메뉴 건너뛰기




Volumn 27, Issue 1, 2014, Pages 129-137

Structured and disordered facets of the GPCR fold

Author keywords

[No Author keywords available]

Indexed keywords

CYTOSOL RECEPTOR; FRIZZLED PROTEIN; G PROTEIN COUPLED RECEPTOR; METABOTROPIC RECEPTOR; RHODOPSIN LIKE RECEPTOR; SECRETIN LIKE RECEPTOR; UNCLASSIFIED DRUG; RHODOPSIN; SECRETIN;

EID: 84908054224     PISSN: 0959440X     EISSN: 1879033X     Source Type: Journal    
DOI: 10.1016/j.sbi.2014.08.002     Document Type: Review
Times cited : (66)

References (84)
  • 2
    • 42149181885 scopus 로고    scopus 로고
    • Structural diversity of G protein-coupled receptors and significance for drug discovery
    • Lagerstrom M.C., Schioth H.B. Structural diversity of G protein-coupled receptors and significance for drug discovery. Nat Rev Drug Discov 2008, 7:339-357.
    • (2008) Nat Rev Drug Discov , vol.7 , pp. 339-357
    • Lagerstrom, M.C.1    Schioth, H.B.2
  • 3
    • 78650150896 scopus 로고    scopus 로고
    • International Union of Basic and Clinical Pharmacology. LXXX. The class Frizzled receptors
    • Schulte G. International Union of Basic and Clinical Pharmacology. LXXX. The class Frizzled receptors. Pharmacol Rev 2010, 62:632-667.
    • (2010) Pharmacol Rev , vol.62 , pp. 632-667
    • Schulte, G.1
  • 5
    • 67149136711 scopus 로고    scopus 로고
    • Passing the baton in class B GPCRs: peptide hormone activation via helix induction?
    • Parthier C., Reedtz-Runge S., Rudolph R., Stubbs M.T. Passing the baton in class B GPCRs: peptide hormone activation via helix induction?. Trends Biochem Sci 2009, 34:303-310.
    • (2009) Trends Biochem Sci , vol.34 , pp. 303-310
    • Parthier, C.1    Reedtz-Runge, S.2    Rudolph, R.3    Stubbs, M.T.4
  • 6
    • 0038662595 scopus 로고    scopus 로고
    • Evolution, structure, and activation mechanism of family 3/C G-protein-coupled receptors
    • Pin J.P., Galvez T., Prezeau L. Evolution, structure, and activation mechanism of family 3/C G-protein-coupled receptors. Pharmacol Ther 2003, 98:325-354.
    • (2003) Pharmacol Ther , vol.98 , pp. 325-354
    • Pin, J.P.1    Galvez, T.2    Prezeau, L.3
  • 13
    • 17644405396 scopus 로고    scopus 로고
    • G protein-coupled receptors show unusual patterns of intrinsic unfolding
    • Jaakola V.P., Prilusky J., Sussman J.L., Goldman A. G protein-coupled receptors show unusual patterns of intrinsic unfolding. Protein Eng Des Sel 2005, 18:103-110.
    • (2005) Protein Eng Des Sel , vol.18 , pp. 103-110
    • Jaakola, V.P.1    Prilusky, J.2    Sussman, J.L.3    Goldman, A.4
  • 16
    • 84866463338 scopus 로고    scopus 로고
    • Structural biology. Versatility from protein disorder
    • Babu M.M., Kriwacki R.W., Pappu R.V. Structural biology. Versatility from protein disorder. Science 2012, 337:1460-1461.
    • (2012) Science , vol.337 , pp. 1460-1461
    • Babu, M.M.1    Kriwacki, R.W.2    Pappu, R.V.3
  • 19
    • 84861434240 scopus 로고    scopus 로고
    • Shifting hydrogen bonds may produce flexible transmembrane helices
    • Cao Z., Bowie J.U. Shifting hydrogen bonds may produce flexible transmembrane helices. Proc Natl Acad Sci U S A 2012, 109:8121-8126.
    • (2012) Proc Natl Acad Sci U S A , vol.109 , pp. 8121-8126
    • Cao, Z.1    Bowie, J.U.2
  • 20
    • 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 1995, 25:366-428.
    • (1995) Methods Neurosci , vol.25 , pp. 366-428
    • Ballesteros, J.A.1    Weinstein, H.2
  • 21
    • 67651173221 scopus 로고    scopus 로고
    • A highly conserved tryptophan residue in the fourth transmembrane domain of the A adenosine receptor is essential for ligand binding but not receptor homodimerization
    • Suzuki T., Namba K., Yamagishi R., Kaneko H., Haga T., Nakata H. A highly conserved tryptophan residue in the fourth transmembrane domain of the A adenosine receptor is essential for ligand binding but not receptor homodimerization. J Neurochem 2009, 110:1352-1362.
    • (2009) J Neurochem , vol.110 , pp. 1352-1362
    • Suzuki, T.1    Namba, K.2    Yamagishi, R.3    Kaneko, H.4    Haga, T.5    Nakata, H.6
  • 26
    • 84890023965 scopus 로고    scopus 로고
    • Genetically encoded chemical probes in cells reveal the binding path of urocortin-I to CRF class B GPCR
    • Coin I., Katritch V., Sun T., Xiang Z., Siu F.Y., Beyermann M., Stevens R.C., Wang L. Genetically encoded chemical probes in cells reveal the binding path of urocortin-I to CRF class B GPCR. Cell 2013, 155:1258-1269.
    • (2013) Cell , vol.155 , pp. 1258-1269
    • Coin, I.1    Katritch, V.2    Sun, T.3    Xiang, Z.4    Siu, F.Y.5    Beyermann, M.6    Stevens, R.C.7    Wang, L.8
  • 29
    • 84896268722 scopus 로고    scopus 로고
    • Designer receptor manipulations reveal a role of the locus coeruleus noradrenergic system in isoflurane general anesthesia
    • Vazey E.M., Aston-Jones G. Designer receptor manipulations reveal a role of the locus coeruleus noradrenergic system in isoflurane general anesthesia. Proc Natl Acad Sci U S A 2014, 111:3859-3864.
    • (2014) Proc Natl Acad Sci U S A , vol.111 , pp. 3859-3864
    • Vazey, E.M.1    Aston-Jones, G.2
  • 30
    • 49449090028 scopus 로고    scopus 로고
    • Structural plasticity in G-protein coupled receptors as demonstrated by the allosteric actions of homocysteine and computer-assisted analysis of disordered domains
    • Agnati L.F., Leo G., Genedani S., Andreoli N., Marcellino D., Woods A., Piron L., Guidolin D., Fuxe K. Structural plasticity in G-protein coupled receptors as demonstrated by the allosteric actions of homocysteine and computer-assisted analysis of disordered domains. Brain Res Rev 2008, 58:459-474.
    • (2008) Brain Res Rev , vol.58 , pp. 459-474
    • Agnati, L.F.1    Leo, G.2    Genedani, S.3    Andreoli, N.4    Marcellino, D.5    Woods, A.6    Piron, L.7    Guidolin, D.8    Fuxe, K.9
  • 31
    • 84856511452 scopus 로고    scopus 로고
    • Domain coupling in GPCRs: the engine for induced conformational changes
    • Unal H., Karnik S.S. Domain coupling in GPCRs: the engine for induced conformational changes. Trends Pharmacol Sci 2012, 33:79-88.
    • (2012) Trends Pharmacol Sci , vol.33 , pp. 79-88
    • Unal, H.1    Karnik, S.S.2
  • 32
    • 0037452868 scopus 로고    scopus 로고
    • Sequence analyses of G-protein-coupled receptors: similarities to rhodopsin
    • Mirzadegan T., Benko G., Filipek S., Palczewski K. Sequence analyses of G-protein-coupled receptors: similarities to rhodopsin. Biochemistry 2003, 42:2759-2767.
    • (2003) Biochemistry , vol.42 , pp. 2759-2767
    • Mirzadegan, T.1    Benko, G.2    Filipek, S.3    Palczewski, K.4
  • 33
    • 84902765269 scopus 로고    scopus 로고
    • Role of the third intracellular loop in the subtype-specific internalization and recycling of muscarinic M2 and M4 receptors
    • Yoshida N., Jojima E., Saito H., Haga T. Role of the third intracellular loop in the subtype-specific internalization and recycling of muscarinic M2 and M4 receptors. Biomed Res 2014, 35:185-192.
    • (2014) Biomed Res , vol.35 , pp. 185-192
    • Yoshida, N.1    Jojima, E.2    Saito, H.3    Haga, T.4
  • 34
    • 77957778459 scopus 로고    scopus 로고
    • Molecular basis for activation of G protein-coupled receptor kinases
    • Boguth C.A., Singh P., Huang C.C., Tesmer J.J. Molecular basis for activation of G protein-coupled receptor kinases. EMBO J 2010, 29:3249-3259.
    • (2010) EMBO J , vol.29 , pp. 3249-3259
    • Boguth, C.A.1    Singh, P.2    Huang, C.C.3    Tesmer, J.J.4
  • 37
    • 14644435825 scopus 로고    scopus 로고
    • Intrinsically unstructured proteins and their functions
    • Dyson H.J., Wright P.E. Intrinsically unstructured proteins and their functions. Nat Rev Mol Cell Biol 2005, 6:197-208.
    • (2005) Nat Rev Mol Cell Biol , vol.6 , pp. 197-208
    • Dyson, H.J.1    Wright, P.E.2
  • 40
    • 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. Nat Rev Mol Cell Biol 2009, 10:819-830.
    • (2009) Nat Rev Mol Cell Biol , vol.10 , pp. 819-830
    • Ritter, S.L.1    Hall, R.A.2
  • 41
    • 84902446852 scopus 로고    scopus 로고
    • Short linear motifs: ubiquitous and functionally diverse protein interaction modules directing cell regulation
    • Van Roey K., Uyar B., Weatheritt R.J., Dinkel H., Seiler M., Budd A., Gibson T.J., Davey N.E. Short linear motifs: ubiquitous and functionally diverse protein interaction modules directing cell regulation. Chem Rev 2014, 114:6733-6778.
    • (2014) Chem Rev , vol.114 , pp. 6733-6778
    • Van Roey, K.1    Uyar, B.2    Weatheritt, R.J.3    Dinkel, H.4    Seiler, M.5    Budd, A.6    Gibson, T.J.7    Davey, N.E.8
  • 42
    • 27144464910 scopus 로고    scopus 로고
    • Flexible nets. The roles of intrinsic disorder in protein interaction networks
    • Dunker A.K., Cortese M.S., Romero P., Iakoucheva L.M., Uversky V.N. Flexible nets. The roles of intrinsic disorder in protein interaction networks. FEBS J 2005, 272:5129-5148.
    • (2005) FEBS J , vol.272 , pp. 5129-5148
    • Dunker, A.K.1    Cortese, M.S.2    Romero, P.3    Iakoucheva, L.M.4    Uversky, V.N.5
  • 44
    • 84904469894 scopus 로고    scopus 로고
    • A million peptide motifs for the molecular biologist
    • Tompa P.D.N., Gibson T., Babu M.M. A million peptide motifs for the molecular biologist. Mol Cell 2014.
    • (2014) Mol Cell
    • Tompa, P.D.N.1    Gibson, T.2    Babu, M.M.3
  • 45
    • 70349996473 scopus 로고    scopus 로고
    • ANCHOR: web server for predicting protein binding regions in disordered proteins
    • Dosztanyi Z., Meszaros B., Simon I. ANCHOR: web server for predicting protein binding regions in disordered proteins. Bioinformatics 2009, 25:2745-2746.
    • (2009) Bioinformatics , vol.25 , pp. 2745-2746
    • Dosztanyi, Z.1    Meszaros, B.2    Simon, I.3
  • 46
    • 1842866233 scopus 로고    scopus 로고
    • AKAPs (A-kinase anchoring proteins) and molecules that compose their G-protein-coupled receptor signalling complexes
    • Malbon C.C., Tao J., Wang H.Y. AKAPs (A-kinase anchoring proteins) and molecules that compose their G-protein-coupled receptor signalling complexes. Biochem J 2004, 379:1-9.
    • (2004) Biochem J , vol.379 , pp. 1-9
    • Malbon, C.C.1    Tao, J.2    Wang, H.Y.3
  • 47
    • 47849101639 scopus 로고    scopus 로고
    • Location, location, location.site-specific GPCR phosphorylation offers a mechanism for cell-type-specific signalling
    • Tobin A.B., Butcher A.J., Kong K.C. Location, location, location.site-specific GPCR phosphorylation offers a mechanism for cell-type-specific signalling. Trends Pharmacol Sci 2008, 29:413-420.
    • (2008) Trends Pharmacol Sci , vol.29 , pp. 413-420
    • Tobin, A.B.1    Butcher, A.J.2    Kong, K.C.3
  • 48
    • 77957061477 scopus 로고    scopus 로고
    • The dopamine D(4) receptor, the ultimate disordered protein
    • Woods A.S. The dopamine D(4) receptor, the ultimate disordered protein. J Recept Signal Transduct Res 2010, 30:331-336.
    • (2010) J Recept Signal Transduct Res , vol.30 , pp. 331-336
    • Woods, A.S.1
  • 51
    • 84883419186 scopus 로고    scopus 로고
    • Promiscuity as a functional trait: intrinsically disordered regions as central players of interactomes
    • Cumberworth A., Lamour G., Babu M.M., Gsponer J. Promiscuity as a functional trait: intrinsically disordered regions as central players of interactomes. Biochem J 2013, 454:361-369.
    • (2013) Biochem J , vol.454 , pp. 361-369
    • Cumberworth, A.1    Lamour, G.2    Babu, M.M.3    Gsponer, J.4
  • 52
    • 84902500178 scopus 로고    scopus 로고
    • Controlling entropy to tune the functions of intrinsically disordered regions
    • Flock T., Weatheritt R.J., Latysheva N.S., Babu M.M. Controlling entropy to tune the functions of intrinsically disordered regions. Curr Opin Struct Biol 2014, 26C:62-72.
    • (2014) Curr Opin Struct Biol , vol.26 C , pp. 62-72
    • Flock, T.1    Weatheritt, R.J.2    Latysheva, N.S.3    Babu, M.M.4
  • 54
    • 84876221513 scopus 로고    scopus 로고
    • Higher-order assemblies in a new paradigm of signal transduction
    • Wu H. Higher-order assemblies in a new paradigm of signal transduction. Cell 2013, 153:287-292.
    • (2013) Cell , vol.153 , pp. 287-292
    • Wu, H.1
  • 56
    • 84890744445 scopus 로고    scopus 로고
    • Kinetics and mechanism of G protein-coupled receptor activation
    • Lohse M.J., Maiellaro I., Calebiro D. Kinetics and mechanism of G protein-coupled receptor activation. Curr Opin Cell Biol 2014, 27:87-93.
    • (2014) Curr Opin Cell Biol , vol.27 , pp. 87-93
    • Lohse, M.J.1    Maiellaro, I.2    Calebiro, D.3
  • 57
    • 84872195772 scopus 로고    scopus 로고
    • Single-molecule analysis of fluorescently labeled G-protein-coupled receptors reveals complexes with distinct dynamics and organization
    • Calebiro D., Rieken F., Wagner J., Sungkaworn T., Zabel U., Borzi A., Cocucci E., Zurn A., Lohse M.J. Single-molecule analysis of fluorescently labeled G-protein-coupled receptors reveals complexes with distinct dynamics and organization. Proc Natl Acad Sci U S A 2013, 110:743-748.
    • (2013) Proc Natl Acad Sci U S A , vol.110 , pp. 743-748
    • Calebiro, D.1    Rieken, F.2    Wagner, J.3    Sungkaworn, T.4    Zabel, U.5    Borzi, A.6    Cocucci, E.7    Zurn, A.8    Lohse, M.J.9
  • 59
    • 77952335311 scopus 로고    scopus 로고
    • Net charge per residue modulates conformational ensembles of intrinsically disordered proteins
    • Mao A.H., Crick S.L., Vitalis A., Chicoine C.L., Pappu R.V. Net charge per residue modulates conformational ensembles of intrinsically disordered proteins. Proc Natl Acad Sci U S A 2010, 107:8183-8188.
    • (2010) Proc Natl Acad Sci U S A , vol.107 , pp. 8183-8188
    • Mao, A.H.1    Crick, S.L.2    Vitalis, A.3    Chicoine, C.L.4    Pappu, R.V.5
  • 61
    • 84890157678 scopus 로고    scopus 로고
    • Role of beta-arrestins and arrestin domain-containing proteins in G protein-coupled receptor trafficking
    • Kang D.S., Tian X., Benovic J.L. Role of beta-arrestins and arrestin domain-containing proteins in G protein-coupled receptor trafficking. Curr Opin Cell Biol 2014, 27:63-71.
    • (2014) Curr Opin Cell Biol , vol.27 , pp. 63-71
    • Kang, D.S.1    Tian, X.2    Benovic, J.L.3
  • 62
  • 67
    • 84891467843 scopus 로고    scopus 로고
    • GPCR signaling along the endocytic pathway
    • Irannejad R., von Zastrow M. GPCR signaling along the endocytic pathway. Curr Opin Cell Biol 2014, 27:109-116.
    • (2014) Curr Opin Cell Biol , vol.27 , pp. 109-116
    • Irannejad, R.1    von Zastrow, M.2
  • 68
    • 84902668477 scopus 로고    scopus 로고
    • The ubiquitin ligase deltex-3l regulates endosomal sorting of the G protein-coupled receptor CXCR4
    • Holleman J., Marchese A. The ubiquitin ligase deltex-3l regulates endosomal sorting of the G protein-coupled receptor CXCR4. Mol Biol Cell 2014, 25:1892-1904.
    • (2014) Mol Biol Cell , vol.25 , pp. 1892-1904
    • Holleman, J.1    Marchese, A.2
  • 69
    • 84889644449 scopus 로고    scopus 로고
    • Atypical regulation of G protein-coupled receptor intracellular trafficking by ubiquitination
    • Dores M.R., Trejo J. Atypical regulation of G protein-coupled receptor intracellular trafficking by ubiquitination. Curr Opin Cell Biol 2014, 27:44-50.
    • (2014) Curr Opin Cell Biol , vol.27 , pp. 44-50
    • Dores, M.R.1    Trejo, J.2
  • 70
    • 70350512023 scopus 로고    scopus 로고
    • Alternative splicing of G protein-coupled receptors: physiology and pathophysiology
    • Markovic D., Challiss R.A. Alternative splicing of G protein-coupled receptors: physiology and pathophysiology. Cell Mol Life Sci 2009, 66:3337-3352.
    • (2009) Cell Mol Life Sci , vol.66 , pp. 3337-3352
    • Markovic, D.1    Challiss, R.A.2
  • 71
    • 84894901769 scopus 로고    scopus 로고
    • Functional understanding of the diverse exon-intron structures of human GPCR genes
    • Hammond D.A., Olman V., Xu Y. Functional understanding of the diverse exon-intron structures of human GPCR genes. J Bioinform Comput Biol 2014, 12:1350019.
    • (2014) J Bioinform Comput Biol , vol.12 , pp. 1350019
    • Hammond, D.A.1    Olman, V.2    Xu, Y.3
  • 72
    • 42449122192 scopus 로고    scopus 로고
    • Alternative splicing of the G protein-coupled receptor superfamily in human airway smooth muscle diversifies the complement of receptors
    • Einstein R., Jordan H., Zhou W., Brenner M., Moses E.G., Liggett S.B. Alternative splicing of the G protein-coupled receptor superfamily in human airway smooth muscle diversifies the complement of receptors. Proc Natl Acad Sci U S A 2008, 105:5230-5235.
    • (2008) Proc Natl Acad Sci U S A , vol.105 , pp. 5230-5235
    • Einstein, R.1    Jordan, H.2    Zhou, W.3    Brenner, M.4    Moses, E.G.5    Liggett, S.B.6
  • 73
    • 84865550650 scopus 로고    scopus 로고
    • The roles played by highly truncated splice variants of G protein-coupled receptors
    • Wise H. The roles played by highly truncated splice variants of G protein-coupled receptors. J Mol Signal 2012, 7:13.
    • (2012) J Mol Signal , vol.7 , pp. 13
    • Wise, H.1
  • 74
    • 0033118334 scopus 로고    scopus 로고
    • Molecular tinkering of G protein-coupled receptors: an evolutionary success
    • Bockaert J., Pin J.P. Molecular tinkering of G protein-coupled receptors: an evolutionary success. EMBO J 1999, 18:1723-1729.
    • (1999) EMBO J , vol.18 , pp. 1723-1729
    • Bockaert, J.1    Pin, J.P.2
  • 75
    • 69949090808 scopus 로고    scopus 로고
    • Focus on the splicing of secretin GPCRs transmembrane-domain 7
    • Markovic D., Grammatopoulos D.K. Focus on the splicing of secretin GPCRs transmembrane-domain 7. Trends Biochem Sci 2009, 34:443-452.
    • (2009) Trends Biochem Sci , vol.34 , pp. 443-452
    • Markovic, D.1    Grammatopoulos, D.K.2
  • 76
    • 84862992463 scopus 로고    scopus 로고
    • Tissue-specific splicing of disordered segments that embed binding motifs rewires protein interaction networks
    • Buljan M., Chalancon G., Eustermann S., Wagner G.P., Fuxreiter M., Bateman A., Babu M.M. Tissue-specific splicing of disordered segments that embed binding motifs rewires protein interaction networks. Mol Cell 2012, 46:871-883.
    • (2012) Mol Cell , vol.46 , pp. 871-883
    • Buljan, M.1    Chalancon, G.2    Eustermann, S.3    Wagner, G.P.4    Fuxreiter, M.5    Bateman, A.6    Babu, M.M.7
  • 78
    • 84863928687 scopus 로고    scopus 로고
    • Linear motifs confer functional diversity onto splice variants
    • Weatheritt R.J., Davey N.E., Gibson T.J. Linear motifs confer functional diversity onto splice variants. Nucleic Acids Res 2012, 40:7123-7131.
    • (2012) Nucleic Acids Res , vol.40 , pp. 7123-7131
    • Weatheritt, R.J.1    Davey, N.E.2    Gibson, T.J.3
  • 80
    • 84879054442 scopus 로고    scopus 로고
    • Detection of G protein-selective G protein-coupled receptor (GPCR) conformations in live cells
    • Malik R.U., Ritt M., DeVree B.T., Neubig R.R., Sunahara R.K., Sivaramakrishnan S. Detection of G protein-selective G protein-coupled receptor (GPCR) conformations in live cells. J Biol Chem 2013, 288:17167-17178.
    • (2013) J Biol Chem , vol.288 , pp. 17167-17178
    • Malik, R.U.1    Ritt, M.2    DeVree, B.T.3    Neubig, R.R.4    Sunahara, R.K.5    Sivaramakrishnan, S.6
  • 84
    • 84897000286 scopus 로고    scopus 로고
    • Biochemistry. The resolution revolution
    • Kuhlbrandt W. Biochemistry. The resolution revolution. Science 2014, 343:1443-1444.
    • (2014) Science , vol.343 , pp. 1443-1444
    • Kuhlbrandt, W.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.