메뉴 건너뛰기




Volumn 30, Issue 2, 2009, Pages 72-78

Recent methodological advances in the discovery of GPCR-associated protein complexes

Author keywords

[No Author keywords available]

Indexed keywords

ADAPTOR PROTEIN; FERRIC OXIDE; G PROTEIN COUPLED RECEPTOR; GALLIUM; GUANINE NUCLEOTIDE BINDING PROTEIN ALPHA SUBUNIT; GUANINE NUCLEOTIDE BINDING PROTEIN BETA SUBUNIT; GUANINE NUCLEOTIDE BINDING PROTEIN GAMMA SUBUNIT; LEVAMISOLE; MEMBRANE RECEPTOR; SEROTONIN 2A RECEPTOR; SEROTONIN 2C RECEPTOR; SEROTONIN 4 RECEPTOR; TITANIUM DIOXIDE; TRANSPORTER ASSOCIATED WITH ANTIGEN PROCESSING 1;

EID: 59549102113     PISSN: 01656147     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.tips.2008.10.009     Document Type: Review
Times cited : (39)

References (45)
  • 1
    • 42149181885 scopus 로고    scopus 로고
    • Structural diversity of G protein-coupled receptors and significance for drug discovery
    • Lagerstrom M.C., and Schioth H.B. Structural diversity of G protein-coupled receptors and significance for drug discovery. Nat. Rev. Drug Discov. 7 (2008) 339-357
    • (2008) Nat. Rev. Drug Discov. , vol.7 , pp. 339-357
    • Lagerstrom, M.C.1    Schioth, H.B.2
  • 2
    • 0037050026 scopus 로고    scopus 로고
    • Functional organization of the yeast proteome by systematic analysis of protein complexes
    • Gavin A.C., et al. Functional organization of the yeast proteome by systematic analysis of protein complexes. Nature 415 (2002) 141-147
    • (2002) Nature , vol.415 , pp. 141-147
    • Gavin, A.C.1
  • 3
    • 4644260473 scopus 로고    scopus 로고
    • GPCR interacting proteins (GIP)
    • Bockaert J., et al. GPCR interacting proteins (GIP). Pharmacol. Ther. 103 (2004) 203-221
    • (2004) Pharmacol. Ther. , vol.103 , pp. 203-221
    • Bockaert, J.1
  • 4
    • 3042670429 scopus 로고    scopus 로고
    • 2 'receptosomes'
    • 2 'receptosomes'. Biol. Cell 96 (2004) 373-381
    • (2004) Biol. Cell , vol.96 , pp. 373-381
    • Gavarini, S.1
  • 5
    • 2342470026 scopus 로고    scopus 로고
    • Identification and functional roles of metabotropic glutamate receptor-interacting proteins
    • Fagni L., et al. Identification and functional roles of metabotropic glutamate receptor-interacting proteins. Semin. Cell Dev. Biol. 15 (2004) 289-298
    • (2004) Semin. Cell Dev. Biol. , vol.15 , pp. 289-298
    • Fagni, L.1
  • 6
    • 33748068161 scopus 로고    scopus 로고
    • Proteome analysis to study signal transduction of G protein-coupled receptors
    • Pluder F., et al. Proteome analysis to study signal transduction of G protein-coupled receptors. Pharmacol. Ther. 112 (2006) 1-11
    • (2006) Pharmacol. Ther. , vol.112 , pp. 1-11
    • Pluder, F.1
  • 7
    • 33846615765 scopus 로고    scopus 로고
    • The trick of the tail: protein-protein interactions of metabotropic glutamate receptors
    • Enz R. The trick of the tail: protein-protein interactions of metabotropic glutamate receptors. Bioessays 29 (2007) 60-73
    • (2007) Bioessays , vol.29 , pp. 60-73
    • Enz, R.1
  • 8
    • 34249670262 scopus 로고    scopus 로고
    • Purification and identification of G protein-coupled receptor protein complexes under native conditions
    • Daulat A.M., et al. Purification and identification of G protein-coupled receptor protein complexes under native conditions. Mol. Cell. Proteomics 6 (2007) 835-844
    • (2007) Mol. Cell. Proteomics , vol.6 , pp. 835-844
    • Daulat, A.M.1
  • 9
    • 41849128212 scopus 로고    scopus 로고
    • An optimized split-ubiquitin cDNA-library screening system to identify novel interactors of the human Frizzled 1 receptor
    • Dirnberger D., et al. An optimized split-ubiquitin cDNA-library screening system to identify novel interactors of the human Frizzled 1 receptor. Nucleic Acids Res. 36 (2008) e37
    • (2008) Nucleic Acids Res. , vol.36
    • Dirnberger, D.1
  • 11
    • 47749156829 scopus 로고    scopus 로고
    • 1 melatonin receptor
    • 1 melatonin receptor. J. Biol. Chem. 283 (2008) 16762-16771
    • (2008) J. Biol. Chem. , vol.283 , pp. 16762-16771
    • Guillaume, J.L.1
  • 12
    • 11144229682 scopus 로고    scopus 로고
    • A library of 7TM receptor C-terminal tails. Interactions with the proposed post-endocytic sorting proteins ERM-binding phosphoprotein 50 (EBP50), N-ethylmaleimide-sensitive factor (NSF), sorting nexin 1 (SNX1), and G protein-coupled receptor-associated sorting protein (GASP)
    • Heydorn A., et al. A library of 7TM receptor C-terminal tails. Interactions with the proposed post-endocytic sorting proteins ERM-binding phosphoprotein 50 (EBP50), N-ethylmaleimide-sensitive factor (NSF), sorting nexin 1 (SNX1), and G protein-coupled receptor-associated sorting protein (GASP). J. Biol. Chem. 279 (2004) 54291-54303
    • (2004) J. Biol. Chem. , vol.279 , pp. 54291-54303
    • Heydorn, A.1
  • 13
    • 20344390032 scopus 로고    scopus 로고
    • P2Y1 receptor signaling is controlled by interaction with the PDZ scaffold NHERF-2
    • Fam S.R., et al. P2Y1 receptor signaling is controlled by interaction with the PDZ scaffold NHERF-2. Proc. Natl. Acad. Sci. U. S. A. 102 (2005) 8042-8047
    • (2005) Proc. Natl. Acad. Sci. U. S. A. , vol.102 , pp. 8042-8047
    • Fam, S.R.1
  • 14
    • 34547127612 scopus 로고    scopus 로고
    • PDZ domain binding selectivity is optimized across the mouse proteome
    • Stiffler M.A., et al. PDZ domain binding selectivity is optimized across the mouse proteome. Science 317 (2007) 364-369
    • (2007) Science , vol.317 , pp. 364-369
    • Stiffler, M.A.1
  • 15
    • 33749559624 scopus 로고    scopus 로고
    • The PDZ scaffold NHERF-2 interacts with mGluR5 and regulates receptor activity
    • Paquet M., et al. The PDZ scaffold NHERF-2 interacts with mGluR5 and regulates receptor activity. J. Biol. Chem. 281 (2006) 29949-29961
    • (2006) J. Biol. Chem. , vol.281 , pp. 29949-29961
    • Paquet, M.1
  • 16
    • 0037093469 scopus 로고    scopus 로고
    • 2C receptors: a proteomic approach
    • 2C receptors: a proteomic approach. EMBO J. 21 (2002) 2332-2342
    • (2002) EMBO J. , vol.21 , pp. 2332-2342
    • Becamel, C.1
  • 17
    • 2442626585 scopus 로고    scopus 로고
    • 2C receptors interact with specific sets of PDZ proteins
    • 2C receptors interact with specific sets of PDZ proteins. J. Biol. Chem. 279 (2004) 20257-20266
    • (2004) J. Biol. Chem. , vol.279 , pp. 20257-20266
    • Becamel, C.1
  • 18
    • 9444267090 scopus 로고    scopus 로고
    • 4a receptor splice variant: roles in receptor targeting
    • 4a receptor splice variant: roles in receptor targeting. J. Cell Sci. 117 (2004) 5367-5379
    • (2004) J. Cell Sci. , vol.117 , pp. 5367-5379
    • Joubert, L.1
  • 19
    • 0035918289 scopus 로고    scopus 로고
    • Interaction of serotonin 5-hydroxytryptamine type 2C receptors with PDZ10 of the multi-PDZ domain protein MUPP1
    • Becamel C., et al. Interaction of serotonin 5-hydroxytryptamine type 2C receptors with PDZ10 of the multi-PDZ domain protein MUPP1. J. Biol. Chem. 276 (2001) 12974-12982
    • (2001) J. Biol. Chem. , vol.276 , pp. 12974-12982
    • Becamel, C.1
  • 20
    • 8744262113 scopus 로고    scopus 로고
    • GPCR-interacting proteins (GIPs): nature and functions
    • Bockaert J., et al. GPCR-interacting proteins (GIPs): nature and functions. Biochem. Soc. Trans. 32 (2004) 851-855
    • (2004) Biochem. Soc. Trans. , vol.32 , pp. 851-855
    • Bockaert, J.1
  • 21
    • 33750501125 scopus 로고    scopus 로고
    • 2C receptor desensitization and membrane stability
    • 2C receptor desensitization and membrane stability. Mol. Biol. Cell 17 (2006) 4619-4631
    • (2006) Mol. Biol. Cell , vol.17 , pp. 4619-4631
    • Gavarini, S.1
  • 22
    • 58149306364 scopus 로고    scopus 로고
    • 2C receptor C-terminus is essential for G Protein-independent, arrestin-dependent, receptor signaling
    • 2C receptor C-terminus is essential for G Protein-independent, arrestin-dependent, receptor signaling. Mol. Biol. Cell 19 (2008) 4640-4650
    • (2008) Mol. Biol. Cell , vol.19 , pp. 4640-4650
    • Labasque, M.1
  • 23
    • 47249083145 scopus 로고    scopus 로고
    • A generic approach for the purification of signaling complexes that specifically interact with the carboxy-terminal domain of G protein-coupled receptors
    • Maurice P., et al. A generic approach for the purification of signaling complexes that specifically interact with the carboxy-terminal domain of G protein-coupled receptors. Mol. Cell. Proteomics 7 (2008) 1556-1569
    • (2008) Mol. Cell. Proteomics , vol.7 , pp. 1556-1569
    • Maurice, P.1
  • 24
    • 40849088096 scopus 로고    scopus 로고
    • i proteins, MEK 1/2 and microtubule modulation
    • i proteins, MEK 1/2 and microtubule modulation. J. Pineal Res. 44 (2008) 288-298
    • (2008) J. Pineal Res. , vol.44 , pp. 288-298
    • Bondi, C.D.1
  • 25
    • 5444257565 scopus 로고    scopus 로고
    • Proteomic analysis of native metabotropic glutamate receptor 5 protein complexes reveals novel molecular constituents
    • Farr C.D., et al. Proteomic analysis of native metabotropic glutamate receptor 5 protein complexes reveals novel molecular constituents. J. Neurochem. 91 (2004) 438-450
    • (2004) J. Neurochem. , vol.91 , pp. 438-450
    • Farr, C.D.1
  • 26
    • 0032828715 scopus 로고    scopus 로고
    • A generic protein purification method for protein complex characterization and proteome exploration
    • Rigaut G., et al. A generic protein purification method for protein complex characterization and proteome exploration. Nat. Biotechnol. 17 (1999) 1030-1032
    • (1999) Nat. Biotechnol. , vol.17 , pp. 1030-1032
    • Rigaut, G.1
  • 27
    • 49649105002 scopus 로고    scopus 로고
    • Blood pressure is regulated by an α1D-adrenergic receptor/dystrophin signalosome
    • Lyssand J.S., et al. Blood pressure is regulated by an α1D-adrenergic receptor/dystrophin signalosome. J. Biol. Chem. 283 (2008) 18792-18800
    • (2008) J. Biol. Chem. , vol.283 , pp. 18792-18800
    • Lyssand, J.S.1
  • 28
    • 57649165543 scopus 로고    scopus 로고
    • Disease causing mutation in GPR54 reveals importance of second intracellular loop for class A GPCR function
    • Wacker J.L., et al. Disease causing mutation in GPR54 reveals importance of second intracellular loop for class A GPCR function. J. Biol. Chem. 283 (2008) 31068-31078
    • (2008) J. Biol. Chem. , vol.283 , pp. 31068-31078
    • Wacker, J.L.1
  • 29
    • 3042647602 scopus 로고    scopus 로고
    • Control of cell size through phosphorylation of upstream binding factor 1 by nuclear phosphatidylinositol 3-kinase
    • Drakas R., et al. Control of cell size through phosphorylation of upstream binding factor 1 by nuclear phosphatidylinositol 3-kinase. Proc. Natl. Acad. Sci. U. S. A. 101 (2004) 9272-9276
    • (2004) Proc. Natl. Acad. Sci. U. S. A. , vol.101 , pp. 9272-9276
    • Drakas, R.1
  • 30
    • 33751211249 scopus 로고    scopus 로고
    • An efficient tandem affinity purification procedure for interaction proteomics in mammalian cells
    • Burckstummer T., et al. An efficient tandem affinity purification procedure for interaction proteomics in mammalian cells. Nat. Methods 3 (2006) 1013-1019
    • (2006) Nat. Methods , vol.3 , pp. 1013-1019
    • Burckstummer, T.1
  • 31
    • 37048999786 scopus 로고    scopus 로고
    • A novel tandem affinity purification strategy for the efficient isolation and characterisation of native protein complexes
    • Gloeckner C.J., et al. A novel tandem affinity purification strategy for the efficient isolation and characterisation of native protein complexes. Proteomics 7 (2007) 4228-4234
    • (2007) Proteomics , vol.7 , pp. 4228-4234
    • Gloeckner, C.J.1
  • 32
    • 33644670152 scopus 로고    scopus 로고
    • An integrated mass spectrometry-based proteomic approach: quantitative analysis of tandem affinity-purified in vivo cross-linked protein complexes (QTAX) to decipher the 26 S proteasome-interacting network
    • Guerrero C., et al. An integrated mass spectrometry-based proteomic approach: quantitative analysis of tandem affinity-purified in vivo cross-linked protein complexes (QTAX) to decipher the 26 S proteasome-interacting network. Mol. Cell. Proteomics 5 (2006) 366-378
    • (2006) Mol. Cell. Proteomics , vol.5 , pp. 366-378
    • Guerrero, C.1
  • 33
    • 33645703441 scopus 로고    scopus 로고
    • A tandem affinity tag for two-step purification under fully denaturing conditions: application in ubiquitin profiling and protein complex identification combined with in vivo cross-linking
    • Tagwerker C., et al. A tandem affinity tag for two-step purification under fully denaturing conditions: application in ubiquitin profiling and protein complex identification combined with in vivo cross-linking. Mol. Cell. Proteomics 5 (2006) 737-748
    • (2006) Mol. Cell. Proteomics , vol.5 , pp. 737-748
    • Tagwerker, C.1
  • 34
    • 34547131554 scopus 로고    scopus 로고
    • Analysis of protein complexes using mass spectrometry
    • Gingras A.C., et al. Analysis of protein complexes using mass spectrometry. Nat. Rev. Mol. Cell Biol. 8 (2007) 645-654
    • (2007) Nat. Rev. Mol. Cell Biol. , vol.8 , pp. 645-654
    • Gingras, A.C.1
  • 35
    • 40549140726 scopus 로고    scopus 로고
    • Proteomic approaches to the analysis of multiprotein signaling complexes
    • Yang W., et al. Proteomic approaches to the analysis of multiprotein signaling complexes. Proteomics 8 (2008) 832-851
    • (2008) Proteomics , vol.8 , pp. 832-851
    • Yang, W.1
  • 36
    • 33845989449 scopus 로고    scopus 로고
    • Transgenic mouse proteomics identifies new 14-3-3-associated proteins involved in cytoskeletal rearrangements and cell signaling
    • Angrand P.O., et al. Transgenic mouse proteomics identifies new 14-3-3-associated proteins involved in cytoskeletal rearrangements and cell signaling. Mol. Cell. Proteomics 5 (2006) 2211-2227
    • (2006) Mol. Cell. Proteomics , vol.5 , pp. 2211-2227
    • Angrand, P.O.1
  • 37
    • 57649186970 scopus 로고    scopus 로고
    • Stable form of Jab1 enhances proliferation and maintenance of hematopoietic progenitors
    • Mori M., et al. Stable form of Jab1 enhances proliferation and maintenance of hematopoietic progenitors. J. Biol. Chem. 283 (2008) 29011-29021
    • (2008) J. Biol. Chem. , vol.283 , pp. 29011-29021
    • Mori, M.1
  • 38
    • 0346094408 scopus 로고    scopus 로고
    • Recent developments in the analysis of protein complexes
    • Dziembowski A., and Seraphin B. Recent developments in the analysis of protein complexes. FEBS Lett. 556 (2004) 1-6
    • (2004) FEBS Lett. , vol.556 , pp. 1-6
    • Dziembowski, A.1    Seraphin, B.2
  • 39
    • 23044432697 scopus 로고    scopus 로고
    • Identification and characterization of novel nicotinic receptor-associated proteins in Caenorhabditis elegans
    • Gottschalk A., et al. Identification and characterization of novel nicotinic receptor-associated proteins in Caenorhabditis elegans. EMBO J. 24 (2005) 2566-2578
    • (2005) EMBO J. , vol.24 , pp. 2566-2578
    • Gottschalk, A.1
  • 40
    • 33751564506 scopus 로고    scopus 로고
    • Amphipathic polymers: tools to fold integral membrane proteins to their active form
    • Pocanschi C.L., et al. Amphipathic polymers: tools to fold integral membrane proteins to their active form. Biochemistry 45 (2006) 13954-13961
    • (2006) Biochemistry , vol.45 , pp. 13954-13961
    • Pocanschi, C.L.1
  • 41
    • 33644874562 scopus 로고    scopus 로고
    • Robust enrichment of phosphorylated species in complex mixtures by sequential protein and peptide metal-affinity chromatography and analysis by tandem mass spectrometry
    • Collins M.O., et al. Robust enrichment of phosphorylated species in complex mixtures by sequential protein and peptide metal-affinity chromatography and analysis by tandem mass spectrometry. Sci. STKE 2005 (2005) pl6
    • (2005) Sci. STKE , vol.2005
    • Collins, M.O.1
  • 42
    • 0036849482 scopus 로고    scopus 로고
    • Analysis of membrane protein interactions using yeast-based technologies
    • Stagljar I., and Fields S. Analysis of membrane protein interactions using yeast-based technologies. Trends Biochem. Sci. 27 (2002) 559-563
    • (2002) Trends Biochem. Sci. , vol.27 , pp. 559-563
    • Stagljar, I.1    Fields, S.2
  • 43
    • 47849096465 scopus 로고    scopus 로고
    • Monitoring protein-protein interactions between the mammalian integral membrane transporters and PDZ-interacting partners using a modified split-ubiquitin membrane yeast two-hybrid system
    • Gisler S.M., et al. Monitoring protein-protein interactions between the mammalian integral membrane transporters and PDZ-interacting partners using a modified split-ubiquitin membrane yeast two-hybrid system. Mol. Cell. Proteomics 7 (2008) 1362-1377
    • (2008) Mol. Cell. Proteomics , vol.7 , pp. 1362-1377
    • Gisler, S.M.1
  • 44
    • 33747120931 scopus 로고    scopus 로고
    • Biosynthesis and trafficking of seven transmembrane receptor signalling complexes
    • Dupre D.J., and Hebert T.E. Biosynthesis and trafficking of seven transmembrane receptor signalling complexes. Cell. Signal. 18 (2006) 1549-1559
    • (2006) Cell. Signal. , vol.18 , pp. 1549-1559
    • Dupre, D.J.1    Hebert, T.E.2
  • 45
    • 33750502435 scopus 로고    scopus 로고
    • Do orphan G-protein-coupled receptors have ligand-independent functions? New insights from receptor heterodimers
    • Levoye A., et al. Do orphan G-protein-coupled receptors have ligand-independent functions? New insights from receptor heterodimers. EMBO Rep. 7 (2006) 1094-1098
    • (2006) EMBO Rep. , vol.7 , pp. 1094-1098
    • Levoye, A.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.