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Volumn 48, Issue 30, 2009, Pages 7132-7139

Identification of amino acids at two dimer interface regions of the α-factor receptor (Ste2)

Author keywords

[No Author keywords available]

Indexed keywords

CLASS A; CYS RESIDUES; DIMER FORMATION; DIMER INTERFACE; DISULFIDE BONDS; EXTRACELLULAR; G PROTEIN COUPLED RECEPTORS; INTERFACE REGIONS; INTERMOLECULAR DISULFIDE BOND; TRANS-MEMBRANE DOMAINS;

EID: 68049089705     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi900424h     Document Type: Article
Times cited : (32)

References (50)
  • 1
    • 3042798261 scopus 로고    scopus 로고
    • Molecular mechanisms of ligand binding, signaling, and regulation within the superfamily of G-protein-coupled receptors: Molecular modeling and mutagenesis approaches to receptor structure and function
    • Kristiansen, K. (2004) Molecular mechanisms of ligand binding, signaling, and regulation within the superfamily of G-protein-coupled receptors: Molecular modeling and mutagenesis approaches to receptor structure and function. Pharmacol. Ther. 103, 21-80.
    • (2004) Pharmacol. Ther. , vol.103 , pp. 21-80
    • Kristiansen, K.1
  • 2
    • 0034464742 scopus 로고    scopus 로고
    • Uncovering molecular mechanisms involved in activation of G protein-coupled receptors
    • Gether, U. (2000) Uncovering molecular mechanisms involved in activation of G protein-coupled receptors. Endocrin. Rev. 21, 90-113.
    • (2000) Endocrin. Rev. , vol.21 , pp. 90-113
    • Gether, U.1
  • 3
    • 0028338534 scopus 로고
    • GCRDb: A G-protein-coupled receptor database
    • Kolakowski, L. F.Jr. (1994) GCRDb: A G-protein-coupled receptor database. Receptors Channels 2, 1-7.
    • (1994) Receptors Channels , vol.2 , pp. 1-7
    • Kolakowski Jr., L.F.1
  • 5
    • 21744449334 scopus 로고    scopus 로고
    • Comparison of class a and D G protein-coupled receptors: Common features in structure and activation
    • DOI 10.1021/bi047316u
    • Eilers, M., Hornak, V., Smith, S. O., and Konopka, J. B. (2005) Comparison of Class A and D G Protein-Coupled Receptors: Common Features in Structure and Activation. Biochemistry 44, 8959-8975. (Pubitemid 40943213)
    • (2005) Biochemistry , vol.44 , Issue.25 , pp. 8959-8975
    • Eilers, M.1    Hornak, V.2    Smith, S.O.3    Konopka, J.B.4
  • 6
    • 1242276192 scopus 로고    scopus 로고
    • Roles of G-protein-coupled receptor dimerization
    • Terrillon, S., and Bouvier, M. (2004) Roles of G-protein-coupled receptor dimerization. EMBO Rep. 5, 30-34.
    • (2004) EMBO Rep. , vol.5 , pp. 30-34
    • Terrillon, S.1    Bouvier, M.2
  • 7
    • 14644387575 scopus 로고    scopus 로고
    • Emerging role of homo- and heterodimerization in G-protein-coupled receptor biosynthesis and maturation
    • Bulenger, S., Marullo, S., and Bouvier, M. (2005) Emerging role of homo- and heterodimerization in G-protein-coupled receptor biosynthesis and maturation. Trends Pharmacol. Sci. 26, 131-137.
    • (2005) Trends Pharmacol. Sci. , vol.26 , pp. 131-137
    • Bulenger, S.1    Marullo, S.2    Bouvier, M.3
  • 8
    • 10844255797 scopus 로고    scopus 로고
    • Oligomerization of G protein-coupled receptors: Past, present, and future
    • DOI 10.1021/bi047907k
    • Park, P. S., Filipek, S., Wells, J. W., and Palczewski, K. (2004) Oligomerization of G protein-coupled receptors: Past, present, and future. Biochemistry 43, 15643-15656. (Pubitemid 39665065)
    • (2004) Biochemistry , vol.43 , Issue.50 , pp. 15643-15656
    • Park, P.S.-H.1    Filipek, S.2    Wells, J.W.3    Palczewski, K.4
  • 9
    • 29144466481 scopus 로고    scopus 로고
    • Oligomerization of G-protein-coupled receptors: Lessons from the yeast Saccharomyces cerevisiae
    • DOI 10.1128/EC.4.12.1963-1970.2005
    • Overton, M. C., Chinault, S. L., and Blumer, K. J. (2005) Oligomerization of G-protein-coupled receptors: Lessons from the yeast Saccharomyces cerevisiae. Eukaryotic Cell 4, 1963-1970. (Pubitemid 41799617)
    • (2005) Eukaryotic Cell , vol.4 , Issue.12 , pp. 1963-1970
    • Overton, M.C.1    Chinault, S.L.2    Blumer, K.J.3
  • 10
    • 0038159530 scopus 로고    scopus 로고
    • Organization of the G protein-coupled receptors rhodopsin and opsin in native membranes
    • Liang, Y., Fotiadis, D., Filipek, S., Saperstein, D. A., Palczewski, K., and Engel, A. (2003) Organization of the G protein-coupled receptors rhodopsin and opsin in native membranes. J. Biol. Chem. 278, 21655-21662.
    • (2003) J. Biol. Chem. , vol.278 , pp. 21655-21662
    • Liang, Y.1    Fotiadis, D.2    Filipek, S.3    Saperstein, D.A.4    Palczewski, K.5    Engel, A.6
  • 12
    • 0035976714 scopus 로고    scopus 로고
    • Three-dimensional structure of an invertebrate rhodopsin and basis for ordered alignment in the photoreceptor membrane
    • Davies, A., Gowen, B. E., Krebs, A. M., Schertler, G. F., and Saibil, H. R. (2001) Three-dimensional structure of an invertebrate rhodopsin and basis for ordered alignment in the photoreceptor membrane. J. Mol. Biol. 314, 455-463.
    • (2001) J. Mol. Biol. , vol.314 , pp. 455-463
    • Davies, A.1    Gowen, B.E.2    Krebs, A.M.3    Schertler, G.F.4    Saibil, H.R.5
  • 13
    • 51049112029 scopus 로고    scopus 로고
    • Dopamine D2 receptors form higher order oligomers at physiological expression levels
    • Guo, W., Urizar, E., Kralikova, M., Mobarec, J. C., Shi, L., Filizola, M., and Javitch, J. A. (2008) Dopamine D2 receptors form higher order oligomers at physiological expression levels. EMBO J. 27, 2293-2304.
    • (2008) EMBO J. , vol.27 , pp. 2293-2304
    • Guo, W.1    Urizar, E.2    Kralikova, M.3    Mobarec, J.C.4    Shi, L.5    Filizola, M.6    Javitch, J.A.7
  • 14
    • 48749126827 scopus 로고    scopus 로고
    • Ligand sensitivity in dimeric associations of the serotonin 5HT2c receptor
    • Mancia, F., Assur, Z., Herman, A. G., Siegel, R., and Hendrickson, W. A. (2008) Ligand sensitivity in dimeric associations of the serotonin 5HT2c receptor. EMBO Rep. 9, 363-369.
    • (2008) EMBO Rep. , vol.9 , pp. 363-369
    • Mancia, F.1    Assur, Z.2    Herman, A.G.3    Siegel, R.4    Hendrickson, W.A.5
  • 15
    • 0041315589 scopus 로고    scopus 로고
    • C5a receptor oligomerization. I. Disulfide trapping reveals oligomers and potential contact surfaces in a G protein-coupled receptor
    • Klco, J. M., Lassere, T. B., and Baranski, T. J. (2003) C5a receptor oligomerization. I. Disulfide trapping reveals oligomers and potential contact surfaces in a G protein-coupled receptor. J. Biol. Chem. 278, 35345-35353.
    • (2003) J. Biol. Chem. , vol.278 , pp. 35345-35353
    • Klco, J.M.1    Lassere, T.B.2    Baranski, T.J.3
  • 16
    • 33644781659 scopus 로고    scopus 로고
    • Opsin is present as dimers in COS1 cells: Identification of amino acids at the dimeric interface
    • Kota, P., Reeves, P. J., Rajbhandary, U. L., and Khorana, H. G. (2006) Opsin is present as dimers in COS1 cells: Identification of amino acids at the dimeric interface. Proc. Natl. Acad. Sci. U.S.A. 103, 3054-3059.
    • (2006) Proc. Natl. Acad. Sci. U.S.A. , vol.103 , pp. 3054-3059
    • Kota, P.1    Reeves, P.J.2    Rajbhandary, U.L.3    Khorana, H.G.4
  • 17
    • 36448988595 scopus 로고    scopus 로고
    • Activation of a dimeric metabotropic glutamate receptor by intersubunit rearrangement
    • Brock, C., Oueslati, N., Soler, S., Boudier, L., Rondard, P., and Pin, J. P. (2007) Activation of a dimeric metabotropic glutamate receptor by intersubunit rearrangement. J. Biol. Chem. 282, 33000-33008.
    • (2007) J. Biol. Chem. , vol.282 , pp. 33000-33008
    • Brock, C.1    Oueslati, N.2    Soler, S.3    Boudier, L.4    Rondard, P.5    Pin, J.P.6
  • 19
    • 34250666273 scopus 로고    scopus 로고
    • A monomeric G protein-coupled receptor isolated in a high-density lipoprotein particle efficiently activates its G protein
    • Whorton, M. R., Bokoch, M. P., Rasmussen, S. G., Huang, B., Zare, R. N., Kobilka, B., and Sunahara, R. K. (2007) A monomeric G protein-coupled receptor isolated in a high-density lipoprotein particle efficiently activates its G protein. Proc. Natl. Acad. Sci. U.S.A. 104, 7682-7687.
    • (2007) Proc. Natl. Acad. Sci. U.S.A. , vol.104 , pp. 7682-7687
    • Whorton, M.R.1    Bokoch, M.P.2    Rasmussen, S.G.3    Huang, B.4    Zare, R.N.5    Kobilka, B.6    Sunahara, R.K.7
  • 20
    • 0035312774 scopus 로고    scopus 로고
    • Transmembrane signaling in bacterial chemoreceptors
    • Falke, J. J., and Hazelbauer, G. L. (2001) Transmembrane signaling in bacterial chemoreceptors. Trends Biochem. Sci. 26, 257-265.
    • (2001) Trends Biochem. Sci. , vol.26 , pp. 257-265
    • Falke, J.J.1    Hazelbauer, G.L.2
  • 21
    • 0031717187 scopus 로고    scopus 로고
    • Cys-scanning mutagenesis: A novel approach to structure-function relationships in polytopic membrane proteins
    • Frillingos, S., Sahin-Toth, M., Wu, J., and Kaback, H. R. (1998) Cys-scanning mutagenesis: A novel approach to structure function relationships in polytopic membrane proteins. FASEB J. 12, 1281-1299. (Pubitemid 28475570)
    • (1998) FASEB Journal , vol.12 , Issue.13 , pp. 1281-1299
    • Frillingos, S.1    Sahin-Toth, M.2    Wu, J.3    Kaback, H.R.4
  • 23
    • 33746339971 scopus 로고    scopus 로고
    • Oligomerization of the yeast α-factor receptor: Implications for dominant negative effects of mutant receptors
    • Gehret, A. U., Bajaj, A., Naider, F., and Dumont, M. E. (2006) Oligomerization of the yeast α-factor receptor: Implications for dominant negative effects of mutant receptors. J. Biol. Chem. 281, 20698-20714.
    • (2006) J. Biol. Chem. , vol.281 , pp. 20698-20714
    • Gehret, A.U.1    Bajaj, A.2    Naider, F.3    Dumont, M.E.4
  • 24
    • 0034704906 scopus 로고    scopus 로고
    • G-protein-coupled receptors function as oligomers in vivo
    • Overton, M. C., and Blumer, K. J. (2000) G-protein-coupled receptors function as oligomers in vivo. Curr. Biol. 10, 341-344.
    • (2000) Curr. Biol. , vol.10 , pp. 341-344
    • Overton, M.C.1    Blumer, K.J.2
  • 25
    • 12744280975 scopus 로고    scopus 로고
    • Protein interaction quantified in vivo by spectrally resolved fluorescence resonance energy transfer
    • Raicu, V., Jansma, D. B., Miller, R. J., and Friesen, J. D. (2005) Protein interaction quantified in vivo by spectrally resolved fluorescence resonance energy transfer. Biochem. J. 385, 265-277.
    • (2005) Biochem. J. , vol.385 , pp. 265-277
    • Raicu, V.1    Jansma, D.B.2    Miller, R.J.3    Friesen, J.D.4
  • 26
    • 1342346495 scopus 로고    scopus 로고
    • A microdomain formed by the extracellular ends of the transmembrane domains promotes activation of the G protein-coupled α-factor receptor
    • Lin, J. C., Duell, K., and Konopka, J. B. (2004) A microdomain formed by the extracellular ends of the transmembrane domains promotes activation of the G protein-coupled α-factor receptor. Mol. Cell. Biol. 24, 2041-2051.
    • (2004) Mol. Cell. Biol. , vol.24 , pp. 2041-2051
    • Lin, J.C.1    Duell, K.2    Konopka, J.B.3
  • 27
    • 0037457812 scopus 로고    scopus 로고
    • Aromatic residues at the extracellular ends of transmembrane domains 5 and 6 promote ligand activation of the G protein-coupled α-factor receptor
    • DOI 10.1021/bi026766o
    • Lin, J., Parrish, W., Eilers, M., Smith, S. O., and Konopka, J. B. (2003) Aromatic residues at the extracellular ends of transmembrane domains 5 and 6 are important for ligand activation of the G protein-coupled α-factor receptor. Biochemistry 42, 293-301. (Pubitemid 36105747)
    • (2003) Biochemistry , vol.42 , Issue.2 , pp. 293-301
    • Lin, J.C.1    Parrish, W.2    Eilers, M.3    Smith, S.O.4    Konopka, J.B.5
  • 28
    • 0034714383 scopus 로고    scopus 로고
    • Interaction between transmembrane domains 5 and 6 in the α-factor receptor
    • Dube, P., DeConstanzo, A., and Konopka, J. B. (2000) Interaction between transmembrane domains 5 and 6 in the α-factor receptor. J. Biol. Chem. 275, 26492-26499.
    • (2000) J. Biol. Chem. , vol.275 , pp. 26492-26499
    • Dube, P.1    DeConstanzo, A.2    Konopka, J.B.3
  • 29
    • 0022446007 scopus 로고
    • Down regulation of the α-factor pheromone receptor in Saccharomyces cerevisiae
    • Jenness, D. D., and Spatrick, P. (1986) Down regulation of the α-factor pheromone receptor in Saccharomyces cerevisiae. Cell 46, 345-353.
    • (1986) Cell , vol.46 , pp. 345-353
    • Jenness, D.D.1    Spatrick, P.2
  • 31
    • 0038576278 scopus 로고    scopus 로고
    • The fourth transmembrane segment forms the interface of the dopamine D2 receptor homodimer
    • Guo, W., Shi, L., and Javitch, J. A. (2003) The fourth transmembrane segment forms the interface of the dopamine D2 receptor homodimer. J. Biol. Chem. 278, 4385-4388.
    • (2003) J. Biol. Chem. , vol.278 , pp. 4385-4388
    • Guo, W.1    Shi, L.2    Javitch, J.A.3
  • 32
    • 0036829815 scopus 로고    scopus 로고
    • The extracellular N-terminal domain and transmembrane domains 1 and 2 mediate oligomerization of a yeast G protein-coupled receptor
    • Overton, M. C., and Blumer, K. J. (2002) The extracellular N-terminal domain and transmembrane domains 1 and 2 mediate oligomerization of a yeast G protein-coupled receptor. J. Biol. Chem. 277, 41463-74142.
    • (2002) J. Biol. Chem. , vol.277 , pp. 41463-74142
    • Overton, M.C.1    Blumer, K.J.2
  • 33
    • 1542467519 scopus 로고    scopus 로고
    • Oligomerization, biogenesis, and signaling is promoted by a glycophorin A-like dimerization motif in transmembrane domain 1 of a yeast G protein-coupled receptor
    • Overton, M. C., Chinault, S. L., and Blumer, K. J. (2003) Oligomerization, biogenesis, and signaling is promoted by a glycophorin A-like dimerization motif in transmembrane domain 1 of a yeast G protein-coupled receptor. J. Biol. Chem. 278, 49369-49377.
    • (2003) J. Biol. Chem. , vol.278 , pp. 49369-49377
    • Overton, M.C.1    Chinault, S.L.2    Blumer, K.J.3
  • 39
    • 0030932407 scopus 로고    scopus 로고
    • A transmembrane helix dimer: Structure and implications
    • MacKenzie, K. R., Prestegard, J. H., and Engelman, D. M. (1997) A transmembrane helix dimer: Structure and implications. Science 276, 131-133.
    • (1997) Science , vol.276 , pp. 131-133
    • MacKenzie, K.R.1    Prestegard, J.H.2    Engelman, D.M.3
  • 40
    • 0036298264 scopus 로고    scopus 로고
    • Mutagenic mapping of helical structures in the transmembrane segments of the yeast α-factor receptor
    • Martin, N. P., Celic, A., and Dumont, M. E. (2002) Mutagenic mapping of helical structures in the transmembrane segments of the yeast α-factor receptor. J. Mol. Biol. 317, 765-788.
    • (2002) J. Mol. Biol. , vol.317 , pp. 765-788
    • Martin, N.P.1    Celic, A.2    Dumont, M.E.3
  • 41
    • 0031705403 scopus 로고    scopus 로고
    • Dominant-negative mutations in the G protein-coupled α-factor receptor map to the extracellular ends of the transmembrane segments
    • Dosil, M., Giot, L., Davis, C., and Konopka, J. B. (1998) Dominant-negative mutations in the G protein-coupled α-factor receptor map to the extracellular ends of the transmembrane segments. Mol. Cell. Biol. 18, 5981-5991.
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 5981-5991
    • Dosil, M.1    Giot, L.2    Davis, C.3    Konopka, J.B.4
  • 42
    • 0027943713 scopus 로고
    • Direct evidence for ligand-induced internalization of the yeast α-factor pheromone receptor
    • Schandel, K. A., and Jenness, D. D. (1994) Direct evidence for ligand-induced internalization of the yeast α-factor pheromone receptor. Mol. Cell. Biol. 14, 7245-7255.
    • (1994) Mol. Cell. Biol. , vol.14 , pp. 7245-7255
    • Schandel, K.A.1    Jenness, D.D.2
  • 43
    • 5444264224 scopus 로고    scopus 로고
    • Identification of ligand binding regions of the Saccharomyces cerevisiae α-factor pheromone receptor by photoaffinity cross-linking
    • DOI 10.1021/bi0496889
    • Son, C. D., Sargsyan, H., Naider, F., and Becker, J. M. (2004) Identification of ligand binding regions of the Saccharomyces cerevisiae α-factor pheromone receptor by photoaffinity cross-linking. Biochemistry 43, 13193-13203. (Pubitemid 39362788)
    • (2004) Biochemistry , vol.43 , Issue.41 , pp. 13193-13203
    • Son, C.D.1    Sargsyan, H.2    Naider, F.3    Becker, J.M.4
  • 44
    • 0032788711 scopus 로고    scopus 로고
    • Dominant negative mutations in the α-factor receptor, a G protein-coupled receptor encoded by the STE2 gene of the yeast Saccharomyces cerevisiae
    • Leavitt, L. M., Macaluso, C. R., Kim, K. S., Martin, N. P., and Dumont, M. E. (1999) Dominant negative mutations in the α-factor receptor, a G protein-coupled receptor encoded by the STE2 gene of the yeast Saccharomyces cerevisiae. Mol. Gen. Genet. 261, 917-932.
    • (1999) Mol. Gen. Genet. , vol.261 , pp. 917-932
    • Leavitt, L.M.1    Macaluso, C.R.2    Kim, K.S.3    Martin, N.P.4    Dumont, M.E.5
  • 45
    • 57149136593 scopus 로고    scopus 로고
    • In vitro characterization of ligand-induced oligomerization of the S. cerevisiae G-protein coupled receptor, Ste2p
    • Shi, C., Paige, M. F., Maley, J., and Loewen, M. C. (2009) In vitro characterization of ligand-induced oligomerization of the S. cerevisiae G-protein coupled receptor, Ste2p. Biochim. Biophys. Acta 1790, 1-7.
    • (2009) Biochim. Biophys. Acta , vol.1790 , pp. 1-7
    • Shi, C.1    Paige, M.F.2    Maley, J.3    Loewen, M.C.4
  • 46
    • 33644850470 scopus 로고    scopus 로고
    • Interacting residues in an activated state of a G protein-coupled receptor
    • Lee, Y. H., Naider, F., and Becker, J. M. (2006) Interacting residues in an activated state of a G protein-coupled receptor. J. Biol. Chem. 281, 2263-2272.
    • (2006) J. Biol. Chem. , vol.281 , pp. 2263-2272
    • Lee, Y.H.1    Naider, F.2    Becker, J.M.3
  • 48
    • 1542268949 scopus 로고    scopus 로고
    • Helix packing moments reveal diversity and conservation in membrane protein structure
    • Liu, W., Eilers, M., Patel, A. B., and Smith, S. O. (2004) Helix packing moments reveal diversity and conservation in membrane protein structure. J. Mol. Biol. 337, 713-729.
    • (2004) J. Mol. Biol. , vol.337 , pp. 713-729
    • Liu, W.1    Eilers, M.2    Patel, A.B.3    Smith, S.O.4
  • 50
    • 33845959757 scopus 로고    scopus 로고
    • Accessibility of cysteine residues substituted into the cytoplasmic regions of the α-factor receptor identifies the intracellular residues that are available for G protein interaction
    • DOI 10.1021/bi0614939
    • Choi, Y., and Konopka, J. B. (2006) Accessibility of Cys residues substituted into the cytoplasmic regions of the α-factor receptor identifies the intracellular residues that are available for G protein interaction. Biochemistry 45, 15310-15317. (Pubitemid 46032457)
    • (2006) Biochemistry , vol.45 , Issue.51 , pp. 15310-15317
    • Choi, Y.1    Konopka, J.B.2


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