메뉴 건너뛰기




Volumn 158, Issue 3, 2007, Pages 482-493

Cell-free production of G protein-coupled receptors for functional and structural studies

Author keywords

Corticotropin releasing factor receptor; Detergent; Endothelin B receptor; Melatonin 1B receptor; Neuropeptide Y4 receptor; Single particle analysis; TIRFS; Vasopressin type 2 receptor

Indexed keywords

CORTICOTROPIN; DETERGENT; ENDOTHELIN B RECEPTOR; G PROTEIN COUPLED RECEPTOR; MELATONIN 1 RECEPTOR; MELATONIN 1B RECEPTOR; MEMBRANE PROTEIN; NEUROPEPTIDE Y4 RECEPTOR; POLYOXYETHYLENE STEARYL ETHER; RHODOPSIN; UNCLASSIFIED DRUG; VASOPRESSIN RECEPTOR; VASOPRESSIN TYPE 2 RECEPTOR;

EID: 34248572721     PISSN: 10478477     EISSN: 10958657     Source Type: Journal    
DOI: 10.1016/j.jsb.2007.01.006     Document Type: Article
Times cited : (89)

References (52)
  • 2
    • 33646155331 scopus 로고    scopus 로고
    • Enhancing functional production of G protein-coupled receptors in Pichia pastoris to levels required for structural studies via a single expression screen
    • André N., Cherouati N., Prual C., Steffan T., Zeder-Lutz G., Magnin T., Pattui{dotless}̀ F., Michel H., Wagner R., and Reinhart C. Enhancing functional production of G protein-coupled receptors in Pichia pastoris to levels required for structural studies via a single expression screen. Protein Sci. 15 (2006) 1115-1126
    • (2006) Protein Sci. , vol.15 , pp. 1115-1126
    • André, N.1    Cherouati, N.2    Prual, C.3    Steffan, T.4    Zeder-Lutz, G.5    Magnin, T.6    Pattuì, F.7    Michel, H.8    Wagner, R.9    Reinhart, C.10
  • 3
    • 0037077208 scopus 로고    scopus 로고
    • Monitoring of ligand-independent dimerization and ligand-induced conformational changes of melatonin receptors in living cells by bioluminescence resonance energy transfer
    • Ayoub M.A., Coutourier C., Lucas-Meunier E., Angers S., Fossier P., Bouvier M., and Jockers R. Monitoring of ligand-independent dimerization and ligand-induced conformational changes of melatonin receptors in living cells by bioluminescence resonance energy transfer. J. Biol. Chem. 277 (2002) 21522-21528
    • (2002) J. Biol. Chem. , vol.277 , pp. 21522-21528
    • Ayoub, M.A.1    Coutourier, C.2    Lucas-Meunier, E.3    Angers, S.4    Fossier, P.5    Bouvier, M.6    Jockers, R.7
  • 4
    • 0242572132 scopus 로고    scopus 로고
    • Dimerization of G-protein-coupled receptors: roles in signal transduction
    • Bai M. Dimerization of G-protein-coupled receptors: roles in signal transduction. Cell. Signal. 16 (2004) 175-186
    • (2004) Cell. Signal. , vol.16 , pp. 175-186
    • Bai, M.1
  • 5
    • 4744351698 scopus 로고    scopus 로고
    • Cell-free synthesis of a functional ion channel in the absence of a membrane and in the presence of detergent
    • Berrier C., Park K.H., Abes S., Bibonne A., Betton J.M., and Ghazi A. Cell-free synthesis of a functional ion channel in the absence of a membrane and in the presence of detergent. Biochemistry 43 (2004) 12585-12591
    • (2004) Biochemistry , vol.43 , pp. 12585-12591
    • Berrier, C.1    Park, K.H.2    Abes, S.3    Bibonne, A.4    Betton, J.M.5    Ghazi, A.6
  • 6
    • 0038237527 scopus 로고    scopus 로고
    • Homodimerization of neuropeptide y receptors investigated by fluorescence resonance energy transfer in living cells
    • Dinger M.C., Bader J.E., Kobor A.D., Kretschmar A.K., and Beck-Sickinger A.G. Homodimerization of neuropeptide y receptors investigated by fluorescence resonance energy transfer in living cells. J. Biol. Chem. 278 (2003) 10562-71051
    • (2003) J. Biol. Chem. , vol.278 , pp. 10562-71051
    • Dinger, M.C.1    Bader, J.E.2    Kobor, A.D.3    Kretschmar, A.K.4    Beck-Sickinger, A.G.5
  • 7
    • 1242319564 scopus 로고    scopus 로고
    • In vitro synthesis of fully functional EmrE, a multidrug transporter, and study of its oligomeric state
    • Elbaz Y., Steiner-Mordoch S., Danieli T., and Schuldiner S. In vitro synthesis of fully functional EmrE, a multidrug transporter, and study of its oligomeric state. Proc. Natl. Acad. Sci. USA 101 (2004) 1519-1524
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 1519-1524
    • Elbaz, Y.1    Steiner-Mordoch, S.2    Danieli, T.3    Schuldiner, S.4
  • 11
    • 0020406488 scopus 로고
    • Multivariate statistical analysis of ribosome electron micrographs. L and R lateral views of the 40 S subunit from HeLa cells
    • Frank J., Verschoor A., and Boublik M. Multivariate statistical analysis of ribosome electron micrographs. L and R lateral views of the 40 S subunit from HeLa cells. J. Mol. Biol. 161 (1982) 107-133
    • (1982) J. Mol. Biol. , vol.161 , pp. 107-133
    • Frank, J.1    Verschoor, A.2    Boublik, M.3
  • 12
    • 0029975088 scopus 로고    scopus 로고
    • SPIDER and WEB: processing and visualization of images in 3D electron microscopy and related fields
    • Frank J., Radermacher M., Pencek P., Zhu J., Li Y., Ladjadj M., and Leith A. SPIDER and WEB: processing and visualization of images in 3D electron microscopy and related fields. J. Struct. Biol. 116 (1996) 190-199
    • (1996) J. Struct. Biol. , vol.116 , pp. 190-199
    • Frank, J.1    Radermacher, M.2    Pencek, P.3    Zhu, J.4    Li, Y.5    Ladjadj, M.6    Leith, A.7
  • 13
    • 20444452736 scopus 로고    scopus 로고
    • Lateral ligand-receptor interactions on membranes probed by simultaneous fluorescence-interference detection
    • Gavutis M., Lata S., Lamken P., Müller P., and Piehler J. Lateral ligand-receptor interactions on membranes probed by simultaneous fluorescence-interference detection. Biophys. J. 88 (2005) 4289-4302
    • (2005) Biophys. J. , vol.88 , pp. 4289-4302
    • Gavutis, M.1    Lata, S.2    Lamken, P.3    Müller, P.4    Piehler, J.5
  • 14
    • 11144271570 scopus 로고    scopus 로고
    • Fluorescence resonance energy transfer analysis reveals the existence of endothelin-A and endothelin-B receptor homodimers
    • Gregan B., Schaefer M., Rosenthal W., and Oksche A. Fluorescence resonance energy transfer analysis reveals the existence of endothelin-A and endothelin-B receptor homodimers. J. Cardiovasc. Pharmacol. 44 (2004) S30-S33
    • (2004) J. Cardiovasc. Pharmacol. , vol.44
    • Gregan, B.1    Schaefer, M.2    Rosenthal, W.3    Oksche, A.4
  • 15
    • 26444581283 scopus 로고    scopus 로고
    • Large-scale expression and purification of a G-protein-coupled receptor for structure determination-an overview
    • Grisshammer R., White J.F., Trinh L.B., and Shiloach J. Large-scale expression and purification of a G-protein-coupled receptor for structure determination-an overview. J. Struct. Funct. Genom. 6 (2005) 159-163
    • (2005) J. Struct. Funct. Genom. , vol.6 , pp. 159-163
    • Grisshammer, R.1    White, J.F.2    Trinh, L.B.3    Shiloach, J.4
  • 16
    • 9644263918 scopus 로고    scopus 로고
    • Functional consequences of 7TM receptor dimerization
    • Hansen J.L., and Sheikh S.P. Functional consequences of 7TM receptor dimerization. Eur. J. Pharmaceut. Sci. 23 (2004) 301-317
    • (2004) Eur. J. Pharmaceut. Sci. , vol.23 , pp. 301-317
    • Hansen, J.L.1    Sheikh, S.P.2
  • 18
    • 0038646059 scopus 로고    scopus 로고
    • Structural and functional aspects of G protein-coupled receptor oligomerization
    • Hebert T.E., and Bouvier M. Structural and functional aspects of G protein-coupled receptor oligomerization. Biochem. Cell. Biol. 76 (1998) 1-10
    • (1998) Biochem. Cell. Biol. , vol.76 , pp. 1-10
    • Hebert, T.E.1    Bouvier, M.2
  • 19
    • 0025196885 scopus 로고
    • Binding of [125I]-endothelin-1 to rat cerebellar homogenates and its interactions with some analogues
    • Hiley C.R., Jones C.R., Pelton J.T., and Miller R.C. Binding of [125I]-endothelin-1 to rat cerebellar homogenates and its interactions with some analogues. Br. J. Pharmacol. 101 (1990) 319-324
    • (1990) Br. J. Pharmacol. , vol.101 , pp. 319-324
    • Hiley, C.R.1    Jones, C.R.2    Pelton, J.T.3    Miller, R.C.4
  • 20
    • 0032200201 scopus 로고    scopus 로고
    • Purification of recombinant M1 muscarinic acetylcholine receptor
    • Hulme E.C., and Curtis C.A. Purification of recombinant M1 muscarinic acetylcholine receptor. Biochem. Soc. Trans. 26 (1998) S361
    • (1998) Biochem. Soc. Trans. , vol.26
    • Hulme, E.C.1    Curtis, C.A.2
  • 21
    • 15744391469 scopus 로고    scopus 로고
    • Expression of G protein coupled receptors in a cell-free translational system using detergents and thioredoxin-fusion vectors
    • Ishihara G., Goto M., Saeki M., Ito K., Hori T., Kigawa T., Shirouzu M., and Yokoyama S. Expression of G protein coupled receptors in a cell-free translational system using detergents and thioredoxin-fusion vectors. Protein Expres. Purif. 41 (2005) 27-37
    • (2005) Protein Expres. Purif. , vol.41 , pp. 27-37
    • Ishihara, G.1    Goto, M.2    Saeki, M.3    Ito, K.4    Hori, T.5    Kigawa, T.6    Shirouzu, M.7    Yokoyama, S.8
  • 22
    • 0032923295 scopus 로고    scopus 로고
    • Cell-free production and stable-isotope labeling of milligram quantities of proteins
    • Kigawa T., Yabuki T., Yoshida Y., Tsutsui M., Ito Y., Shibata T., and Yokoyama S. Cell-free production and stable-isotope labeling of milligram quantities of proteins. FEBS Lett. 442 (1999) 15-19
    • (1999) FEBS Lett. , vol.442 , pp. 15-19
    • Kigawa, T.1    Yabuki, T.2    Yoshida, Y.3    Tsutsui, M.4    Ito, Y.5    Shibata, T.6    Yokoyama, S.7
  • 23
    • 0037020329 scopus 로고    scopus 로고
    • Drug design strategies for targeting G-protein-coupled receptors
    • Klabunde T., and Hessler G. Drug design strategies for targeting G-protein-coupled receptors. ChemBioChem 3 (2002) 928-944
    • (2002) ChemBioChem , vol.3 , pp. 928-944
    • Klabunde, T.1    Hessler, G.2
  • 25
    • 28244458078 scopus 로고    scopus 로고
    • Evaluation of detergents for the soluble expression of alpha-helical and beta-barrel- type integral membrane proteins by a preparative scale individual cell-free expression system
    • Klammt C., Schwarz D., Fendler K., Haase W., Dötsch V., and Bernhard F. Evaluation of detergents for the soluble expression of alpha-helical and beta-barrel- type integral membrane proteins by a preparative scale individual cell-free expression system. FEBS J. 272 (2005) 6024-6038
    • (2005) FEBS J. , vol.272 , pp. 6024-6038
    • Klammt, C.1    Schwarz, D.2    Fendler, K.3    Haase, W.4    Dötsch, V.5    Bernhard, F.6
  • 26
    • 33748307399 scopus 로고    scopus 로고
    • Cell-free expression as an emerging technique for the large scale production of integral membrane proteins
    • Klammt C., Schwarz D., Löhr F., Schneider B., Dötsch V., and Bernhard F. Cell-free expression as an emerging technique for the large scale production of integral membrane proteins. FEBS J. 273 (2006) 4141-4153
    • (2006) FEBS J. , vol.273 , pp. 4141-4153
    • Klammt, C.1    Schwarz, D.2    Löhr, F.3    Schneider, B.4    Dötsch, V.5    Bernhard, F.6
  • 28
    • 3042798261 scopus 로고    scopus 로고
    • Molecular mechanisms of ligand binding, signalling, and regulation within the superfamily of G-protein-coupled receptors: molecular modelling and mutagenesis approaches to receptor structure and function
    • Kristiansen K. Molecular mechanisms of ligand binding, signalling, and regulation within the superfamily of G-protein-coupled receptors: molecular modelling and mutagenesis approaches to receptor structure and function. Pharmacol. Ther. 103 (2004) 21-80
    • (2004) Pharmacol. Ther. , vol.103 , pp. 21-80
    • Kristiansen, K.1
  • 29
    • 13844263242 scopus 로고    scopus 로고
    • Stable and functional immobilization of histidine-tagged proteins via multivalent chelator headgroups on a molecular poly(ethylene glycol) brush
    • Lata S., and Piehler J. Stable and functional immobilization of histidine-tagged proteins via multivalent chelator headgroups on a molecular poly(ethylene glycol) brush. Anal. Chem. 77 (2005) 1096-1105
    • (2005) Anal. Chem. , vol.77 , pp. 1096-1105
    • Lata, S.1    Piehler, J.2
  • 30
    • 0028850654 scopus 로고
    • Characterization of endothelin receptor subtypes in isolated rat renal preglomerular microvessels
    • De Leon H., and Garcia R. Characterization of endothelin receptor subtypes in isolated rat renal preglomerular microvessels. Regul. Pept. 60 (1995) 1-8
    • (1995) Regul. Pept. , vol.60 , pp. 1-8
    • De Leon, H.1    Garcia, R.2
  • 31
    • 0033166764 scopus 로고    scopus 로고
    • A modified protocol for fast purification of T7 RNA polymerase
    • Li Y., Wang E., and Wang Y. A modified protocol for fast purification of T7 RNA polymerase. Protein Expr. Purif. 16 (1999) 355-358
    • (1999) Protein Expr. Purif. , vol.16 , pp. 355-358
    • Li, Y.1    Wang, E.2    Wang, Y.3
  • 32
    • 0033377664 scopus 로고    scopus 로고
    • EMAN: semiautomated software for high- resolution single-particle reconstructions
    • Ludtke S.J., Baldwin P.R., and Chiu W. EMAN: semiautomated software for high- resolution single-particle reconstructions. J. Struct. Biol. 128 (1999) 82-97
    • (1999) J. Struct. Biol. , vol.128 , pp. 82-97
    • Ludtke, S.J.1    Baldwin, P.R.2    Chiu, W.3
  • 33
    • 33846145129 scopus 로고    scopus 로고
    • Lundstrom, K., Wagner, R., Reinhart, C., Desmyter, A., Cherouati, N., Magnin, T., Zeder- Lutz, G., Courtot, M., Prual, C., Andre, N., Hassaine, G., Michel, H., Cambillau, C., Pattus, F., 2006. Structural genomics on membrane proteins: comparison of more than 100 GPCRs in 3 expression systems. J. Struct. Funct. Genomics Nov 22; [Epub ahead of print, DOI 10.1007/s10969-006-9011-2].
  • 34
    • 0037450572 scopus 로고    scopus 로고
    • G protein-coupled receptor overexpression with the baculovirus-insect cell system: a tool for structural and functional studies
    • Massotte D. G protein-coupled receptor overexpression with the baculovirus-insect cell system: a tool for structural and functional studies. Biochim. Biophys. Acta 1610 (2003) 77-89
    • (2003) Biochim. Biophys. Acta , vol.1610 , pp. 77-89
    • Massotte, D.1
  • 36
    • 0026521233 scopus 로고
    • Three-dimensional reconstruction of single particles embedded in ice
    • Penczek P., Radermacher M., and Frank J. Three-dimensional reconstruction of single particles embedded in ice. Ultramicroscopy 40 (1992) 33-53
    • (1992) Ultramicroscopy , vol.40 , pp. 33-53
    • Penczek, P.1    Radermacher, M.2    Frank, J.3
  • 39
    • 0035726693 scopus 로고    scopus 로고
    • G-protein-coupled receptor dimerization: modulation of receptor function
    • Rios C.D., Jordan B.A., Gomes I., and Devi L.A. G-protein-coupled receptor dimerization: modulation of receptor function. Pharmacol. Ther. 92 (2001) 71-87
    • (2001) Pharmacol. Ther. , vol.92 , pp. 71-87
    • Rios, C.D.1    Jordan, B.A.2    Gomes, I.3    Devi, L.A.4
  • 40
    • 0036514182 scopus 로고    scopus 로고
    • Optimizing functional versus total expression of the human u-opiod receptor in Picchia pastoris
    • Sarramegna V., Demange P., Milon A., and Talmont F. Optimizing functional versus total expression of the human u-opiod receptor in Picchia pastoris. Protein Expr. Purif. 24 (2002) 212-220
    • (2002) Protein Expr. Purif. , vol.24 , pp. 212-220
    • Sarramegna, V.1    Demange, P.2    Milon, A.3    Talmont, F.4
  • 41
    • 0041876269 scopus 로고    scopus 로고
    • Heterologous expression of G-protein-coupled receptors: comparison of expression systems from the standpoint of large-scale production and purification
    • Sarramegna V., Talmont F., Demange P., and Milon A. Heterologous expression of G-protein-coupled receptors: comparison of expression systems from the standpoint of large-scale production and purification. Cell. Mol. Life Sci. 60 (2003) 1529-1546
    • (2003) Cell. Mol. Life Sci. , vol.60 , pp. 1529-1546
    • Sarramegna, V.1    Talmont, F.2    Demange, P.3    Milon, A.4
  • 42
    • 0033884343 scopus 로고    scopus 로고
    • The human ET(B) endothelin receptor heterologously produced in the methylotrophic yeast Pichia pastoris shows high-affinity binding and induction of stacked membranes
    • Schiller H., Haase W., Molsberger E., Janssen P., Michel H., and Reilander H. The human ET(B) endothelin receptor heterologously produced in the methylotrophic yeast Pichia pastoris shows high-affinity binding and induction of stacked membranes. Receptors Cannels 7 (2000) 93-107
    • (2000) Receptors Cannels , vol.7 , pp. 93-107
    • Schiller, H.1    Haase, W.2    Molsberger, E.3    Janssen, P.4    Michel, H.5    Reilander, H.6
  • 43
    • 34248563102 scopus 로고    scopus 로고
    • Preparative scale cell-free expression systems: new tools for the large scale preparation of integral membrane proteins for functional and structural studies
    • Schwarz D., Klammt C., Koglin A., Löhr F., Schneider B., Dötsch V., and Bernhard F. Preparative scale cell-free expression systems: new tools for the large scale preparation of integral membrane proteins for functional and structural studies. Methods online (2006)
    • (2006) Methods online
    • Schwarz, D.1    Klammt, C.2    Koglin, A.3    Löhr, F.4    Schneider, B.5    Dötsch, V.6    Bernhard, F.7
  • 44
    • 0024297305 scopus 로고
    • A continuous cell-free translation system capable of producing polypeptides in high yield
    • Spirin A.S., Baranov V.I., Ryabova L.A., Ovodov S.Y., and Alakhov Y.B. A continuous cell-free translation system capable of producing polypeptides in high yield. Science 242 (1988) 1162-1164
    • (1988) Science , vol.242 , pp. 1162-1164
    • Spirin, A.S.1    Baranov, V.I.2    Ryabova, L.A.3    Ovodov, S.Y.4    Alakhov, Y.B.5
  • 45
    • 0027960964 scopus 로고
    • The effect of N-linked glycosylation on activity of the Na(+)- and Cl(-)-dependent serotonin transporter expressed using recombinant baculovirus in insect cells
    • Tate C.G., and Blakely R.D. The effect of N-linked glycosylation on activity of the Na(+)- and Cl(-)-dependent serotonin transporter expressed using recombinant baculovirus in insect cells. J. Biol. Chem. 269 (1994) 26303
    • (1994) J. Biol. Chem. , vol.269 , pp. 26303
    • Tate, C.G.1    Blakely, R.D.2
  • 46
    • 0035979797 scopus 로고    scopus 로고
    • Overexpression of mammalian integral membrane proteins for structural studies
    • Tate C.G. Overexpression of mammalian integral membrane proteins for structural studies. FEBS Letts. 504 (2001) 94-98
    • (2001) FEBS Letts. , vol.504 , pp. 94-98
    • Tate, C.G.1
  • 47
    • 0348003908 scopus 로고    scopus 로고
    • Comparison of seven different heterologous protein expression systems for the production of the serotonin transporter
    • Tate C.G., Haase J., Baker C., Boorsma M., Magnani F., Vallis Y., and Williams D.C. Comparison of seven different heterologous protein expression systems for the production of the serotonin transporter. Biochim. Biophys. Acta 1610 (2003) 141-153
    • (2003) Biochim. Biophys. Acta , vol.1610 , pp. 141-153
    • Tate, C.G.1    Haase, J.2    Baker, C.3    Boorsma, M.4    Magnani, F.5    Vallis, Y.6    Williams, D.C.7
  • 48
    • 11244300993 scopus 로고    scopus 로고
    • Efficient protocol of isotopically labelled proteins by cell-free synthesis: a practical protocol
    • Torizawa T., Shimizu M., Taoka M., Miyano H., and Kainosho M. Efficient protocol of isotopically labelled proteins by cell-free synthesis: a practical protocol. J. Biomol. NMR 30 (2004) 311-325
    • (2004) J. Biomol. NMR , vol.30 , pp. 311-325
    • Torizawa, T.1    Shimizu, M.2    Taoka, M.3    Miyano, H.4    Kainosho, M.5
  • 50
    • 0029838532 scopus 로고    scopus 로고
    • Purification of a rat neurotensin receptor expressed in Escherichia coli
    • Tucker J., and Grisshammer R. Purification of a rat neurotensin receptor expressed in Escherichia coli. Biochem. J. 317 (1996) 891-899
    • (1996) Biochem. J. , vol.317 , pp. 891-899
    • Tucker, J.1    Grisshammer, R.2
  • 52
    • 0032506160 scopus 로고    scopus 로고
    • Truncated V2 vasopressin receptors as negative regulators of wild-type V2 receptor function
    • Zhu X., and Wess J. Truncated V2 vasopressin receptors as negative regulators of wild-type V2 receptor function. Biochemistry 37 (1998) 15773-15778
    • (1998) Biochemistry , vol.37 , pp. 15773-15778
    • Zhu, X.1    Wess, J.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.