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Volumn 3, Issue , 2013, Pages

Membrane driven spatial organization of GPCRs

Author keywords

[No Author keywords available]

Indexed keywords

1-PALMITOYL-2-OLEOYLPHOSPHATIDYLCHOLINE; BETA 1 ADRENERGIC RECEPTOR; BETA 2 ADRENERGIC RECEPTOR; CHOLESTEROL; LIPID BILAYER; PHOSPHATIDYLCHOLINE;

EID: 84885465776     PISSN: None     EISSN: 20452322     Source Type: Journal    
DOI: 10.1038/srep02909     Document Type: Article
Times cited : (95)

References (60)
  • 1
    • 80052967337 scopus 로고    scopus 로고
    • Multiple ligand-specific conformations of the b2-adrenergic receptor
    • Kahsai, A. W. et al. Multiple ligand-specific conformations of the b2-adrenergic receptor. Nat. Chem. Biol. 7, 692-700 (2011).
    • (2011) Nat. Chem. Biol. , vol.7 , pp. 692-700
    • Kahsai, A.W.1
  • 3
    • 66249144426 scopus 로고    scopus 로고
    • The structure and function of G-protein-coupled receptors
    • Rosenbaum, D. M., Rasmussen, S. G. F. & Kobilka, B. K. The structure and function of G-protein-coupled receptors. Nature 459, 356-363 (2009).
    • (2009) Nature , vol.459 , pp. 356-363
    • Rosenbaum, D.M.1    Rasmussen, S.G.F.2    Kobilka, B.K.3
  • 4
    • 84872221774 scopus 로고    scopus 로고
    • Structure-function of the G proteincoupled receptor superfamily
    • Katritch, V., Cherezov, V. & Stevens, R. C. Structure-function of the G proteincoupled receptor superfamily. Annu. Rev. Pharmacol. Toxicol. 53, 531-556 (2012).
    • (2012) Annu. Rev. Pharmacol. Toxicol , vol.53 , pp. 531-556
    • Katritch, V.1    Cherezov, V.2    Stevens, R.C.3
  • 5
    • 47949129742 scopus 로고    scopus 로고
    • Structure of a beta1-adrenergic G-protein-coupled receptor
    • Warne, T. et al. Structure of a beta1-adrenergic G-protein-coupled receptor. Nature 454, 486-491 (2008).
    • (2008) Nature , vol.454 , pp. 486-491
    • Warne, T.1
  • 7
    • 84861165939 scopus 로고    scopus 로고
    • Liganddependent conformations and dynamics of the serotonin 5-HT2A receptor determine its activation and membrane-driven oligomerization properties
    • Shan, J., Khelashvili, G., Mondal, S., Mehler, E. L. & Weinstein, H. Liganddependent conformations and dynamics of the serotonin 5-HT2A receptor determine its activation and membrane-driven oligomerization properties. PLoS Comput. Biol. 8, e1002473 (2012).
    • (2012) PLoS Comput. Biol , vol.8
    • Shan, J.1    Khelashvili, G.2    Mondal, S.3    Mehler, E.L.4    Weinstein, H.5
  • 9
    • 69249158290 scopus 로고    scopus 로고
    • Allosteric communication between protomers of dopamine class A GPCR dimers modulates activation
    • Han, Y., Moreira, I. S., Urizar, E., Weinstein, H. & Javitch, J. A. Allosteric communication between protomers of dopamine class A GPCR dimers modulates activation. Nat. Chem. Biol. 5, 688-695 (2009).
    • (2009) Nat. Chem. Biol , vol.5 , pp. 688-695
    • Han, Y.1    Moreira, I.S.2    Urizar, E.3    Weinstein, H.4    Javitch, J.A.5
  • 10
    • 84875725399 scopus 로고    scopus 로고
    • Asymmetry of the rhodopsin dimer in complex with transducin
    • Jastrzebska, B., Orban, T., Golczak, M., Engel, A. & Palczewski, K. Asymmetry of the rhodopsin dimer in complex with transducin. FASEB J. 27, 1572-1584 (2013).
    • (2013) FASEB J , vol.27 , pp. 1572-1584
    • Jastrzebska, B.1    Orban, T.2    Golczak, M.3    Engel, A.4    Palczewski, K.5
  • 11
    • 84876734275 scopus 로고    scopus 로고
    • The rhodopsin-transducin complex houses two distinct rhodopsin molecules
    • Jastrzebska, B., Ringler, P., Palczewski, K. & Engel, A. The rhodopsin-transducin complex houses two distinct rhodopsin molecules. J. Struct. Biol. 182, 164-172 (2013).
    • (2013) J. Struct. Biol , vol.182 , pp. 164-172
    • Jastrzebska, B.1    Ringler, P.2    Palczewski, K.3    Engel, A.4
  • 13
    • 76649114492 scopus 로고    scopus 로고
    • Rescue of defective Gprotein-coupled receptor function in vivo by intermolecular cooperation
    • Rivero-Muller, A. et al. Rescue of defective Gprotein-coupled receptor function in vivo by intermolecular cooperation. Sci. Signal. 107, 2319-2324 (2010).
    • (2010) Sci. Signal , vol.107 , pp. 2319-2324
    • Rivero-Muller, A.1
  • 15
    • 84857840913 scopus 로고    scopus 로고
    • Rhodopsin forms a dimer with cytoplasmic helix 8 contacts in native membranes
    • Knepp, A. M., Periole, X., Marrink, S. J., Sakmar, T. P. & Huber, T. Rhodopsin forms a dimer with cytoplasmic helix 8 contacts in native membranes. Biochemistry 51, 1819-1821 (2012).
    • (2012) Biochemistry , vol.51 , pp. 1819-1821
    • Knepp, A.M.1    Periole, X.2    Marrink, S.J.3    Sakmar, T.P.4    Huber, T.5
  • 16
    • 77955262698 scopus 로고    scopus 로고
    • Lessons from free energy simulations of delta opioid receptor homodimers involving the fourth transmembrane helix
    • Provasi, D., Johnston, J. M. & Filizola, M. Lessons from free energy simulations of delta opioid receptor homodimers involving the fourth transmembrane helix. Biochemistry 49, 6771-6776 (2010).
    • (2010) Biochemistry , vol.49 , pp. 6771-6776
    • Provasi, D.1    Johnston, J.M.2    Filizola, M.3
  • 17
    • 84863535732 scopus 로고    scopus 로고
    • Structural determinants of the supramolecular organization of G protein-coupled receptors in bilayers
    • Periole, X., Knepp, A. M., Sakmar, T. P., Marrink, S. J. & Huber, T. Structural determinants of the supramolecular organization of G protein-coupled receptors in bilayers. J. Am. Chem. Soc. 134, 10959-10965 (2012).
    • (2012) J. Am. Chem. Soc , vol.134 , pp. 10959-10965
    • Periole, X.1    Knepp, A.M.2    Sakmar, T.P.3    Marrink, S.J.4    Huber, T.5
  • 18
    • 79952393275 scopus 로고    scopus 로고
    • Making structural sense of dimerization interfaces of delta opioid receptor homodimers
    • Johnston, J. M. et al. Making structural sense of dimerization interfaces of delta opioid receptor homodimers. Biochemistry 50, 1682-1690 (2011).
    • (2011) Biochemistry , vol.50 , pp. 1682-1690
    • Johnston, J.M.1
  • 19
    • 21344467203 scopus 로고    scopus 로고
    • The study of G-protein coupled receptor oligomerization with computational modeling and bioinformatics
    • DOI 10.1111/j.1742-4658.2005.04730.x
    • Filizola, M. & Weinstein, H. The study of G protein coupled receptor oligomerization with computational modeling and bioinformatics. FEBS J. 272, 2926-2938 (2005). (Pubitemid 40904681)
    • (2005) FEBS Journal , vol.272 , Issue.12 , pp. 2926-2938
    • Filizola, M.1    Weinstein, H.2
  • 20
    • 76049124690 scopus 로고    scopus 로고
    • Lipid bilayer regulation of membrane protein function: Gramicidin channels as molecular force probes
    • Lundbaek, J. A., Collingwood, S. A., Ingelfsson, H. I., Kapoor, R. &Andersen,O. S. Lipid bilayer regulation of membrane protein function: gramicidin channels as molecular force probes. J. R. Soc. Interface 7, 373-395 (2010).
    • (2010) J. R. Soc. Interface , vol.7 , pp. 373-395
    • Lundbaek, J.A.1    Collingwood, S.A.2    Ingelfsson, H.I.3    Kapoor, R.4    Andersen, O.S.5
  • 21
    • 33845505655 scopus 로고    scopus 로고
    • Curvature and Hydrophobic forces drive oligomerization and modulate activity of rhodopsin in membranes
    • DOI 10.1529/biophysj.106.082776
    • Botelho, A. V. r., Huber, T., Sakmar, T. P. & Brown, M. F. Curvature and hydrophobic forces drive oligomerization and modulate activity of rhodopsin in membranes. Biophys. J. 91, 4464-4477 (2006). (Pubitemid 44911035)
    • (2006) Biophysical Journal , vol.91 , Issue.12 , pp. 4464-4477
    • Botelho, A.V.1    Huber, T.2    Sakmar, T.P.3    Brown, M.F.4
  • 22
    • 34548146523 scopus 로고    scopus 로고
    • G protein-coupled receptors self-assemble in dynamics simulations of model bilayers
    • DOI 10.1021/ja0706246
    • Periole, X., Huber, T., Marrink, S. J. & Sakmar, T. P. G protein-coupled receptors self-assemble in dynamics simulations of model bilayers. J. Am. Chem. Soc 129, 10126-10132 (2007). (Pubitemid 47312953)
    • (2007) Journal of the American Chemical Society , vol.129 , Issue.33 , pp. 10126-10132
    • Periole, X.1    Huber, T.2    Marrink, S.-J.3    Sakmar, T.P.4
  • 23
    • 80455164853 scopus 로고    scopus 로고
    • Quantitative modeling of membrane deformations by multihelical membrane proteins: Application to G-protein coupled receptors
    • Mondal, S., Khelashvili, G., Shan, J., Andersen, O. S. & Weinstein,H. Quantitative modeling of membrane deformations by multihelical membrane proteins: application to G-protein coupled receptors. Biophys. J. 101, 2092-2101 (2011).
    • (2011) Biophys. J , vol.101 , pp. 2092-2101
    • Mondal, S.1    Khelashvili, G.2    Shan, J.3    Andersen, O.S.4    Weinsteinh5
  • 24
    • 43849083897 scopus 로고    scopus 로고
    • Energetics of hydrophobic matching in lipid-protein interactions
    • Marsh, D. Energetics of hydrophobic matching in lipid-protein interactions. Biophys. J. 94, 3996-4013 (2008).
    • (2008) Biophys. J. , vol.94 , pp. 3996-4013
    • Marsh, D.1
  • 25
    • 84876416484 scopus 로고    scopus 로고
    • The cost of living in the membrane: A case study of hydrophobic mismatch for the multi-segment protein LeuT
    • Mondal, S., Khelashvili, G., Shi, L. & Weinstein, H. The cost of living in the membrane: a case study of hydrophobic mismatch for the multi-segment protein LeuT. Chem. Phys. Lipids 169, 27-38 (2013).
    • (2013) Chem. Phys. Lipids , vol.169 , pp. 27-38
    • Mondal, S.1    Khelashvili, G.2    Shi, L.3    Weinstein, H.4
  • 27
    • 84876197291 scopus 로고    scopus 로고
    • Crystal structure of oligomeric beta1-adrenergic G protein coupled receptors in ligand-free basal state
    • Huang, J., Chen, S., Zhang, J. J. & Huang, X.-Y. Crystal structure of oligomeric beta1-adrenergic G protein coupled receptors in ligand-free basal state. Nat. Struct. Mol. Biol. 20, 419-425 (2013).
    • (2013) Nat. Struct. Mol. Biol , vol.20 , pp. 419-425
    • Huang, J.1    Chen, S.2    Zhang, J.J.3    Huang, X.-Y.4
  • 28
    • 70350752293 scopus 로고    scopus 로고
    • Ligand-regulated oligomerization of b2-adrenoceptors in a model lipid bilayer
    • Fung, J. J. et al. Ligand-regulated oligomerization of b2-adrenoceptors in a model lipid bilayer. EMBO J. 28, 3315-3328 (2009).
    • (2009) EMBO J , vol.28 , pp. 3315-3328
    • Fung, J.J.1
  • 29
    • 84866056455 scopus 로고    scopus 로고
    • Assessing the relative stability of dimer interfaces in G protein-coupled receptors
    • Johnston, J.M., Wang, H., Provasi, D. &Filizola, M. Assessing the relative stability of dimer interfaces in G protein-coupled receptors. PLoS Comput. Biol. 8, e1002649 (2012).
    • (2012) PLoS Comput. Biol. , vol.8
    • Johnston, J.M.1    Wang, H.2    Provasi, D.3    Filizola, M.4
  • 31
    • 84872195772 scopus 로고    scopus 로고
    • Single-molecule analysis of fluorescently labeled G-protein coupled receptors reveals complexes with distinct dynamics and organization
    • Calebiro, D. et al. Single-molecule analysis of fluorescently labeled G-protein coupled receptors reveals complexes with distinct dynamics and organization. Proc. Natl. Acad. Sci. USA 110, 743-748 (2013).
    • (2013) Proc. Natl. Acad. Sci. USA , vol.110 , pp. 743-748
    • Calebiro, D.1
  • 32
    • 77956762740 scopus 로고    scopus 로고
    • Cholesterol modulates the membrane effects and spatial organization of membranepenetrating ligands for G-protein coupled receptors
    • Khelashvili, G., Mondal, S., Andersen, O. S. & Weinstein, H. Cholesterol modulates the membrane effects and spatial organization of membranepenetrating ligands for G-protein coupled receptors. J. Phys. Chem. B 114, 12046-12057 (2010).
    • (2010) J. Phys. Chem B , vol.114 , pp. 12046-12057
    • Khelashvili, G.1    Mondal, S.2    Andersen, O.S.3    Weinstein, H.4
  • 35
    • 0034731376 scopus 로고    scopus 로고
    • Differential targeting of b2-adrenergic receptor subtypes and adenylyl cyclase to cardiomyocyte caveolae
    • Rybin, V. O., Xu, X., Lisanti, M. P. & Steinberg, S. F. Differential targeting of b2-adrenergic receptor subtypes and adenylyl cyclase to cardiomyocyte caveolae. J. Biol. Chem. 275, 41447-41457 (2000).
    • (2000) J. Biol. Chem , vol.275 , pp. 41447-41457
    • Rybin, V.O.1    Xu, X.2    Lisanti, M.P.3    Steinberg, S.F.4
  • 36
    • 77957055780 scopus 로고
    • Integrated methods for the construction of three-dimensional models and computational probing of structure-function relations in G protein-coupled receptors
    • Ballesteros, J. A. & Weinstein, H. Integrated methods for the construction of three-dimensional models and computational probing of structure-function relations in G protein-coupled receptors. Methods Neurosci. 25, 366-428 (1995).
    • (1995) Methods Neurosci , vol.25 , pp. 366-428
    • Ballesteros, J.A.1    Weinstein, H.2
  • 37
    • 0037050575 scopus 로고    scopus 로고
    • Positioning and stabilization of dynorphin peptides in membrane bilayers: The mechanistic role of aromatic and basic residues revealed from comparative MD simulations
    • DOI 10.1021/jp012174o
    • Sankararamakrishnan, R. & Weinstein, H. Positioning and stabilization of dynorphin peptides in membrane bilayers: the mechanistic role of aromatic and basic residues revealed from comparative MD simulations. J. Phys. Chem. B 106, 209-218 (2002). (Pubitemid 35263217)
    • (2002) Journal of Physical Chemistry B , vol.106 , Issue.1 , pp. 209-218
    • Sankararamakrishnan, R.1    Weinstein, H.2
  • 38
    • 77249150932 scopus 로고    scopus 로고
    • Formation and dissociation of M1 muscarinic receptor dimers seen by total internal reflection fluorescence imaging of single molecules
    • Hern, J. A. et al. Formation and dissociation of M1 muscarinic receptor dimers seen by total internal reflection fluorescence imaging of single molecules. Proc. Natl. Acad. Sci. USA 107, 2693-2698 (2010).
    • (2010) Proc. Natl. Acad. Sci. USA , vol.107 , pp. 2693-2698
    • Hern, J.A.1
  • 39
    • 77953672210 scopus 로고    scopus 로고
    • GPCR dimers fall apart
    • Lambert, N. A. GPCR dimers fall apart. Sci. Signal. 3, pe12 (2010).
    • (2010) Sci. Signal , vol.3
    • Lambert, N.A.1
  • 40
    • 66849132354 scopus 로고    scopus 로고
    • Instability of a class A G protein-coupled receptor oligomer interface
    • Fonseca, J. M. & Lambert, N. A. Instability of a class A G protein-coupled receptor oligomer interface. Mol. Pharmacol. 75, 1296-1299 (2009).
    • (2009) Mol. Pharmacol , vol.75 , pp. 1296-1299
    • Fonseca, J.M.1    Lambert, N.A.2
  • 41
    • 79551711208 scopus 로고    scopus 로고
    • Full characterization of GPCR monomer-dimer dynamic equilibrium by single molecule imaging
    • Kasai, R. S. et al. Full characterization of GPCR monomer-dimer dynamic equilibrium by single molecule imaging. J. Cell Biol. 192, 463 (2011).
    • (2011) J. Cell Biol , vol.192 , pp. 463
    • Kasai, R.S.1
  • 43
    • 21344433619 scopus 로고    scopus 로고
    • Methods to monitor the quaternary structure of G protein-coupled receptors
    • DOI 10.1111/j.1742-4658.2005.04731.x
    • Milligan, G. & Bouvier, M. Methods to monitor the quaternary structure of G protein-coupled receptors. FEBS J. 272, 2914-2925 (2005). (Pubitemid 40904680)
    • (2005) FEBS Journal , vol.272 , Issue.12 , pp. 2914-2925
    • Milligan, G.1    Bouvier, M.2
  • 45
    • 61549138107 scopus 로고    scopus 로고
    • Constitutive dimerization of the G-protein coupled receptor, neurotensin receptor 1, reconstituted into phospholipid bilayers
    • Harding, P. J. et al. Constitutive dimerization of the G-protein coupled receptor, neurotensin receptor 1, reconstituted into phospholipid bilayers. Biophys. J. 96, 964-973 (2009).
    • (2009) Biophys. J , vol.96 , pp. 964-973
    • Harding, P.J.1
  • 47
    • 0032552880 scopus 로고    scopus 로고
    • The preference of tryptophan for membrane interfaces
    • DOI 10.1021/bi980809c
    • Yau, W. M., Wimley, W. C., Gawrisch, K. & White, S. H. The preference of tryptophan for membrane interfaces. Biochemistry 37, 14713-14718 (1998). (Pubitemid 28487579)
    • (1998) Biochemistry , vol.37 , Issue.42 , pp. 14713-14718
    • Yau, W.-M.1    Wimley, W.C.2    Gawrisch, K.3    White, S.H.4
  • 48
    • 0021755525 scopus 로고
    • Intrahelical hydrogen bonding of serine, threonine and cysteine residues within alpha-helices and its relevance to membrane-bound proteins
    • Gray, T. M. &Matthews, B. W. Intrahelical hydrogen bonding of serine, threonine and cysteine residues within alpha-helices and its relevance to membrane-bound proteins. J. Mol. Biol. 175, 75-81 (1984).
    • (1984) J. Mol. Biol , vol.175 , pp. 75-81
    • Gray, T.M.1    Matthews, B.W.2
  • 49
    • 0029669955 scopus 로고    scopus 로고
    • Free-energy determinants of alpha-helix insertion into lipid bilayers
    • Ben-Tal, N., Ben-Shaul, A., Nicholls, A. & Honig, B. Free-energy determinants of alpha-helix insertion into lipid bilayers. Biophys. J. 70, 1803-1812 (1996).
    • (1996) Biophys. J , vol.70 , pp. 1803-1812
    • Ben-Tal, N.1    Ben-Shaul, A.2    Nicholls, A.3    Honig, B.4
  • 50
    • 84986483798 scopus 로고
    • The double cubic lattice method: Efficient approaches to numerical integration of surface area and volume and to dot surface contouring of molecular assemblies
    • Eisenhaber, F., Lijnzaad, P., Argos, P., Sander, C. & Scharf, M. The double cubic lattice method: efficient approaches to numerical integration of surface area and volume and to dot surface contouring of molecular assemblies. J. Comput. Chem. 16, 273-284 (1995).
    • (1995) J. Comput. Chem , vol.16 , pp. 273-284
    • Eisenhaber, F.1    Lijnzaad, P.2    Argos, P.3    Sander, C.4    Scharf, M.5
  • 51
    • 0023018907 scopus 로고
    • Deformation free energy of bilayer membrane and its effect on gramicidin channel lifetime
    • Huang, H. W. Deformation free energy of bilayer membrane and its effect on gramicidin channel lifetime. Biophys. J. 50, 1061-1070 (1986). (Pubitemid 17205992)
    • (1986) Biophysical Journal , vol.50 , Issue.6 , pp. 1061-1070
    • Huang, H.W.1
  • 52
    • 0031895461 scopus 로고    scopus 로고
    • Energetics of inclusion-induced bilayer deformations
    • Nielsen, C.,Goulian,M. & Andersen,O. S. Energetics of inclusion-induced bilayer deformations. Biophys. J. 74, 1966-1983 (1998).
    • (1998) Biophys. J , vol.74 , pp. 1966-1983
    • Nielsen, C.1    Goulian, M.2    Andersen, O.S.3
  • 53
    • 0033932837 scopus 로고    scopus 로고
    • Effect of chain length and unsaturation on elasticity of lipid bilayers
    • Rawicz, W., Olbrich, K. C.,McIntosh, T., Needham, D. & Evans, E. Effect of chain length and unsaturation on elasticity of lipid bilayers. Biophys. J. 79, 328-339 (2000). (Pubitemid 30436749)
    • (2000) Biophysical Journal , vol.79 , Issue.1 , pp. 328-339
    • Rawicz, W.1    Olbrich, K.C.2    McIntosh, T.3    Needham, D.4    Evans, E.5
  • 54
    • 0030949722 scopus 로고    scopus 로고
    • The influence of cholesterol on phospholipid membrane curvature and bending elasticity
    • Chen, Z. & Rand, R. P. The influence of cholesterol on phospholipid membrane curvature and bending elasticity. Biophys. J. 73, 267-276 (1997). (Pubitemid 27274124)
    • (1997) Biophysical Journal , vol.73 , Issue.1 , pp. 267-276
    • Chen, Z.1    Rand, R.P.2
  • 56
    • 49449113010 scopus 로고    scopus 로고
    • The MARTINI coarse-grained force field: Extension to proteins
    • Monticelli, L. et al. The MARTINI coarse-grained force field: extension to proteins. J Chem. Theory Comput. 4, 819-834 (2008).
    • (2008) J Chem. Theory Comput. , vol.4 , pp. 819-834
    • Monticelli, L.1
  • 58
    • 84866698760 scopus 로고    scopus 로고
    • Why GPCRs behave differently in cubic and lamellar lipidic mesophases
    • Khelashvili, G. et al. Why GPCRs behave differently in cubic and lamellar lipidic mesophases. J. Am. Chem. Soc. 134, 15858-15868 (2012).
    • (2012) J. Am. Chem. Soc , vol.134 , pp. 15858-15868
    • Khelashvili, G.1
  • 59
    • 84872142909 scopus 로고    scopus 로고
    • Improved parameters for the Martini coarse-grained protein force field
    • de Jong, D. H. et al. Improved parameters for the Martini coarse-grained protein force field. J Chem. Theory Comput. 9, 687-697 (2012).
    • (2012) J Chem. Theory Comput , vol.9 , pp. 687-697
    • De Jong, D.H.1
  • 60
    • 51949088673 scopus 로고    scopus 로고
    • Lipid-rhodopsin hydrophobic mismatch alters rhodopsin helical content
    • Soubias, O., Niu, S. L., Mitchell, D. C. & Gawrisch, K. Lipid-rhodopsin hydrophobic mismatch alters rhodopsin helical content. J. Am. Chem. Soc. 130, 12465-12471 (2008).
    • (2008) J. Am. Chem. Soc , vol.130 , pp. 12465-12471
    • Soubias, O.1    Niu, S.L.2    Mitchell, D.C.3    Gawrisch, K.4


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