Kim J., Rollins E.N., Daaka Y., Lefkowitz R.J., Scott J.D. Assembly of an A kinase-anchoring protein-2-adrenergic receptor complex facilitates receptor phosphorylation and signaling. Current Biology 2000, 10:409-412.
    • (2000) Current Biology , vol.10 , pp. 409-412
    • Fraser, I.D.C.1    Cong, M.2    Kim, J.3    Rollins, E.N.4    Daaka, Y.5    Lefkowitz, R.J.6    Scott, J.D.7
  • 63
    • 13544253361 scopus 로고    scopus 로고
    • Type I PDZ ligands are sufficient to promote rapid recycling of G protein-coupled receptors independent of binding to N-ethylmaleimide-sensitive factor
    • Gage R.M., Matveeva E.A., Whiteheart S.W., von Zastrow M. Type I PDZ ligands are sufficient to promote rapid recycling of G protein-coupled receptors independent of binding to N-ethylmaleimide-sensitive factor. The Journal of Biological Chemistry 2005, 280:3305-3313.
    • (2005) The Journal of Biological Chemistry , vol.280 , pp. 3305-3313
    • Gage, R.M.1    Matveeva, E.A.2    Whiteheart, S.W.3    von Zastrow, M.4
  • 65
    • 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., Bockaert J., Marin P. Opposite effects of PSD-95 and MPP3 PDZ proteins on serotonin 5-hydroxytryptamine2C receptor desensitization and membrane stability. Molecular Biology of the Cell 2006, 17:4619-4631.
    • (2006) Molecular Biology of the Cell , vol.17 , pp. 4619-4631
    • Gavarini, S.1    Becamel, C.2    Altier, C.3    Lory, P.4    Poncet, J.5    Wijnholds, J.6    Bockaert, J.7    Marin, P.8
  • 66
    • 66849091680 scopus 로고    scopus 로고
    • Mu-Opioid receptor cell surface expression is regulated by its direct interaction with Ribophorin I
    • Ge X., Loh H.H., Law P.Y. mu-Opioid receptor cell surface expression is regulated by its direct interaction with Ribophorin I. Molecular Pharmacology 2009, 75:1307-1316.
    • (2009) Molecular Pharmacology , vol.75 , pp. 1307-1316
    • Ge, X.1    Loh, H.H.2    Law, P.Y.3
  • 68
    • 32244436712 scopus 로고    scopus 로고
    • Selective interactions between G protein subunits and RGS4 with the C-terminal domains of the mu- and delta-opioid receptors regulate opioid receptor signaling
    • Georgoussi Z., Leontiadis L., Mazarakou G., Merkouris M., Hyde K., Hamm H. Selective interactions between G protein subunits and RGS4 with the C-terminal domains of the mu- and delta-opioid receptors regulate opioid receptor signaling. Cellular Signalling 2006, 18:771-782.
    • (2006) Cellular Signalling , vol.18 , pp. 771-782
    • Georgoussi, Z.1    Leontiadis, L.2    Mazarakou, G.3    Merkouris, M.4    Hyde, K.5    Hamm, H.6
  • 70
    • 22844433094 scopus 로고    scopus 로고
    • Selective inhibition of alpha1A-adrenergic receptor signaling by RGS2 association with the receptor third intracellular loop
    • Hague C., Bernstein L.S., Ramineni S., Chen Z., Minneman K.P., Hepler J.R. Selective inhibition of alpha1A-adrenergic receptor signaling by RGS2 association with the receptor third intracellular loop. The Journal of Biological Chemistry 2005, 280:27289-27295.
    • (2005) The Journal of Biological Chemistry , vol.280 , pp. 27289-27295
    • Hague, C.1    Bernstein, L.S.2    Ramineni, S.3    Chen, Z.4    Minneman, K.P.5    Hepler, J.R.6
  • 72
    • 77956894271 scopus 로고    scopus 로고
    • Chaperones contribute to G protein coupled receptor oligomerization, but do not participate in assembly of the G protein with the receptor signaling complex
    • Hammad M.M., Dupre D.J. Chaperones contribute to G protein coupled receptor oligomerization, but do not participate in assembly of the G protein with the receptor signaling complex. Journal of Molecular Signaling 2010, 5:16.
    • (2010) Journal of Molecular Signaling , vol.5 , pp. 16
    • Hammad, M.M.1    Dupre, D.J.2
  • 73
    • 78049383086 scopus 로고    scopus 로고
    • Na+/H+ exchanger regulatory factor-1 is involved in chemokine receptor homodimer CCR5 internalization and signal transduction but does not affect CXCR4 homodimer or CXCR4-CCR5 heterodimer
    • Hammad M.M., Kuang Y.Q., Yan R., Allen H., Dupre D.J. Na+/H+ exchanger regulatory factor-1 is involved in chemokine receptor homodimer CCR5 internalization and signal transduction but does not affect CXCR4 homodimer or CXCR4-CCR5 heterodimer. The Journal of Biological Chemistry 2010, 285:34653-34664.
    • (2010) The Journal of Biological Chemistry , vol.285 , pp. 34653-34664
    • Hammad, M.M.1    Kuang, Y.Q.2    Yan, R.3    Allen, H.4    Dupre, D.J.5
  • 75
    • 0035860748 scopus 로고    scopus 로고
    • Filamin-A binds to the carboxyl-terminal tail of the calcium-sensing receptor, an interaction that participates in CaR-mediated activation of mitogen-activated protein kinase
    • Hjalm G., MacLeod R.J., Kifor O., Chattopadhyay N., Brown E.M. Filamin-A binds to the carboxyl-terminal tail of the calcium-sensing receptor, an interaction that participates in CaR-mediated activation of mitogen-activated protein kinase. The Journal of Biological Chemistry 2001, 276:34880-34887.
    • (2001) The Journal of Biological Chemistry , vol.276 , pp. 34880-34887
    • Hjalm, G.1    MacLeod, R.J.2    Kifor, O.3    Chattopadhyay, N.4    Brown, E.M.5
  • 76
    • 0034623942 scopus 로고    scopus 로고
    • Beta 1-adrenergic receptor association with PSD-95-Inhibition of receptor internalization and facilitation of beta(1)-adrenergic receptor interaction with N-methyl-d-aspartate receptors
    • Hu L.Y.A., Tang Y.T., Miller W.E., Cong M., Lau A.G., Lefkowitz R.J., Hall R.A. Beta 1-adrenergic receptor association with PSD-95-Inhibition of receptor internalization and facilitation of beta(1)-adrenergic receptor interaction with N-methyl-d-aspartate receptors. The Journal of Biological Chemistry 2000, 275:38659-38666.
    • (2000) The Journal of Biological Chemistry , vol.275 , pp. 38659-38666
    • Hu, L.Y.A.1    Tang, Y.T.2    Miller, W.E.3    Cong, M.4    Lau, A.G.5    Lefkowitz, R.J.6    Hall, R.A.7
  • 80
    • 0005169503 scopus 로고    scopus 로고
    • GABAb receptors function as a heterotrimeric assembly of the subunits GABAbR1 and GAGbR2
    • Jones K.A., Borowsky B., Tamm J.A., Gerald C. GABAb receptors function as a heterotrimeric assembly of the subunits GABAbR1 and GAGbR2. Nature 1998, 396:674-679.
    • (1998) Nature , vol.396 , pp. 674-679
    • Jones, K.A.1    Borowsky, B.2    Tamm, J.A.3    Gerald, C.4
  • 81
    • 0037101632 scopus 로고    scopus 로고
    • Neurofilament-M interacts with the D1 dopamine receptor to regulate cell surface expression and desensitization
    • Kim O.J., Ariano M.A., Lazzarini R.A., Levine M.S., Sibley D.R. Neurofilament-M interacts with the D1 dopamine receptor to regulate cell surface expression and desensitization. The Journal of Neuroscience 2002, 22:5920-5930.
    • (2002) The Journal of Neuroscience , vol.22 , pp. 5920-5930
    • Kim, O.J.1    Ariano, M.A.2    Lazzarini, R.A.3    Levine, M.S.4    Sibley, D.R.5
  • 82
    • 16844377622 scopus 로고    scopus 로고
    • G protein-coupled receptor kinase regulates dopamine D3 receptor signaling by modulating the stability of a receptor-filamin-beta-arrestin complex. A case of autoreceptor regulation
    • Kim K.M., Gainetdinov R.R., Laporte S.A., Caron M.G., Barak L.S. G protein-coupled receptor kinase regulates dopamine D3 receptor signaling by modulating the stability of a receptor-filamin-beta-arrestin complex. A case of autoreceptor regulation. The Journal of Biological Chemistry 2005, 280:12774-12780.
    • (2005) The Journal of Biological Chemistry , vol.280 , pp. 12774-12780
    • Kim, K.M.1    Gainetdinov, R.R.2    Laporte, S.A.3    Caron, M.G.4    Barak, L.S.5
  • 84
    • 73649098238 scopus 로고    scopus 로고
    • Molecular mechanisms of rhodopsin retinitis pigmentosa and the efficacy of pharmacological rescue
    • Krebs M.P., Holden D.C., Joshi P., Clark C.L., Lee A.H., Kaushal S. Molecular mechanisms of rhodopsin retinitis pigmentosa and the efficacy of pharmacological rescue. Journal of Molecular Biology 2010, 395:1063-1078.
    • (2010) Journal of Molecular Biology , vol.395 , pp. 1063-1078
    • Krebs, M.P.1    Holden, D.C.2    Joshi, P.3    Clark, C.L.4    Lee, A.H.5    Kaushal, S.6
  • 85
    • 69549130897 scopus 로고    scopus 로고
    • Effects of spinophilin on the function of RGS8 regulating signals from M2 and M3-mAChRs
    • Kurogi M., Nagatomo K., Kubo Y., Saitoh O. Effects of spinophilin on the function of RGS8 regulating signals from M2 and M3-mAChRs. NeuroReport 2009, 20:1134-1139.
    • (2009) NeuroReport , vol.20 , pp. 1134-1139
    • Kurogi, M.1    Nagatomo, K.2    Kubo, Y.3    Saitoh, O.4
  • 86
    • 58149306364 scopus 로고    scopus 로고
    • Physical interaction of calmodulin with the 5-HT2C receptor C-terminus is essential for G protein-independent, arrestin-dependent, receptor signaling
    • Labasque M., Reiter E., Becamel C., Bockaert J., Marin P. Physical interaction of calmodulin with the 5-HT2C receptor C-terminus is essential for G protein-independent, arrestin-dependent, receptor signaling. Molecular Biology of the Cell 2008, 19:4640-4650.
    • (2008) Molecular Biology of the Cell , vol.19 , pp. 4640-4650
    • Labasque, M.1    Reiter, E.2    Becamel, C.3    Bockaert, J.4    Marin, P.5
  • 87
    • 62149122981 scopus 로고    scopus 로고
    • Evidence for a direct and functional interaction between the regulators of G protein signaling-2 and phosphorylated C terminus of cholecystokinin-2 receptor
    • Langer I., Tikhonova I.G., Boulegue C., Esteve J.P., Vatinel S., Ferrand A., Moroder L., Robberecht P., Fourmy D. Evidence for a direct and functional interaction between the regulators of G protein signaling-2 and phosphorylated C terminus of cholecystokinin-2 receptor. Molecular Pharmacology 2009, 75:502-513.
    • (2009) Molecular Pharmacology , vol.75 , pp. 502-513
    • Langer, I.1    Tikhonova, I.G.2    Boulegue, C.3    Esteve, J.P.4    Vatinel, S.5    Ferrand, A.6    Moroder, L.7    Robberecht, P.8    Fourmy, D.9
  • 88
    • 0036892937 scopus 로고    scopus 로고
    • A polyaromatic caveolin-binding-like motif in the cytoplasmic tail of the type 1 receptor for angiotensin II plays an important role in receptor trafficking and signaling
    • Leclerc P.C., Auger-Messier M., Lanctot P.M., Escher E., Leduc R., Guillemette G. A polyaromatic caveolin-binding-like motif in the cytoplasmic tail of the type 1 receptor for angiotensin II plays an important role in receptor trafficking and signaling. Endocrinology 2002, 143:4702-4710.
    • (2002) Endocrinology , vol.143 , pp. 4702-4710
    • Leclerc, P.C.1    Auger-Messier, M.2    Lanctot, P.M.3    Escher, E.4    Leduc, R.5    Guillemette, G.6
  • 89
    • 34247234971 scopus 로고    scopus 로고
    • Dopamine transporter cell surface localization facilitated by a direct interaction with the dopamine D2 receptor
    • Lee F.J., Pei L., Moszczynska A., Vukusic B., Fletcher P.J., Liu F. Dopamine transporter cell surface localization facilitated by a direct interaction with the dopamine D2 receptor. The EMBO Journal 2007, 26:2127-2136.
    • (2007) The EMBO Journal , vol.26 , pp. 2127-2136
    • Lee, F.J.1    Pei, L.2    Moszczynska, A.3    Vukusic, B.4    Fletcher, P.J.5    Liu, F.6
  • 90
    • 79952292419 scopus 로고    scopus 로고
    • MAGI-3 competes with NHERF-2 to negatively regulate LPA(2) receptor signaling in colon cancer cells
    • 140, 924-934
    • 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, 924-934.
    • (2011) Gastroenterology
    • Lee, S.J.1    Ritter, S.L.2    Zhang, H.3    Shim, H.4    Hall, R.A.5    Yun, C.C.6
  • 91
    • 17644402459 scopus 로고    scopus 로고
    • Transduction of receptor signals by beta-arrestins
    • Lefkowitz R.J., Shenoy S.K. Transduction of receptor signals by beta-arrestins. Science 2005, 308:512-517.
    • (2005) Science , vol.308 , pp. 512-517
    • Lefkowitz, R.J.1    Shenoy, S.K.2
  • 92
    • 64849105251 scopus 로고    scopus 로고
    • Regulator of G protein signaling 4 confers selectivity to specific G proteins to modulate mu- and delta-opioid receptor signaling
    • Leontiadis L.J., Papakonstantinou M.P., Georgoussi Z. Regulator of G protein signaling 4 confers selectivity to specific G proteins to modulate mu- and delta-opioid receptor signaling. Cellular Signalling 2009, 21:1218-1228.
    • (2009) Cellular Signalling , vol.21 , pp. 1218-1228
    • Leontiadis, L.J.1    Papakonstantinou, M.P.2    Georgoussi, Z.3
  • 93
    • 0034089048 scopus 로고    scopus 로고
    • Modulation of dopamine D(2) receptor signaling by actin-binding protein (ABP-280)
    • Li M., Bermak J.C., Wang Z.W., Zhou Q.Y. Modulation of dopamine D(2) receptor signaling by actin-binding protein (ABP-280). Molecular Pharmacology 2000, 57:446-452.
    • (2000) Molecular Pharmacology , vol.57 , pp. 446-452
    • Li, M.1    Bermak, J.C.2    Wang, Z.W.3    Zhou, Q.Y.4
  • 97
    • 47949115718 scopus 로고    scopus 로고
    • Novel interaction of the dopamine D2 receptor and the Ca2+ binding protein S100B: Role in D2 receptor function
    • Liu Y., Buck D.C., Neve K.A. Novel interaction of the dopamine D2 receptor and the Ca2+ binding protein S100B: Role in D2 receptor function. Molecular Pharmacology 2008, 74:371-378.
    • (2008) Molecular Pharmacology , vol.74 , pp. 371-378
    • Liu, Y.1    Buck, D.C.2    Neve, K.A.3
  • 98
    • 0034688225 scopus 로고    scopus 로고
    • Direct protein-protein coupling enables cross-talk between dopamine D5 and gamma-aminobutyric acid A receptors
    • Liu F., Wan Q., Pristupa Z.B., Yu X.M., Wang Y.T., Niznik H.B. Direct protein-protein coupling enables cross-talk between dopamine D5 and gamma-aminobutyric acid A receptors. Nature 2000, 403:274-280.
    • (2000) Nature , vol.403 , pp. 274-280
    • Liu, F.1    Wan, Q.2    Pristupa, Z.B.3    Yu, X.M.4    Wang, Y.T.5    Niznik, H.B.6
  • 99
    • 4644308500 scopus 로고    scopus 로고
    • Cytoskeletal protein 4.1G is a binding partner of the metabotropic glutamate receptor subtype 1 alpha
    • Lu D., Yan H., Othman T., Rivkees S.A. Cytoskeletal protein 4.1G is a binding partner of the metabotropic glutamate receptor subtype 1 alpha. Journal of Neuroscience Research 2004, 78:49-55.
    • (2004) Journal of Neuroscience Research , vol.78 , pp. 49-55
    • Lu, D.1    Yan, H.2    Othman, T.3    Rivkees, S.A.4
  • 100
    • 35648992037 scopus 로고    scopus 로고
    • P24A, a type I transmembrane protein, controls ARF1-dependent resensitization of protease-activated receptor-2 by influence on receptor trafficking
    • Luo W., Wang Y., Reiser G. p24A, a type I transmembrane protein, controls ARF1-dependent resensitization of protease-activated receptor-2 by influence on receptor trafficking. The Journal of Biological Chemistry 2007, 282:30246-30255.
    • (2007) The Journal of Biological Chemistry , vol.282 , pp. 30246-30255
    • Luo, W.1    Wang, Y.2    Reiser, G.3
  • 101
    • 79952541443 scopus 로고    scopus 로고
    • Proteinase-activated receptors, nucleotide P2Y receptors, and mu-opioid receptor-1B are under the control of the type I transmembrane proteins p23 and p24A in post-Golgi trafficking
    • 117, 71-81
    • Luo W., Wang Y., Reiser G. Proteinase-activated receptors, nucleotide P2Y receptors, and mu-opioid receptor-1B are under the control of the type I transmembrane proteins p23 and p24A in post-Golgi trafficking. Journal of Neurochemistry 2011, 117, 71-81.
    • (2011) Journal of Neurochemistry
    • Luo, W.1    Wang, Y.2    Reiser, G.3
  • 102
    • 23944494162 scopus 로고    scopus 로고
    • RNA silencing identifies PDE4D5 as the functionally relevant cAMP phosphodiesterase interacting with beta arrestin to control the protein kinase A/AKAP79-mediated switching of the beta2-adrenergic receptor to activation of ERK in HEK293B2 cells
    • Lynch M.J., Baillie G.S., Mohamed A., Li X., Maisonneuve C., Klussmann E., van Heeke G., Houslay M.D. RNA silencing identifies PDE4D5 as the functionally relevant cAMP phosphodiesterase interacting with beta arrestin to control the protein kinase A/AKAP79-mediated switching of the beta2-adrenergic receptor to activation of ERK in HEK293B2 cells. The Journal of Biological Chemistry 2005, 280:33178-33189.
    • (2005) The Journal of Biological Chemistry , vol.280 , pp. 33178-33189
    • Lynch, M.J.1    Baillie, G.S.2    Mohamed, A.3    Li, X.4    Maisonneuve, C.5    Klussmann, E.6    van Heeke, G.7    Houslay, M.D.8
  • 103
    • 0035824563 scopus 로고    scopus 로고
    • Agonist-promoted ubiquitination of the G protein-coupled receptor CXCR4 mediates lysosomal sorting
    • Marchese A., Benovic J.L. Agonist-promoted ubiquitination of the G protein-coupled receptor CXCR4 mediates lysosomal sorting. The Journal of Biological Chemistry 2001, 276:45509-45512.
    • (2001) The Journal of Biological Chemistry , vol.276 , pp. 45509-45512
    • Marchese, A.1    Benovic, J.L.2
  • 104
  • 109
    • 69249206623 scopus 로고    scopus 로고
    • G protein-coupled receptor hetero-dimerization: Contribution to pharmacology and function
    • Milligan G. G protein-coupled receptor hetero-dimerization: Contribution to pharmacology and function. British Journal of Pharmacology 2009, 158:5-14.
    • (2009) British Journal of Pharmacology , vol.158 , pp. 5-14
    • Milligan, G.1
  • 110
    • 46449095877 scopus 로고    scopus 로고
    • Heterotrimeric Galphaq11 co-immunoprecipitates with surface-anchored GRP78 from plasma membranes of alpha2M*-stimulated macrophages
    • Misra U.K., Pizzo S.V. Heterotrimeric Galphaq11 co-immunoprecipitates with surface-anchored GRP78 from plasma membranes of alpha2M*-stimulated macrophages. Journal of Cellular Biochemistry 2008, 104:96-104.
    • (2008) Journal of Cellular Biochemistry , vol.104 , pp. 96-104
    • Misra, U.K.1    Pizzo, S.V.2
  • 111
    • 3042788953 scopus 로고    scopus 로고
    • Intracellularly located misfolded glycoprotein hormone receptors associate with different chaperone proteins than their cognate wild-type receptors
    • Mizrachi D., Segaloff D.L. Intracellularly located misfolded glycoprotein hormone receptors associate with different chaperone proteins than their cognate wild-type receptors. Molecular Endocrinology 2004, 18:1768-1777.
    • (2004) Molecular Endocrinology , vol.18 , pp. 1768-1777
    • Mizrachi, D.1    Segaloff, D.L.2
  • 112
    • 77957682469 scopus 로고    scopus 로고
    • TULP3 bridges the IFT-A complex and membrane phosphoinositides to promote trafficking of G protein-coupled receptors into primary cilia
    • Mukhopadhyay S., Wen X., Chih B., Nelson C.D., Lane W.S., Scales S.J., Jackson P.K. TULP3 bridges the IFT-A complex and membrane phosphoinositides to promote trafficking of G protein-coupled receptors into primary cilia. Genes & Development 2010, 24:2180-2193.
    • (2010) Genes & Development , vol.24 , pp. 2180-2193
    • Mukhopadhyay, S.1    Wen, X.2    Chih, B.3    Nelson, C.D.4    Lane, W.S.5    Scales, S.J.6    Jackson, P.K.7
  • 113
    • 14844323630 scopus 로고    scopus 로고
    • Periplakin interferes with G protein activation by the melanin-concentrating hormone receptor-1 by binding to the proximal segment of the receptor C-terminal tail
    • Murdoch H., Feng G.J., Bachner D., Ormiston L., White J.H., Richter D., Milligan G. Periplakin interferes with G protein activation by the melanin-concentrating hormone receptor-1 by binding to the proximal segment of the receptor C-terminal tail. The Journal of Biological Chemistry 2005, 280:8208-8220.
    • (2005) The Journal of Biological Chemistry , vol.280 , pp. 8208-8220
    • Murdoch, H.1    Feng, G.J.2    Bachner, D.3    Ormiston, L.4    White, J.H.5    Richter, D.6    Milligan, G.7
  • 114
    • 67649321841 scopus 로고    scopus 로고
    • G protein-coupled receptor kinase-mediated phosphorylation regulates post-endocytic trafficking of the D2 dopamine receptor
    • Namkung Y., Dipace C., Javitch J.A., Sibley D.R. G protein-coupled receptor kinase-mediated phosphorylation regulates post-endocytic trafficking of the D2 dopamine receptor. The Journal of Biological Chemistry 2009, 284:15038-15051.
    • (2009) The Journal of Biological Chemistry , vol.284 , pp. 15038-15051
    • Namkung, Y.1    Dipace, C.2    Javitch, J.A.3    Sibley, D.R.4
  • 121
    • 38849121528 scopus 로고    scopus 로고
    • RACK1 regulates the cell surface expression of the G protein-coupled receptor for thromboxane A(2)
    • Parent A., Laroche G., Hamelin E., Parent J.L. RACK1 regulates the cell surface expression of the G protein-coupled receptor for thromboxane A(2). Traffic 2008, 9:394-407.
    • (2008) Traffic , vol.9 , pp. 394-407
    • Parent, A.1    Laroche, G.2    Hamelin, E.3    Parent, J.L.4
  • 122
    • 0038159541 scopus 로고    scopus 로고
    • Agonist-induced phosphorylation of the serotonin 5-HT2C receptor regulates its interaction with multiple PDZ protein 1
    • Parker L.L., Backstrom J.R., Sanders-Bush E., Shieh B.H. Agonist-induced phosphorylation of the serotonin 5-HT2C receptor regulates its interaction with multiple PDZ protein 1. The Journal of Biological Chemistry 2003, 278:21576-21583.
    • (2003) The Journal of Biological Chemistry , vol.278 , pp. 21576-21583
    • Parker, L.L.1    Backstrom, J.R.2    Sanders-Bush, E.3    Shieh, B.H.4
  • 123
    • 77952840083 scopus 로고    scopus 로고
    • The complex G protein-coupled receptor kinase 2 (GRK2) interactome unveils new physiopathological targets
    • Penela P., Murga C., Ribas C., Lafarga V., Mayor F.Jr. The complex G protein-coupled receptor kinase 2 (GRK2) interactome unveils new physiopathological targets. British Journal of Pharmacology 2010, 160:821-832.
    • (2010) British Journal of Pharmacology , vol.160 , pp. 821-832
    • Penela, P.1    Murga, C.2    Ribas, C.3    Lafarga, V.4    Mayor, F.J.5
  • 124
    • 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., Fagni L. PICK1 is required for the control of synaptic transmission by the metabotropic glutamate receptor 7. The EMBO Journal 2002, 21:2990-2999.
    • (2002) The EMBO Journal , vol.21 , pp. 2990-2999
    • Perroy, J.1    El Far, O.2    Bertaso, F.3    Pin, J.P.4    Betz, H.5    Bockaert, J.6    Fagni, L.7
  • 125
    • 0036773284 scopus 로고    scopus 로고
    • Calcium-sensing receptor activation of rho involves filamin and rho-guanine nucleotide exchange factor
    • Pi M., Spurney R.F., Tu Q., Hinson T., Quarles L.D. Calcium-sensing receptor activation of rho involves filamin and rho-guanine nucleotide exchange factor. Endocrinology 2002, 143:3830-3838.
    • (2002) Endocrinology , vol.143 , pp. 3830-3838
    • Pi, M.1    Spurney, R.F.2    Tu, Q.3    Hinson, T.4    Quarles, L.D.5
  • 126
    • 77955174990 scopus 로고    scopus 로고
    • Disrupting 5-HT(2A) receptor/PDZ protein interactions reduces hyperalgesia and enhances SSRI efficacy in neuropathic pain
    • Pichon X., Wattiez A.S., Becamel C., Ehrlich I., Bockaert J., Eschalier A., Marin P., Courteix C. Disrupting 5-HT(2A) receptor/PDZ protein interactions reduces hyperalgesia and enhances SSRI efficacy in neuropathic pain. Molecular Therapy 2010, 18:1462-1470.
    • (2010) Molecular Therapy , vol.18 , pp. 1462-1470
    • Pichon, X.1    Wattiez, A.S.2    Becamel, C.3    Ehrlich, I.4    Bockaert, J.5    Eschalier, A.6    Marin, P.7    Courteix, C.8
  • 127
    • 33947375174 scopus 로고    scopus 로고
    • Physiological roles of G protein-coupled receptor kinases and arrestins
    • Premont R.T., Gainetdinov R.R. Physiological roles of G protein-coupled receptor kinases and arrestins. Annual Review of Physiology 2007, 69:511-534.
    • (2007) Annual Review of Physiology , vol.69 , pp. 511-534
    • Premont, R.T.1    Gainetdinov, R.R.2
  • 128
    • 79251506646 scopus 로고    scopus 로고
    • Nonenzymatic rapid control of GIRK channel function by a G protein-coupled receptor kinase
    • Raveh A., Cooper A., Guy-David L., Reuveny E. Nonenzymatic rapid control of GIRK channel function by a G protein-coupled receptor kinase. Cell 2010, 143:750-760.
    • (2010) Cell , vol.143 , pp. 750-760
    • Raveh, A.1    Cooper, A.2    Guy-David, L.3    Reuveny, E.4
  • 129
    • 77953317400 scopus 로고    scopus 로고
    • Interaction of the human prostacyclin receptor with Rab11: Characterization of a novel Rab11 binding domain within alpha-helix 8 that is regulated by palmitoylation
    • Reid H.M., Mulvaney E.P., Turner E.C., Kinsella B.T. Interaction of the human prostacyclin receptor with Rab11: Characterization of a novel Rab11 binding domain within alpha-helix 8 that is regulated by palmitoylation. The Journal of Biological Chemistry 2010, 285:18709-18726.
    • (2010) The Journal of Biological Chemistry , vol.285 , pp. 18709-18726
    • Reid, H.M.1    Mulvaney, E.P.2    Turner, E.C.3    Kinsella, B.T.4
  • 130
    • 33646162635 scopus 로고    scopus 로고
    • GRKs and beta-arrestins: Roles in receptor silencing, trafficking and signaling
    • Reiter E., Lefkowitz R.J. GRKs and beta-arrestins: Roles in receptor silencing, trafficking and signaling. Trends in Endocrinology and Metabolism 2006, 17:159-165.
    • (2006) Trends in Endocrinology and Metabolism , vol.17 , pp. 159-165
    • Reiter, E.1    Lefkowitz, R.J.2
  • 131
    • 70450263435 scopus 로고    scopus 로고
    • Fine-tuning of GPCR activity by receptor-interacting proteins
    • Ritter S.L., Hall R.A. Fine-tuning of GPCR activity by receptor-interacting proteins. Nature Reviews. Molecular Cell Biology 2009, 10:819-830.
    • (2009) Nature Reviews. Molecular Cell Biology , vol.10 , pp. 819-830
    • Ritter, S.L.1    Hall, R.A.2
  • 133
    • 8844270180 scopus 로고    scopus 로고
    • RTP family members induce functional expression of mammalian odorant receptors
    • Saito H., Kubota M., Roberts R.W., Chi Q., Matsunami H. RTP family members induce functional expression of mammalian odorant receptors. Cell 2004, 119:679-691.
    • (2004) Cell , vol.119 , pp. 679-691
    • Saito, H.1    Kubota, M.2    Roberts, R.W.3    Chi, Q.4    Matsunami, H.5
  • 135
    • 67650400328 scopus 로고    scopus 로고
    • Aberrant trafficking of human melanocortin 1 receptor variants associated with red hair and skin cancer: Steady-state retention of mutant forms in the proximal golgi
    • Sanchez-Laorden B.L., Herraiz C., Valencia J.C., Hearing V.J., Jimenez-Cervantes C., Garcia-Borron J.C. Aberrant trafficking of human melanocortin 1 receptor variants associated with red hair and skin cancer: Steady-state retention of mutant forms in the proximal golgi. Journal of Cellular Physiology 2009, 220:640-654.
    • (2009) Journal of Cellular Physiology , vol.220 , pp. 640-654
    • Sanchez-Laorden, B.L.1    Herraiz, C.2    Valencia, J.C.3    Hearing, V.J.4    Jimenez-Cervantes, C.5    Garcia-Borron, J.C.6
  • 136
    • 34548176765 scopus 로고    scopus 로고
    • Integrating molecular and network biology to decode endocytosis
    • Schmid E.M., McMahon H.T. Integrating molecular and network biology to decode endocytosis. Nature 2007, 448:883-888.
    • (2007) Nature , vol.448 , pp. 883-888
    • Schmid, E.M.1    McMahon, H.T.2
  • 137
    • 0033520487 scopus 로고    scopus 로고
    • In vivo protein transduction: Delivery of a biologically active protein into the mouse
    • Schwarze S.R., Ho A., Vocero-Akbani A., Dowdy S.F. In vivo protein transduction: Delivery of a biologically active protein into the mouse. Science 1999, 285:1569-1572.
    • (1999) Science , vol.285 , pp. 1569-1572
    • Schwarze, S.R.1    Ho, A.2    Vocero-Akbani, A.3    Dowdy, S.F.4
  • 138
    • 0036479228 scopus 로고    scopus 로고
    • Recruitment of activated G protein-coupled receptors to pre-existing clathrin-coated pits in living cells
    • Scott M.G., Benmerah A., Muntaner O., Marullo S. Recruitment of activated G protein-coupled receptors to pre-existing clathrin-coated pits in living cells. The Journal of Biological Chemistry 2002, 277:3552-3559.
    • (2002) The Journal of Biological Chemistry , vol.277 , pp. 3552-3559
    • Scott, M.G.1    Benmerah, A.2    Muntaner, O.3    Marullo, S.4
  • 139
    • 0242321269 scopus 로고    scopus 로고
    • Regulation of G protein-coupled receptor endocytosis and trafficking by Rab GTPases
    • Seachrist J.L., Ferguson S.S. Regulation of G protein-coupled receptor endocytosis and trafficking by Rab GTPases. Life Sciences 2003, 74:225-235.
    • (2003) Life Sciences , vol.74 , pp. 225-235
    • Seachrist, J.L.1    Ferguson, S.S.2
  • 140
    • 34548436564 scopus 로고    scopus 로고
    • The postsynaptic architecture of excitatory synapses: A more quantitative view
    • Sheng M., Hoogenraad C.C. The postsynaptic architecture of excitatory synapses: A more quantitative view. Annual Review of Biochemistry 2007, 76:823-847.
    • (2007) Annual Review of Biochemistry , vol.76 , pp. 823-847
    • Sheng, M.1    Hoogenraad, C.C.2
  • 141
    • 0242721361 scopus 로고    scopus 로고
    • Multifaceted roles of beta-arrestins in the regulation of seven-membrane-spanning receptor trafficking and signalling
    • Shenoy S.K., Lefkowitz R.J. Multifaceted roles of beta-arrestins in the regulation of seven-membrane-spanning receptor trafficking and signalling. The Biochemical Journal 2003, 375:503-515.
    • (2003) The Biochemical Journal , vol.375 , pp. 503-515
    • Shenoy, S.K.1    Lefkowitz, R.J.2
  • 142
    • 0033554893 scopus 로고    scopus 로고
    • Dynamic complexes of beta(2)-adrenergic receptors with protein kinases and phosphatases and the role of gravin
    • Shih M.L., Lin F.B., Scott J.D., Wang H.Y., Malbon C.C. Dynamic complexes of beta(2)-adrenergic receptors with protein kinases and phosphatases and the role of gravin. The Journal of Biological Chemistry 1999, 274:1588-1595.
    • (1999) The Journal of Biological Chemistry , vol.274 , pp. 1588-1595
    • Shih, M.L.1    Lin, F.B.2    Scott, J.D.3    Wang, H.Y.4    Malbon, C.C.5
  • 143
    • 0033538487 scopus 로고    scopus 로고
    • Association of the D2 dopamine receptor third cytoplasmic loop with spinophilin, a protein phosphatase-1-interacting protein
    • Smith F.D., Oxford G.S., Milgram S.L. Association of the D2 dopamine receptor third cytoplasmic loop with spinophilin, a protein phosphatase-1-interacting protein. The Journal of Biological Chemistry 1999, 274:19894-19900.
    • (1999) The Journal of Biological Chemistry , vol.274 , pp. 19894-19900
    • Smith, F.D.1    Oxford, G.S.2    Milgram, S.L.3
  • 144
    • 77951892842 scopus 로고    scopus 로고
    • The cargo receptor p24A facilitates calcium sensing receptor maturation and stabilization in the early secretory pathway
    • Stepanchick A., Breitwieser G.E. The cargo receptor p24A facilitates calcium sensing receptor maturation and stabilization in the early secretory pathway. Biochemical and Biophysical Research Communications 2010, 395:136-140.
    • (2010) Biochemical and Biophysical Research Communications , vol.395 , pp. 136-140
    • Stepanchick, A.1    Breitwieser, G.E.2
  • 146
    • 67649105509 scopus 로고    scopus 로고
    • PSD-95 regulates D1 dopamine receptor resensitization, but not receptor-mediated Gs-protein activation
    • Sun P., Wang J., Gu W., Cheng W., Jin G.Z., Friedman E., Zheng J., Zhen X. PSD-95 regulates D1 dopamine receptor resensitization, but not receptor-mediated Gs-protein activation. Cell Research 2009, 19:612-624.
    • (2009) Cell Research , vol.19 , pp. 612-624
    • Sun, P.1    Wang, J.2    Gu, W.3    Cheng, W.4    Jin, G.Z.5    Friedman, E.6    Zheng, J.7    Zhen, X.8
  • 147
    • 0033603239 scopus 로고    scopus 로고
    • Rhodopsin's carboxy-terminal cytoplasmic tail acts as a membrane receptor for cytoplasmic dynein by binding to the dynein light chain Tctex-1
    • Tai A.W., Chuang J.Z., Bode C., Wolfrum U., Sung C.H. Rhodopsin's carboxy-terminal cytoplasmic tail acts as a membrane receptor for cytoplasmic dynein by binding to the dynein light chain Tctex-1. Cell 1999, 97:877-887.
    • (1999) Cell , vol.97 , pp. 877-887
    • Tai, A.W.1    Chuang, J.Z.2    Bode, C.3    Wolfrum, U.4    Sung, C.H.5
  • 149
    • 33746527488 scopus 로고    scopus 로고
    • Inactivating mutations of G protein-coupled receptors and diseases: Structure-function insights and therapeutic implications
    • Tao Y.X. Inactivating mutations of G protein-coupled receptors and diseases: Structure-function insights and therapeutic implications. Pharmacology and Therapeutics 2006, 111:949-973.
    • (2006) Pharmacology and Therapeutics , vol.111 , pp. 949-973
    • Tao, Y.X.1
  • 150
    • 0346993722 scopus 로고    scopus 로고
    • Protein kinase A regulates AKAP250 (gravin) scaffold binding to the beta2-adrenergic receptor
    • Tao J., Wang H.Y., Malbon C.C. Protein kinase A regulates AKAP250 (gravin) scaffold binding to the beta2-adrenergic receptor. The EMBO Journal 2003, 22:6419-6429.
    • (2003) The EMBO Journal , vol.22 , pp. 6419-6429
    • Tao, J.1    Wang, H.Y.2    Malbon, C.C.3
  • 151
    • 78651399026 scopus 로고    scopus 로고
    • Dopamine D(3) receptors are down-regulated following heterologous endocytosis by a specific interaction with G protein-coupled receptor-associated sorting protein-1
    • Thompson D., Whistler J.L. Dopamine D(3) receptors are down-regulated following heterologous endocytosis by a specific interaction with G protein-coupled receptor-associated sorting protein-1. The Journal of Biological Chemistry 2011, 286:1598-1608.
    • (2011) The Journal of Biological Chemistry , vol.286 , pp. 1598-1608
    • Thompson, D.1    Whistler, J.L.2
  • 152
    • 24744463670 scopus 로고    scopus 로고
    • Interaction of calmodulin with the serotonin 5-hydroxytryptamine2A receptor. A putative regulator of G protein coupling and receptor phosphorylation by protein kinase C
    • Turner J.H., Raymond J.R. Interaction of calmodulin with the serotonin 5-hydroxytryptamine2A receptor. A putative regulator of G protein coupling and receptor phosphorylation by protein kinase C. The Journal of Biological Chemistry 2005, 280:30741-30750.
    • (2005) The Journal of Biological Chemistry , vol.280 , pp. 30741-30750
    • Turner, J.H.1    Raymond, J.R.2
  • 153
    • 0032489347 scopus 로고    scopus 로고
    • Cloning and characterization of MUPP1, a novel PDZ domain protein
    • Ullmer C., Schmuck K., Figge A., Lubbert H. Cloning and characterization of MUPP1, a novel PDZ domain protein. FEBS Letters 1998, 424:63-68.
    • (1998) FEBS Letters , vol.424 , pp. 63-68
    • Ullmer, C.1    Schmuck, K.2    Figge, A.3    Lubbert, H.4
  • 155
    • 0242384217 scopus 로고    scopus 로고
    • Mechanisms regulating membrane trafficking of G protein-coupled receptors in the endocytic pathway
    • von Zastrow M. Mechanisms regulating membrane trafficking of G protein-coupled receptors in the endocytic pathway. Life Sciences 2003, 74:217-224.
    • (2003) Life Sciences , vol.74 , pp. 217-224
    • von Zastrow, M.1
  • 156
    • 77956247356 scopus 로고    scopus 로고
    • Na/H exchanger regulatory factors control parathyroid hormone receptor signaling by facilitating differential activation of G(alpha) protein subunits
    • Wang B., Ardura J.A., Romero G., Yang Y., Hall R.A., Friedman P.A. Na/H exchanger regulatory factors control parathyroid hormone receptor signaling by facilitating differential activation of G(alpha) protein subunits. The Journal of Biological Chemistry 2010, 285:26976-26986.
    • (2010) The Journal of Biological Chemistry , vol.285 , pp. 26976-26986
    • Wang, B.1    Ardura, J.A.2    Romero, G.3    Yang, Y.4    Hall, R.A.5    Friedman, P.A.6
  • 157
    • 0033531225 scopus 로고    scopus 로고
    • GABA(A)-receptor-associated protein links GABA(A) receptors and the cytoskeleton
    • Wang H., Bedford F.K., Brandon N.J., Moss S.J., Olsen R.W. GABA(A)-receptor-associated protein links GABA(A) receptors and the cytoskeleton. Nature 1999, 397:69-72.
    • (1999) Nature , vol.397 , pp. 69-72
    • Wang, H.1    Bedford, F.K.2    Brandon, N.J.3    Moss, S.J.4    Olsen, R.W.5
  • 158
    • 0037184945 scopus 로고    scopus 로고
    • Regulated interactions of the alpha 2A adrenergic receptor with spinophilin, 14-3-3zeta, and arrestin 3
    • Wang Q., Limbird L.E. Regulated interactions of the alpha 2A adrenergic receptor with spinophilin, 14-3-3zeta, and arrestin 3. The Journal of Biological Chemistry 2002, 277:50589-50596.
    • (2002) The Journal of Biological Chemistry , vol.277 , pp. 50589-50596
    • Wang, Q.1    Limbird, L.E.2
  • 159
    • 0033618426 scopus 로고    scopus 로고
    • Calmodulin binding to G protein-coupling domain of opioid receptors
    • Wang D.X., Sadee W., Quillan J.M. Calmodulin binding to G protein-coupling domain of opioid receptors. The Journal of Biological Chemistry 1999, 274:22081-22088.
    • (1999) The Journal of Biological Chemistry , vol.274 , pp. 22081-22088
    • Wang, D.X.1    Sadee, W.2    Quillan, J.M.3
  • 160
    • 66149096210 scopus 로고    scopus 로고
    • NHERF1 regulates parathyroid hormone receptor desensitization: Interference with beta-arrestin binding
    • Wang B., Yang Y., Abou-Samra A.B., Friedman P.A. NHERF1 regulates parathyroid hormone receptor desensitization: Interference with beta-arrestin binding. Molecular Pharmacology 2009, 75:1189-1197.
    • (2009) Molecular Pharmacology , vol.75 , pp. 1189-1197
    • Wang, B.1    Yang, Y.2    Abou-Samra, A.B.3    Friedman, P.A.4
  • 163
    • 61849102413 scopus 로고    scopus 로고
    • Selectivity and functional consequences of interactions of family A G protein-coupled receptors with neurochondrin and periplakin
    • Ward R.J., Jenkins L., Milligan G. Selectivity and functional consequences of interactions of family A G protein-coupled receptors with neurochondrin and periplakin. Journal of Neurochemistry 2009, 109:182-192.
    • (2009) Journal of Neurochemistry , vol.109 , pp. 182-192
    • Ward, R.J.1    Jenkins, L.2    Milligan, G.3
  • 164
    • 33646009701 scopus 로고    scopus 로고
    • The association of NHERF adaptor proteins with G protein-coupled receptors and receptor tyrosine kinases
    • Weinman E.J., Hall R.A., Friedman P.A., Liu-Chen L.Y., Shenolikar S. The association of NHERF adaptor proteins with G protein-coupled receptors and receptor tyrosine kinases. Annual Review of Physiology 2006, 68:491-505.
    • (2006) Annual Review of Physiology , vol.68 , pp. 491-505
    • Weinman, E.J.1    Hall, R.A.2    Friedman, P.A.3    Liu-Chen, L.Y.4    Shenolikar, S.5
  • 167
    • 0037484186 scopus 로고    scopus 로고
    • A direct interaction of PSD-95 with 5-HT2A serotonin receptors regulates receptor trafficking and signal transduction
    • Xia Z., Gray J.A., Compton-Toth B.A., Roth B.L. A direct interaction of PSD-95 with 5-HT2A serotonin receptors regulates receptor trafficking and signal transduction. The Journal of Biological Chemistry 2003, 278:21901-21908.
    • (2003) The Journal of Biological Chemistry , vol.278 , pp. 21901-21908
    • Xia, Z.1    Gray, J.A.2    Compton-Toth, B.A.3    Roth, B.L.4
  • 169
    • 0035798618 scopus 로고    scopus 로고
    • Beta 1-adrenergic receptor association with the synaptic scaffolding protein membrane-associated guanylate kinase inverted-2 (MAGI-2). Differential regulation of receptor internalization by MAGI-2 and PSD-95
    • Xu J., Paquet M., Lau A.G., Wood J.D., Ross C.A., Hall R.A. Beta 1-adrenergic receptor association with the synaptic scaffolding protein membrane-associated guanylate kinase inverted-2 (MAGI-2). Differential regulation of receptor internalization by MAGI-2 and PSD-95. The Journal of Biological Chemistry 2001, 276:41310-41317.
    • (2001) The Journal of Biological Chemistry , vol.276 , pp. 41310-41317
    • Xu, J.1    Paquet, M.2    Lau, A.G.3    Wood, J.D.4    Ross, C.A.5    Hall, R.A.6
  • 170
    • 77952958326 scopus 로고    scopus 로고
    • Beta-2 adrenergic receptor mediated ERK activation is regulated by interaction with MAGI-3
    • Yang X., Zheng J., Xiong Y., Shen H., Sun L., Huang Y., Sun C., Li Y., He J. Beta-2 adrenergic receptor mediated ERK activation is regulated by interaction with MAGI-3. FEBS Letters 2010, 584:2207-2212.
    • (2010) FEBS Letters , vol.584 , pp. 2207-2212
    • Yang, X.1    Zheng, J.2    Xiong, Y.3    Shen, H.4    Sun, L.5    Huang, Y.6    Sun, C.7    Li, Y.8    He, J.9
  • 171
    • 33749510646 scopus 로고    scopus 로고
    • Regulatory dissociation of Tctex-1 light chain from dynein complex is essential for the apical delivery of rhodopsin
    • Yeh T.Y., Peretti D., Chuang J.Z., Rodriguez-Boulan E., Sung C.H. Regulatory dissociation of Tctex-1 light chain from dynein complex is essential for the apical delivery of rhodopsin. Traffic 2006, 7:1495-1502.
    • (2006) Traffic , vol.7 , pp. 1495-1502
    • Yeh, T.Y.1    Peretti, D.2    Chuang, J.Z.3    Rodriguez-Boulan, E.4    Sung, C.H.5
  • 172
    • 40949119063 scopus 로고    scopus 로고
    • Binding of the P2Y2 nucleotide receptor to filamin A regulates migration of vascular smooth muscle cells
    • Yu N., Erb L., Shivaji R., Weisman G.A., Seye C.I. Binding of the P2Y2 nucleotide receptor to filamin A regulates migration of vascular smooth muscle cells. Circulation Research 2008, 102:581-588.
    • (2008) Circulation Research , vol.102 , pp. 581-588
    • Yu, N.1    Erb, L.2    Shivaji, R.3    Weisman, G.A.4    Seye, C.I.5
  • 173
    • 51649112473 scopus 로고    scopus 로고
    • Knock-in mice lacking the PDZ-ligand motif of mGluR7a show impaired PKC-dependent autoinhibition of glutamate release, spatial working memory deficits, and increased susceptibility to pentylenetetrazol
    • Zhang C.S., Bertaso F., Eulenburg V., Lerner-Natoli M., Herin G.A., Bauer L., Bockaert J., Fagni L., Betz H., Scheschonka A. Knock-in mice lacking the PDZ-ligand motif of mGluR7a show impaired PKC-dependent autoinhibition of glutamate release, spatial working memory deficits, and increased susceptibility to pentylenetetrazol. The Journal of Neuroscience 2008, 28:8604-8614.
    • (2008) The Journal of Neuroscience , vol.28 , pp. 8604-8614
    • Zhang, C.S.1    Bertaso, F.2    Eulenburg, V.3    Lerner-Natoli, M.4    Herin, G.A.5    Bauer, L.6    Bockaert, J.7    Fagni, L.8    Betz, H.9    Scheschonka, A.10
  • 174
    • 15744379719 scopus 로고    scopus 로고
    • High affinity interaction with filamin A protects against calcium-sensing receptor degradation
    • Zhang M., Breitwieser G.E. High affinity interaction with filamin A protects against calcium-sensing receptor degradation. The Journal of Biological Chemistry 2005, 280:11140-11146.
    • (2005) The Journal of Biological Chemistry , vol.280 , pp. 11140-11146
    • Zhang, M.1    Breitwieser, G.E.2
  • 177
    • 57049140415 scopus 로고    scopus 로고
    • C-Src-mediated phosphorylation of AP-2 reveals a general mechanism for receptors internalizing through the clathrin pathway
    • Zimmerman B., Simaan M., Lee M.H., Luttrell L.M., Laporte S.A. c-Src-mediated phosphorylation of AP-2 reveals a general mechanism for receptors internalizing through the clathrin pathway. Cellular Signalling 2009, 21:103-110.
    • (2009) Cellular Signalling , vol.21 , pp. 103-110
    • Zimmerman, B.1    Simaan, M.2    Lee, M.H.3    Luttrell, L.M.4    Laporte, S.A.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.