메뉴 건너뛰기




Volumn 63, Issue , 2012, Pages 155-180

Synthesis and assembly of G Protein βγ Dimers: Comparison of in vitro and in vivo studies

Author keywords

Assembly; Chaperone; G protein betagamma

Indexed keywords

CHAPERONE; G PROTEIN BETA GAMMA; G-PROTEIN BETA GAMMA; GUANINE NUCLEOTIDE BINDING PROTEIN BETA SUBUNIT; GUANINE NUCLEOTIDE BINDING PROTEIN GAMMA SUBUNIT;

EID: 84892805195     PISSN: 03060225     EISSN: None     Source Type: Book Series    
DOI: 10.1007/978-94-007-4765-4_9     Document Type: Article
Times cited : (10)

References (115)
  • 1
    • 0842303213 scopus 로고    scopus 로고
    • Roles of molecular chaperones in protein misfolding diseases
    • Barral JM, Broadley SA, Schaffar G, Hartl FU (2004) Roles of molecular chaperones in protein misfolding diseases. Semin Cell Dev Biol 15(1): 17-29. doi: 10. 1016/j. semcdb. 2003. 12. 010.
    • (2004) Semin Cell Dev Biol , vol.15 , Issue.1 , pp. 17-29
    • Barral, J.M.1    Broadley, S.A.2    Schaffar, G.3    Hartl, F.U.4
  • 3
    • 0035011489 scopus 로고    scopus 로고
    • Regulation of transport of the dopamine D1 receptor by a new membrane-associated ER protein
    • Bermak JC, Li M, Bullock C, Zhou QY (2001) Regulation of transport of the dopamine D1 receptor by a new membrane-associated ER protein. Nat Cell Biol 3(5): 492-498. doi: 10. 1038/35074561.
    • (2001) Nat Cell Biol , vol.3 , Issue.5 , pp. 492-498
    • Bermak, J.C.1    Li, M.2    Bullock, C.3    Zhou, Q.Y.4
  • 4
    • 0025355063 scopus 로고
    • G proteins in signal transduction
    • Birnbaumer L (1990) G proteins in signal transduction. Annu Rev Pharmacol Toxicol 30: 675-705.
    • (1990) Annu Rev Pharmacol Toxicol , vol.30 , pp. 675-705
    • Birnbaumer, L.1
  • 6
    • 0025010979 scopus 로고
    • The GTPase superfamily: A conserved switch for diverse cell functions
    • Bourne HR, Sanders DA, McCormick F (1990) The GTPase superfamily: a conserved switch for diverse cell functions. Nature 348: 125-132.
    • (1990) Nature , vol.348 , pp. 125-132
    • Bourne, H.R.1    Sanders, D.A.2    McCormick, F.3
  • 7
    • 67649229560 scopus 로고    scopus 로고
    • Activities of the chaperonin containing TCP-1 (CCT): Implications for cell cycle progression and cytoskeletal organisation
    • Brackley KI, Grantham J (2009) Activities of the chaperonin containing TCP-1 (CCT): implications for cell cycle progression and cytoskeletal organisation. Cell Stress Chaperones 14(1): 23-31. doi: 10. 1007/s12192-008-0057-x.
    • (2009) Cell Stress Chaperones , vol.14 , Issue.1 , pp. 23-31
    • Brackley, K.I.1    Grantham, J.2
  • 10
    • 0345094935 scopus 로고    scopus 로고
    • Eukaryotic chaperonins: Lubricating the folding of WD-repeat proteins
    • Craig E (2003) Eukaryotic chaperonins: lubricating the folding of WD-repeat proteins. Curr Biol 13: R904-R905.
    • (2003) Curr Biol , vol.13 , pp. 904-905
    • Craig, E.1
  • 12
    • 0026437690 scopus 로고
    • Expression, characteization and purification of soluble G protein beta/gamma dimers composed of defined subunits in baculovirus infected cells
    • Dietrich A, Meister M, Spicher K, Schultz G, Camps M, Gierschik P (1992) Expression, characteization and purification of soluble G protein beta/gamma dimers composed of defined subunits in baculovirus infected cells. FEBS Lett 313: 220-224.
    • (1992) FEBS Lett , vol.313 , pp. 220-224
    • Dietrich, A.1    Meister, M.2    Spicher, K.3    Schultz, G.4    Camps, M.5    Gierschik, P.6
  • 13
    • 24344466241 scopus 로고    scopus 로고
    • G protein betagamma dimer formation: Gbeta and Ggamma differentially determine efficiency of in vitro dimer formation
    • Dingus J, Wells CA, Campbell L, Cleator JH, Robinson K, Hildebrandt JD (2005) G protein betagamma dimer formation: Gbeta and Ggamma differentially determine efficiency of in vitro dimer formation. Biochemistry 44: 11882-11890.
    • (2005) Biochemistry , vol.44 , pp. 11882-11890
    • Dingus, J.1    Wells, C.A.2    Campbell, L.3    Cleator, J.H.4    Robinson, K.5    Hildebrandt, J.D.6
  • 14
    • 0033572358 scopus 로고    scopus 로고
    • The G protein subunit gene families
    • Downes GB, Gautam N (1999) The G protein subunit gene families. Genomics 62: 544-552.
    • (1999) Genomics , vol.62 , pp. 544-552
    • Downes, G.B.1    Gautam, N.2
  • 15
    • 34250325496 scopus 로고    scopus 로고
    • Dopamine receptor-interacting protein 78 acts as a molecular chaperone for ggamma subunits before assembly with gbeta
    • Dupre DJ, Robitaille M, Richer M, Ethier N, Mamarbachi AM, Hebert TE (2007) Dopamine receptor-interacting protein 78 acts as a molecular chaperone for ggamma subunits before assembly with gbeta. J Biol Chem 282(18): 13703-13715. doi: 10. 1074/jbc. M608846200.
    • (2007) J Biol Chem , vol.282 , Issue.18 , pp. 13703-13715
    • Dupre, D.J.1    Robitaille, M.2    Richer, M.3    Ethier, N.4    Mamarbachi, A.M.5    Hebert, T.E.6
  • 16
    • 23044445800 scopus 로고    scopus 로고
    • The cotranslational contacts between ribosome-bound nascent polypeptides and the subunits of the hetero-oligomeric chaperonin TRiC probed by photocross-linking
    • Etchells SA, Meyer AS, Yam AY, Roobol A, Miao Y, Shao Y, Carden MJ, Skach WR, Frydman J, Johnson AE (2005) The cotranslational contacts between ribosome-bound nascent polypeptides and the subunits of the hetero-oligomeric chaperonin TRiC probed by photocross-linking. J Biol Chem 280(30): 28118-28126. doi: 10. 1074/jbc. M504110200.
    • (2005) J Biol Chem , vol.280 , Issue.30 , pp. 28118-28126
    • Etchells, S.A.1    Meyer, A.S.2    Yam, A.Y.3    Roobol, A.4    Miao, Y.5    Shao, Y.6    Carden, M.J.7    Skach, W.R.8    Frydman, J.9    Johnson, A.E.10
  • 17
    • 0035968248 scopus 로고    scopus 로고
    • Gbetagamma isoforms selectively rescue plasma membrane localization and palmitoylation of mutant galphas and galphaq
    • Evanko DS, Thiyagarajan MM, Siderovski DP, Wedegaertner DP (2001) Gbetagamma isoforms selectively rescue plasma membrane localization and palmitoylation of mutant galphas and galphaq. J Biol Chem 276: 23945-23953.
    • (2001) J Biol Chem , vol.276 , pp. 23945-23953
    • Evanko, D.S.1    Thiyagarajan, M.M.2    Siderovski, D.P.3    Wedegaertner, D.P.4
  • 18
    • 0030730821 scopus 로고    scopus 로고
    • Chaperonin-mediated folding in the eukaryotic ytosol proceeds through rounds of release of native and nonnative forms
    • Farr GW, Scharl EC, Schumacher RJ, Sondek S, Howrwich AL (1997) Chaperonin-mediated folding in the eukaryotic ytosol proceeds through rounds of release of native and nonnative forms. Cell 89: 927-937.
    • (1997) Cell , vol.89 , pp. 927-937
    • Farr, G.W.1    Scharl, E.C.2    Schumacher, R.J.3    Sondek, S.4    Howrwich, A.L.5
  • 19
    • 0033400674 scopus 로고    scopus 로고
    • Formation of the VHL-elngin BC tumor suppressor complex is mediated by the chaperonin TRiC
    • Feldman DE, Thulasiraman V, Ferreyra RG, Frydman J (1999) Formation of the VHL-elngin BC tumor suppressor complex is mediated by the chaperonin TRiC. Mol Cell 4: 1051-1061.
    • (1999) Mol Cell , vol.4 , pp. 1051-1061
    • Feldman, D.E.1    Thulasiraman, V.2    Ferreyra, R.G.3    Frydman, J.4
  • 22
    • 0033392946 scopus 로고    scopus 로고
    • Enzymology and biology of CaaX protein prenylation
    • Fu H-W, Casey P (1999) Enzymology and biology of CaaX protein prenylation. Recent Prog Horm Res 54: 315-343.
    • (1999) Recent Prog Horm Res , vol.54 , pp. 315-343
    • Fu, H.-W.1    Casey, P.2
  • 24
    • 0029854139 scopus 로고    scopus 로고
    • Folding of proteins with WD-repeats: Comparison of six members of the WD-repeat superfamily to the G protein beta subunit
    • Garcia-Higuera I, Fenoglio J, Li Y, Lewis C, Panchenko MP, Reiner O, Smith TF, Neer EJ (1996a) Folding of proteins with WD-repeats: comparison of six members of the WD-repeat superfamily to the G protein beta subunit. Biochemistry 35(44): 13985-13994. doi: 10. 1021/bi9612879.
    • (1996) Biochemistry , vol.35 , Issue.44 , pp. 13985-13994
    • Garcia-Higuera, I.1    Fenoglio, J.2    Li, Y.3    Lewis, C.4    Panchenko, M.P.5    Reiner, O.6    Smith, T.F.7    Neer, E.J.8
  • 25
    • 0030039493 scopus 로고    scopus 로고
    • Intersubunit surfaces in G protein alpha/beta/gamma heterotrimers. Analysis by cross linking and mutagenesis of beta/gamma
    • Garcia-Higuera I, Thomas TC, Yi F, Neer EJ (1996b) Intersubunit surfaces in G protein alpha/beta/gamma heterotrimers. Analysis by cross linking and mutagenesis of beta/gamma. J Biol Chem 271: 528-535.
    • (1996) J Biol Chem , vol.271 , pp. 528-535
    • Garcia-Higuera, I.1    Thomas, T.C.2    Yi, F.3    Neer, E.J.4
  • 26
    • 0032502778 scopus 로고    scopus 로고
    • Folding a WD repeat propeller. Role of highly conserved aspartic acid residues in the G protein beta subunit and Sec13
    • Garcia-Higuera I, Gaitatzes C, Smith T, Neer EJ (1998) Folding a WD repeat propeller. Role of highly conserved aspartic acid residues in the G protein beta subunit and Sec13. J Biol Chem 273: 9041-9049.
    • (1998) J Biol Chem , vol.273 , pp. 9041-9049
    • Garcia-Higuera, I.1    Gaitatzes, C.2    Smith, T.3    Neer, E.J.4
  • 27
    • 0028050512 scopus 로고
    • Multiple domains of G protein beta confer subunit specificity in bg interactions
    • Garritsen A, Simonds WF (1994) Multiple domains of G protein beta confer subunit specificity in bg interactions. J Biol Chem 269: 24418-24423.
    • (1994) J Biol Chem , vol.269 , pp. 24418-24423
    • Garritsen, A.1    Simonds, W.F.2
  • 28
    • 0030297912 scopus 로고    scopus 로고
    • Crystal structure at 2. 4 A resolution of the complex of transducin beta/gamma and its regulator, phosducin
    • Gaudet R, Bohm A, Sigler PB (1996) Crystal structure at 2. 4 A resolution of the complex of transducin beta/gamma and its regulator, phosducin. Cell 87: 577-588.
    • (1996) Cell , vol.87 , pp. 577-588
    • Gaudet, R.1    Bohm, A.2    Sigler, P.B.3
  • 29
    • 0023062991 scopus 로고
    • G proteins: Transducers of receptor-generated signals
    • Gilman AG (1987) G proteins: transducers of receptor-generated signals. Annu Rev Biochem 56: 615-649.
    • (1987) Annu Rev Biochem , vol.56 , pp. 615-649
    • Gilman, A.G.1
  • 30
    • 0026542256 scopus 로고
    • Expression and purification of functional G protein alpha subunits using a baculovirus expression system
    • Graber SG, Figler RA, Garrison JC (1992a) Expression and purification of functional G protein alpha subunits using a baculovirus expression system. J Biol Chem 267: 1271-1278.
    • (1992) J Biol Chem , vol.267 , pp. 1271-1278
    • Graber, S.G.1    Figler, R.A.2    Garrison, J.C.3
  • 31
    • 0026691771 scopus 로고
    • Expression of functional G protein beta/gamma dimers of defined subunit composition using a baculovirus expression system
    • Graber SG, Figler RA, Kalman-Maltese VK, Robishaw JD, Garrison JC (1992b) Expression of functional G protein beta/gamma dimers of defined subunit composition using a baculovirus expression system. J Biol Chem 267: 13123-13126.
    • (1992) J Biol Chem , vol.267 , pp. 13123-13126
    • Graber, S.G.1    Figler, R.A.2    Kalman-Maltese, V.K.3    Robishaw, J.D.4    Garrison, J.C.5
  • 32
    • 0028070415 scopus 로고
    • Control of protein synthesis by hemin. Purification of a rabbit reticulocyte hsp 70 and characterization of its regulation of the activation of the hemin-controlled eIF-2(a) kinase
    • Gross M, Olin A, Hessefort S, Bender S (1993) Control of protein synthesis by hemin. Purification of a rabbit reticulocyte hsp 70 and characterization of its regulation of the activation of the hemin-controlled eIF-2(a) kinase. J Biol Chem 269: 22738-22748.
    • (1993) J Biol Chem , vol.269 , pp. 22738-22748
    • Gross, M.1    Olin, A.2    Hessefort, S.3    Bender, S.4
  • 33
    • 0031984517 scopus 로고    scopus 로고
    • The many faces of G protein signaling
    • Hamm HE (1998) The many faces of G protein signaling. J Biol Chem 273: 669-672.
    • (1998) J Biol Chem , vol.273 , pp. 669-672
    • Hamm, H.E.1
  • 34
    • 0028982948 scopus 로고
    • Distinct pathways of Gi-and Gq-mediated mitogen-activated protein kinase activation
    • Hawes RE, van Biesen T, Koch WJ, Luttrell LM, Lefkowitz RJ (1995) Distinct pathways of Gi-and Gq-mediated mitogen-activated protein kinase activation. J Biol Chem 270: 17148-17153.
    • (1995) J Biol Chem , vol.270 , pp. 17148-17153
    • Hawes, R.E.1    van Biesen, T.2    Koch, W.J.3    Luttrell, L.M.4    Lefkowitz, R.J.5
  • 35
    • 0028363744 scopus 로고
    • In vitro processing of recombinant G protein gamma subunits. Requirements for assembly of an active beta/gamma complex
    • Higgins JB, Casey PJ (1994) In vitro processing of recombinant G protein gamma subunits. Requirements for assembly of an active beta/gamma complex. J Biol Chem 269: 9067-9073.
    • (1994) J Biol Chem , vol.269 , pp. 9067-9073
    • Higgins, J.B.1    Casey, P.J.2
  • 36
    • 0030248856 scopus 로고    scopus 로고
    • The role of prenylation in G protein assembly and function
    • Higgins JB, Casey PJ (1996) The role of prenylation in G protein assembly and function. Cell Signal 8: 433-437.
    • (1996) Cell Signal , vol.8 , pp. 433-437
    • Higgins, J.B.1    Casey, P.J.2
  • 37
    • 0030771361 scopus 로고    scopus 로고
    • Role of subunit diversity in signaling by heterotrimeric G proteins
    • Hildebrandt JD (1997) Role of subunit diversity in signaling by heterotrimeric G proteins. Biochem Pharmacol 54: 325-339.
    • (1997) Biochem Pharmacol , vol.54 , pp. 325-339
    • Hildebrandt, J.D.1
  • 38
    • 79960280386 scopus 로고    scopus 로고
    • Heterogeneous prenyl processing of the heterotrimeric G protein gamma subunits
    • Hildebrandt JD (2011) Heterogeneous prenyl processing of the heterotrimeric G protein gamma subunits. The Enzym Prot Prenylation Part A 29: 97-124.
    • (2011) The Enzym Prot Prenylation Part A , vol.29 , pp. 97-124
    • Hildebrandt, J.D.1
  • 39
    • 0021327226 scopus 로고
    • Identification of a gamma subunit associated with the adenylyl cyclase regulatory proteins Ns and Ni
    • Hildebrandt JD, Codina J, Risinger R, Birnbaumer L (1984) Identification of a gamma subunit associated with the adenylyl cyclase regulatory proteins Ns and Ni. J Biol Chem 259: 2039-2042.
    • (1984) J Biol Chem , vol.259 , pp. 2039-2042
    • Hildebrandt, J.D.1    Codina, J.2    Risinger, R.3    Birnbaumer, L.4
  • 40
    • 67650221615 scopus 로고    scopus 로고
    • Role of molecular chaperones in g protein beta 5/regulator of G protein signaling dimer assembly and G protein beta gamma dimer specificity
    • pii: M900800200
    • Howlett AC, Gray AJ, Hunter JM, Willardson BM (2009) Role of molecular chaperones in g protein beta 5/regulator of G protein signaling dimer assembly and G protein beta gamma dimer specificity. J Biol Chem. doi: 10. 1074/jbc. M900800200, pii: M900800200.
    • (2009) J Biol Chem
    • Howlett, A.C.1    Gray, A.J.2    Hunter, J.M.3    Willardson, B.M.4
  • 41
    • 0038813716 scopus 로고    scopus 로고
    • Regulation of phosducin-like protein by casein kinase 2 and N-terminal splicing
    • Humrich J, Bermel C, Grubel T, Quitterer U, Lohse MJ (2003) Regulation of phosducin-like protein by casein kinase 2 and N-terminal splicing. J Biol Chem 278: 4474-4481.
    • (2003) J Biol Chem , vol.278 , pp. 4474-4481
    • Humrich, J.1    Bermel, C.2    Grubel, T.3    Quitterer, U.4    Lohse, M.J.5
  • 42
    • 21244460334 scopus 로고    scopus 로고
    • Phosducinlike protein regulates G-protein folding by interaction with tailless complex polypeptide-1 alpha. Dephosphorylation or splicing of phlp turns the switch toward regulation of G folding
    • Humrich J, Bermel C, Bunemann M, Harmark L, Frost R, Quitterer U, Lohse MJ (2005) Phosducinlike protein regulates G-protein folding by interaction with tailless complex polypeptide-1 alpha. Dephosphorylation or splicing of phlp turns the switch toward regulation of G folding. J Biol Chem 280: 20042-20050.
    • (2005) J Biol Chem , vol.280 , pp. 20042-20050
    • Humrich, J.1    Bermel, C.2    Bunemann, M.3    Harmark, L.4    Frost, R.5    Quitterer, U.6    Lohse, M.J.7
  • 43
    • 3142766112 scopus 로고    scopus 로고
    • Visualization of G protein betagamma dimers using bimolecularfluorescence complementation demonstrates roles for both beta and gamma in subcellular targeting
    • Hynes TR, Tang L, Mervine SM, Sabo JL, Yost EA, Devreotes PN, Berlot CH (2004) Visualization of G protein betagamma dimers using bimolecularfluorescence complementation demonstrates roles for both beta and gamma in subcellular targeting. J Biol Chem 279: 30279-30286.
    • (2004) J Biol Chem , vol.279 , pp. 30279-30286
    • Hynes, T.R.1    Tang, L.2    Mervine, S.M.3    Sabo, J.L.4    Yost, E.A.5    Devreotes, P.N.6    Berlot, C.H.7
  • 44
    • 0026452219 scopus 로고
    • G protein beta/gamma subunits synthesized in sf9 cells. Functional characterization and the significance of prenylation of gamma
    • Iniguez-Lluhi JA, Simon MI, Robishaw JD, Gilman AG (1992) G protein beta/gamma subunits synthesized in sf9 cells. Functional characterization and the significance of prenylation of gamma. J Biol Chem 267: 23409-23417.
    • (1992) J Biol Chem , vol.267 , pp. 23409-23417
    • Iniguez-Lluhi, J.A.1    Simon, M.I.2    Robishaw, J.D.3    Gilman, A.G.4
  • 45
    • 73849149481 scopus 로고    scopus 로고
    • Reconciling theories of chaperonin accelerated folding with experimental evidence
    • Jewett AI, Shea JE (2010) Reconciling theories of chaperonin accelerated folding with experimental evidence. Cell Mol Life Sci 67(2): 255-276.
    • (2010) Cell Mol Life Sci , vol.67 , Issue.2 , pp. 255-276
    • Jewett, A.I.1    Shea, J.E.2
  • 46
    • 0033105104 scopus 로고    scopus 로고
    • Instability of the G protein beta5 subunit in detergent
    • Jones MB, Garrison JC (1999) Instability of the G protein beta5 subunit in detergent. Anal Biochem 268: 126-133.
    • (1999) Anal Biochem , vol.268 , pp. 126-133
    • Jones, M.B.1    Garrison, J.C.2
  • 47
    • 4444236667 scopus 로고    scopus 로고
    • The gbetagamma dimer as a novel source of selectivity in G-protein signaling: GGL-ing at convention
    • Jones MB, Siderovski DP, Hooks SB (2004) The gbetagamma dimer as a novel source of selectivity in G-protein signaling: GGL-ing at convention. Mol Interv 4: 200-214.
    • (2004) Mol Interv , vol.4 , pp. 200-214
    • Jones, M.B.1    Siderovski, D.P.2    Hooks, S.B.3
  • 48
    • 34347213434 scopus 로고    scopus 로고
    • Sequence dependence and differential expression of G γ 5 subunit isoforms of the heterotrimeric G proteins variably processed after prenylation in mammalian cells
    • Kilpatrick EL, Hildebrandt JD (2007) Sequence dependence and differential expression of G γ 5 subunit isoforms of the heterotrimeric G proteins variably processed after prenylation in mammalian cells. J Biol Chem 282: 14038-14047.
    • (2007) J Biol Chem , vol.282 , pp. 14038-14047
    • Kilpatrick, E.L.1    Hildebrandt, J.D.2
  • 49
    • 0037450538 scopus 로고    scopus 로고
    • Galpha(s) is palmitoylated at the N-terminal glycine
    • Kleuss C, Krause E (2003) Galpha(s) is palmitoylated at the N-terminal glycine. EMBO J 22: 826-832.
    • (2003) EMBO J , vol.22 , pp. 826-832
    • Kleuss, C.1    Krause, E.2
  • 50
    • 24344482829 scopus 로고    scopus 로고
    • The phosducin-like protein PhLP1 is essential for G{beta}{gamma} dimer formation in dictyostelium discoideum
    • Knol C, Engel R, Blaauw M, Visser AJWG, van Haastert PJM (2005) The phosducin-like protein PhLP1 is essential for G{beta}{gamma} dimer formation in dictyostelium discoideum. Mol Cell Biol 25: 8393-8400.
    • (2005) Mol Cell Biol , vol.25 , pp. 8393-8400
    • Knol, C.1    Engel, R.2    Blaauw, M.3    Visser, A.J.W.G.4    van Haastert, P.J.M.5
  • 51
    • 33744800848 scopus 로고    scopus 로고
    • Cytosolic chaperonin protects folding intermediates of G beta from aggregation by recognizing hydrophobic beta strands
    • Kubota S, Kubota H, Nagata K (2006) Cytosolic chaperonin protects folding intermediates of G beta from aggregation by recognizing hydrophobic beta strands. Proc Natl Acad Sci U S A 103: 8360-8365.
    • (2006) Proc Natl Acad Sci U S A , vol.103 , pp. 8360-8365
    • Kubota, S.1    Kubota, H.2    Nagata, K.3
  • 53
    • 0028933055 scopus 로고
    • Identification of a discrete region of the G protein gamma subunit conferring selectivity in beta/gamma complex formation
    • Lee C, Murakami T, Simonds WF (1995) Identification of a discrete region of the G protein gamma subunit conferring selectivity in beta/gamma complex formation. J Biol Chem 270: 8779-8784.
    • (1995) J Biol Chem , vol.270 , pp. 8779-8784
    • Lee, C.1    Murakami, T.2    Simonds, W.F.3
  • 54
    • 21244474081 scopus 로고    scopus 로고
    • G protein beta2 subunit-derived peptides for inhibition and induction of G protein pathways. Examination of voltage-gated calcium and G protein inwardly rectyfying potasium channels
    • Li X, Hummer A, Han J, Xie M, Melnik-Martinez K, Moreno RL, Buck M, Mark MD, Herlitz S (2006) G protein beta2 subunit-derived peptides for inhibition and induction of G protein pathways. Examination of voltage-gated calcium and G protein inwardly rectyfying potasium channels. J Biol Chem 280: 23945-23959.
    • (2006) J Biol Chem , vol.280 , pp. 23945-23959
    • Li, X.1    Hummer, A.2    Han, J.3    Xie, M.4    Melnik-Martinez, K.5    Moreno, R.L.6    Buck, M.7    Mark, M.D.8    Herlitz, S.9
  • 55
    • 0032545277 scopus 로고    scopus 로고
    • Differential activity of the G protein beta-5 gamma-2 subunit at receptors and effectors
    • Lindorfer MA, Myung CS, Savino Y, Yasuda H, Khazan R, Garrison JC (1998) Differential activity of the G protein beta-5 gamma-2 subunit at receptors and effectors. J Biol Chem 273: 34429-34436.
    • (1998) J Biol Chem , vol.273 , pp. 34429-34436
    • Lindorfer, M.A.1    Myung, C.S.2    Savino, Y.3    Yasuda, H.4    Khazan, R.5    Garrison, J.C.6
  • 56
    • 0032528863 scopus 로고    scopus 로고
    • Phosducin induces a structural change in transducin betagamma
    • Loew A, Ho Y, Blundell T, Bax B (1998) Phosducin induces a structural change in transducin betagamma. Structure 8: 1007-1019.
    • (1998) Structure , vol.8 , pp. 1007-1019
    • Loew, A.1    Ho, Y.2    Blundell, T.3    Bax, B.4
  • 57
    • 2442479974 scopus 로고    scopus 로고
    • Role of the isoprenyl pocket of the G protein beta gamma subunit complex in the binding of phosducin and phosducin-like protein
    • Lukov GL, Myung CS, McIntire WE, Shao J, Zimmerman SS, Garrison JC, Willardson BM (2004) Role of the isoprenyl pocket of the G protein beta gamma subunit complex in the binding of phosducin and phosducin-like protein. Biochemistry 43(19): 5651-5660. doi: 10. 1021/bi035903u.
    • (2004) Biochemistry , vol.43 , Issue.19 , pp. 5651-5660
    • Lukov, G.L.1    Myung, C.S.2    McIntire, W.E.3    Shao, J.4    Zimmerman, S.S.5    Garrison, J.C.6    Willardson, B.M.7
  • 58
    • 21244502200 scopus 로고    scopus 로고
    • Phosducin-like protein acts as a molecular chaperone for G protein betagamma dimer assembly
    • Lukov GL, Hu T, McLaughlin JN, Hamm HE, Willardson BM (2005) Phosducin-like protein acts as a molecular chaperone for G protein betagamma dimer assembly. EMBO J 24: 1965-1975.
    • (2005) EMBO J , vol.24 , pp. 1965-1975
    • Lukov, G.L.1    Hu, T.2    McLaughlin, J.N.3    Hamm, H.E.4    Willardson, B.M.5
  • 59
    • 33746816585 scopus 로고    scopus 로고
    • Mechanism of assembly of G protein betagamma subunits by protein kinase CK2-phosphorylated phosducin-like protein and the cytosolic chaperonin complex
    • Lukov GL, Baker CM, Ludtke PJ, Hu T, Carter MD, Hackett RA, Thulin CD, Willardson BM (2006) Mechanism of assembly of G protein betagamma subunits by protein kinase CK2-phosphorylated phosducin-like protein and the cytosolic chaperonin complex. J Biol Chem 281(31): 22261-22274. doi: 10. 1074/jbc. M601590200.
    • (2006) J Biol Chem , vol.281 , Issue.31 , pp. 22261-22274
    • Lukov, G.L.1    Baker, C.M.2    Ludtke, P.J.3    Hu, T.4    Carter, M.D.5    Hackett, R.A.6    Thulin, C.D.7    Willardson, B.M.8
  • 60
    • 34347357654 scopus 로고    scopus 로고
    • Assembly and trafficking of heterotrimeric G proteins
    • Marrari Y, Crouthamel M, Irannejad R, Wedegaertner PB (2007) Assembly and trafficking of heterotrimeric G proteins. Biochemistry 46(26): 7665-7677. doi: 10. 1021/bi700338m.
    • (2007) Biochemistry , vol.46 , Issue.26 , pp. 7665-7677
    • Marrari, Y.1    Crouthamel, M.2    Irannejad, R.3    Wedegaertner, P.B.4
  • 62
    • 0034193525 scopus 로고    scopus 로고
    • The interaction of the chaperonin tailless complex polypeptide 1 (TCP1) ring complex (TRiC) with ribosome-bound nascent chains examined using photo-cross-linking
    • McCallum CD, Do H, Johnson AE, Frydman J (2000) The interaction of the chaperonin tailless complex polypeptide 1 (TCP1) ring complex (TRiC) with ribosome-bound nascent chains examined using photo-cross-linking. J Cell Biol 149(3): 591-602.
    • (2000) J Cell Biol , vol.149 , Issue.3 , pp. 591-602
    • McCallum, C.D.1    Do, H.2    Johnson, A.E.3    Frydman, J.4
  • 63
    • 0035844213 scopus 로고    scopus 로고
    • The G protein beta subunit is a determinant in the coupling of Gs to the beta-1 adrenergic and A2a adenosine receptors
    • McIntire WE, MacCleery G, Garrison JC (2001) The G protein beta subunit is a determinant in the coupling of Gs to the beta-1 adrenergic and A2a adenosine receptors. J Biol Chem 276: 15801-15809.
    • (2001) J Biol Chem , vol.276 , pp. 15801-15809
    • McIntire, W.E.1    McCleery, G.2    Garrison, J.C.3
  • 64
    • 33749038655 scopus 로고    scopus 로고
    • Influence of differential stability of G protein dimers containing the 11 subunit on functional activity at the M1 muscarinic receptor, A1 adenosine receptor, and phospholipase C
    • McIntire WE, MacCleery G, Murphree LJ, Kerchner KR, Linden J, Garrison JC (2006) Influence of differential stability of G protein dimers containing the 11 subunit on functional activity at the M1 muscarinic receptor, A1 adenosine receptor, and phospholipase C. Biochemistry 45: 11616-11631.
    • (2006) Biochemistry , vol.45 , pp. 11616-11631
    • McIntire, W.E.1    McCleery, G.2    Murphree, L.J.3    Kerchner, K.R.4    Linden, J.5    Garrison, J.C.6
  • 66
    • 0029074154 scopus 로고
    • The G protein gamma subunit. Requirements for dimerization with beta subunits
    • Mende U, Schmidt CJ, Yi F, Spring DJ, Neer EJ (1995) The G protein gamma subunit. Requirements for dimerization with beta subunits. J Biol Chem 270: 15892-15898.
    • (1995) J Biol Chem , vol.270 , pp. 15892-15898
    • Mende, U.1    Schmidt, C.J.2    Yi, F.3    Spring, D.J.4    Neer, E.J.5
  • 67
    • 33745234272 scopus 로고    scopus 로고
    • Analysis of G protein betagamma dimer formation in live cells using multicolor bimolecularfluorescence complementation demonstrates preferences of beta1 for particular gamma subunits
    • Mervine SM, Yost EA, Sabo JL, Hynes TR, Berlot CH (2006) Analysis of G protein betagamma dimer formation in live cells using multicolor bimolecularfluorescence complementation demonstrates preferences of beta1 for particular gamma subunits. Mol Pharmacol 70: 194-205.
    • (2006) Mol Pharmacol , vol.70 , pp. 194-205
    • Mervine, S.M.1    Yost, E.A.2    Sabo, J.L.3    Hynes, T.R.4    Berlot, C.H.5
  • 68
    • 0038737003 scopus 로고    scopus 로고
    • Closing the folding chamber of the eukaryotic chaperonin requires the transition state of ATP hydrolysis
    • Meyer AS, Gillespie JR, Walther D, Millet IA, Doniach S, Frydman J (2003) Closing the folding chamber of the eukaryotic chaperonin requires the transition state of ATP hydrolysis. Cell 113(3): 369-381.
    • (2003) Cell , vol.113 , Issue.3 , pp. 369-381
    • Meyer, A.S.1    Gillespie, J.R.2    Walther, D.3    Millet, I.A.4    Doniach, S.5    Frydman, J.6
  • 69
    • 0036732940 scopus 로고    scopus 로고
    • Membrane trafficking of heterotrimeric G proteins via the endoplasmic reticulum and Golgi
    • Michaelson D, Ahearn I, Bergo M, Young S, Philips M (2002) Membrane trafficking of heterotrimeric G proteins via the endoplasmic reticulum and Golgi. Mol Biol Cell 13: 3294-3302.
    • (2002) Mol Biol Cell , vol.13 , pp. 3294-3302
    • Michaelson, D.1    Ahearn, I.2    Bergo, M.3    Young, S.4    Philips, M.5
  • 71
    • 0027090202 scopus 로고
    • Influence of gamma subunit prenylation on association of guanine nucleotide binding regulatory proteins with membranes
    • Muntz KH, Sternweis PC, Gilman AG, Mumby SM (1993) Influence of gamma subunit prenylation on association of guanine nucleotide binding regulatory proteins with membranes. Mol Biol Cell 3: 49-61.
    • (1993) Mol Biol Cell , vol.3 , pp. 49-61
    • Muntz, K.H.1    Sternweis, P.C.2    Gilman, A.G.3    Mumby, S.M.4
  • 72
    • 0028932506 scopus 로고
    • Molecular cloning and characterization of the G protein gamma subunit of cone photoreceptors
    • Ong O, Yamane HK, Phan KB, Fong HKW, Bok D, Lee RH, Fung BK (1995) Molecular cloning and characterization of the G protein gamma subunit of cone photoreceptors. J Biol Chem 270: 8495-8500.
    • (1995) J Biol Chem , vol.270 , pp. 8495-8500
    • Ong, O.1    Yamane, H.K.2    Phan, K.B.3    Fong, H.K.W.4    Bok, D.5    Lee, R.H.6    Fung, B.K.7
  • 73
    • 80053345905 scopus 로고    scopus 로고
    • SignalP 4. 0: Discriminating signal peptides from transmembrane regions
    • Petersen TM, Brunak S, von Heijne G, Nielsen H (2011) SignalP 4. 0: discriminating signal peptides from transmembrane regions. Nat Methods 8: 785-786.
    • (2011) Nat Methods , vol.8 , pp. 785-786
    • Petersen, T.M.1    Brunak, S.2    von Heijne, G.3    Nielsen, H.4
  • 74
    • 60549101657 scopus 로고    scopus 로고
    • Gbeta3 Forms distinct dimers with specific Ggamma subunits and preferentially activates the beta3 isoform of phospholipase C
    • pii: S0898-6568(09)00017-5
    • Poon LS, Chan AS, Wong YH (2009) Gbeta3 Forms distinct dimers with specific Ggamma subunits and preferentially activates the beta3 isoform of phospholipase C. Cell Signal 21(5): 737-744. doi: 10. 1016/j. cellsig. 2009. 01. 018, pii: S0898-6568(09)00017-5.
    • (2009) Cell Signal , vol.21 , Issue.5 , pp. 737-744
    • Poon, L.S.1    Chan, A.S.2    Wong, Y.H.3
  • 75
    • 0026655342 scopus 로고
    • Interaction between G protein beta and gamma subunit types is selective
    • Pronin AN, Gautam N (1992) Interaction between G protein beta and gamma subunit types is selective. Proc Natl Acad Sci U S A 89: 6220-6224.
    • (1992) Proc Natl Acad Sci U S A , vol.89 , pp. 6220-6224
    • Pronin, A.N.1    Gautam, N.2
  • 76
    • 0029099297 scopus 로고
    • Isolation of cDNA clones encoding eight different human G protein gamma subunits, including three novel forms designated the gamma-4, gamma-10 and gamma-11 subunits
    • Ray K, Kunsch C, Bonner LM, Robishaw JD (1995) Isolation of cDNA clones encoding eight different human G protein gamma subunits, including three novel forms designated the gamma-4, gamma-10 and gamma-11 subunits. J Biol Chem 270: 21765-21771.
    • (1995) J Biol Chem , vol.270 , pp. 21765-21771
    • Ray, K.1    Kunsch, C.2    Bonner, L.M.3    Robishaw, J.D.4
  • 77
    • 0030890789 scopus 로고    scopus 로고
    • Assembly and intracellular targeting of the beta-gamma subunits of heterotrimer G proteins
    • Rehm A, Ploegh HL (1997) Assembly and intracellular targeting of the beta-gamma subunits of heterotrimer G proteins. J Cell Biol 137: 305-317.
    • (1997) J Cell Biol , vol.137 , pp. 305-317
    • Rehm, A.1    Ploegh, H.L.2
  • 78
    • 0033531794 scopus 로고    scopus 로고
    • The alpha 2A-adrenergic receptor discriminates between Gi heterotrimers of different beta gamma subunit composition in Sf9 insect cell membranes
    • Richardson M, Robishaw JD (1999) The alpha 2A-adrenergic receptor discriminates between Gi heterotrimers of different beta gamma subunit composition in Sf9 insect cell membranes. J Biol Chem 274: 13525-13533.
    • (1999) J Biol Chem , vol.274 , pp. 13525-13533
    • Richardson, M.1    Robishaw, J.D.2
  • 80
    • 0026644614 scopus 로고
    • Production, processing and partial purification of functional G protein beta/gamma subunits in baculovirus infected insect cells
    • Robishaw JD, Kalman VK, Proulx KL (1992) Production, processing and partial purification of functional G protein beta/gamma subunits in baculovirus infected insect cells. Biochem J 286: 677-680.
    • (1992) Biochem J , vol.286 , pp. 677-680
    • Robishaw, J.D.1    Kalman, V.K.2    Proulx, K.L.3
  • 82
    • 0038356731 scopus 로고    scopus 로고
    • The human G protein beta4 subunit: Gene structure, expression, Ggamma and effector interaction
    • Rosskopf D, Nikula C, Manthey I, Joisten M, Frey U, Kohnen S, Siffert W (2003b) The human G protein beta4 subunit: gene structure, expression, Ggamma and effector interaction. FEBS Lett 544: 27-32.
    • (2003) FEBS Lett , vol.544 , pp. 27-32
    • Rosskopf, D.1    Nikula, C.2    Manthey, I.3    Joisten, M.4    Frey, U.5    Kohnen, S.6    Siffert, W.7
  • 83
    • 39149143645 scopus 로고    scopus 로고
    • Chaperone machines in action
    • Saibil HR (2008) Chaperone machines in action. Curr Opin Struct Biol 18(1): 35-42. doi: 10. 1016/j. sbi. 2007. 11. 006.
    • (2008) Curr Opin Struct Biol , vol.18 , Issue.1 , pp. 35-42
    • Saibil, H.R.1
  • 85
    • 0025898422 scopus 로고
    • In vitro synthesis of G protein beta/gamma dimers
    • Schmidt CJ, Neer EJ (1991) In vitro synthesis of G protein beta/gamma dimers. J Biol Chem 266: 4538-4544.
    • (1991) J Biol Chem , vol.266 , pp. 4538-4544
    • Schmidt, C.J.1    Neer, E.J.2
  • 86
    • 0026655036 scopus 로고
    • Specificity of G protein beta and gamma subunit interactions
    • Schmidt CJ, Thomas TC, Levine MA, Neer EJ (1992) Specificity of G protein beta and gamma subunit interactions. J Biol Chem 267: 13807-13810.
    • (1992) J Biol Chem , vol.267 , pp. 13807-13810
    • Schmidt, C.J.1    Thomas, T.C.2    Levine, M.A.3    Neer, E.J.4
  • 87
    • 0029935648 scopus 로고    scopus 로고
    • Inhibition of G protein beta/gamma subunit function by phosducin-like protein
    • Schroder S, Lohse MJ (1996) Inhibition of G protein beta/gamma subunit function by phosducin-like protein. Proc Natl Acad Sci U S A 93: 2100-2104.
    • (1996) Proc Natl Acad Sci U S A , vol.93 , pp. 2100-2104
    • Schroder, S.1    Lohse, M.J.2
  • 88
    • 0035952766 scopus 로고    scopus 로고
    • Heterotrimeric G-protein betagamma dimers in growth and differentiation
    • Schwindinger WF, Robishaw JD (2001) Heterotrimeric G-protein betagamma dimers in growth and differentiation. Oncogene 20: 1653-1660.
    • (2001) Oncogene , vol.20 , pp. 1653-1660
    • Schwindinger, W.F.1    Robishaw, J.D.2
  • 90
    • 0141613640 scopus 로고    scopus 로고
    • Tric/CCT cooperates with different upstream chaperones in the folding of distinct perotein classes
    • Siegers K, Bolter B, Schwarz JP, Bottcher UMK, Guha S, Hartl FU (2003) Tric/CCT cooperates with different upstream chaperones in the folding of distinct perotein classes. EMBO J 22: 5230-5240.
    • (2003) EMBO J , vol.22 , pp. 5230-5240
    • Siegers, K.1    Bolter, B.2    Schwarz, J.P.3    Bottcher, U.M.K.4    Guha, S.5    Hartl, F.U.6
  • 91
    • 0026009360 scopus 로고
    • G protein beta/gamma dimers. Membrane targeting requires subunit coexpression and intact gamma C-a-a-X domain
    • Simonds WF, Butrynski JE, Gautam N, Unson CG, Spiegel AM (1991) G protein beta/gamma dimers. Membrane targeting requires subunit coexpression and intact gamma C-a-a-X domain. J Biol Chem 266: 5363-5366.
    • (1991) J Biol Chem , vol.266 , pp. 5363-5366
    • Simonds, W.F.1    Butrynski, J.E.2    Gautam, N.3    Unson, C.G.4    Spiegel, A.M.5
  • 92
    • 1042278172 scopus 로고    scopus 로고
    • Selective contribution of eukaryotic prefoldin subunits to actin and tubulin binding
    • Simons CT, Staes A, Rommelaere H, Ampe C, Lewis SA, Cowan NJ (2004) Selective contribution of eukaryotic prefoldin subunits to actin and tubulin binding. J Biol Chem 279: 4196-4203.
    • (2004) J Biol Chem , vol.279 , pp. 4196-4203
    • Simons, C.T.1    Staes, A.2    Rommelaere, H.3    Ampe, C.4    Lewis, S.A.5    Cowan, N.J.6
  • 94
    • 3543099503 scopus 로고    scopus 로고
    • Palmitoylation of intracellular signaling proteins: Regulation and function
    • Smotrys JE, Linder ME (2004) Palmitoylation of intracellular signaling proteins: regulation and function. Annu Rev Biochem 73: 559-587.
    • (2004) Annu Rev Biochem , vol.73 , pp. 559-587
    • Smotrys, J.E.1    Linder, M.E.2
  • 95
    • 0030034646 scopus 로고    scopus 로고
    • Crystal structure of a G protein beta/gamma dimer at 2. 1 Angstrom resolution
    • Sondek J, Bohm A, Lambright DG, Hamm HE, Sigler PB (1996) Crystal structure of a G protein beta/gamma dimer at 2. 1 Angstrom resolution. Nature 379: 369-374.
    • (1996) Nature , vol.379 , pp. 369-374
    • Sondek, J.1    Bohm, A.2    Lambright, D.G.3    Hamm, H.E.4    Sigler, P.B.5
  • 96
    • 7444231693 scopus 로고    scopus 로고
    • Mechanism of the eukaryotic chaperonin: Protein folding in the chamber of secrets
    • Spiess C, Meyer AS, Reissmann S, Frydman J (2004) Mechanism of the eukaryotic chaperonin: protein folding in the chamber of secrets. Trends Cell Biol 14(11): 598-604. doi: 10. 1016/j. tcb. 2004. 09. 015.
    • (2004) Trends Cell Biol , vol.14 , Issue.11 , pp. 598-604
    • Spiess, C.1    Meyer, A.S.2    Reissmann, S.3    Frydman, J.4
  • 98
    • 2942617262 scopus 로고    scopus 로고
    • Exocytic pathway-independent plasma membrane targeting of heterotrimeric G proteins
    • Takida S, Wedegaertner DP (2004) Exocytic pathway-independent plasma membrane targeting of heterotrimeric G proteins. FEBS Lett 567: 2009-2213.
    • (2004) FEBS Lett , vol.567 , pp. 2009-2213
    • Takida, S.1    Wedegaertner, D.P.2
  • 99
    • 0030924690 scopus 로고    scopus 로고
    • Interaction of phosducin-like protein with G protein betagamma subunits
    • Thibault C, Sganga MW, MIles MF (1997) Interaction of phosducin-like protein with G protein betagamma subunits. J Biol Chem 272: 12253-12256.
    • (1997) J Biol Chem , vol.272 , pp. 12253-12256
    • Thibault, C.1    Sganga, M.W.2    Miles, M.F.3
  • 104
    • 0032530652 scopus 로고    scopus 로고
    • Structural basis of activity and subunit recognition in G protein heterotrimers
    • Wall MA, Posner BA, Sprang SR (1998) Structural basis of activity and subunit recognition in G protein heterotrimers. Structure 6: 1169-1183.
    • (1998) Structure , vol.6 , pp. 1169-1183
    • Wall, M.A.1    Posner, B.A.2    Sprang, S.R.3
  • 105
    • 0028068380 scopus 로고
    • Afifth member of the mammalian G-protein beta subunit family
    • Watson AJ, Katz A, Simon MI (1994) Afifth member of the mammalian G-protein beta subunit family. J Biol Chem 269: 22150-22156.
    • (1994) J Biol Chem , vol.269 , pp. 22150-22156
    • Watson, A.J.1    Katz, A.2    Simon, M.I.3
  • 106
    • 0029985041 scopus 로고    scopus 로고
    • A novel form of the G protein beta subunit G beta-5 is specifically expressed in the vertebrate retina
    • Watson AJ, Aragay AM, Slepak VZ, Simon MI (1996) A novel form of the G protein beta subunit G beta-5 is specifically expressed in the vertebrate retina. J Biol Chem 271: 28154-28160.
    • (1996) J Biol Chem , vol.271 , pp. 28154-28160
    • Watson, A.J.1    Aragay, A.M.2    Slepak, V.Z.3    Simon, M.I.4
  • 107
    • 33745989271 scopus 로고    scopus 로고
    • Role of the chaperonin CCT/TRiC complex in G protein betagamma dimer assembly
    • Wells CA, Dingus J, Hildebrandt JD (2006) Role of the chaperonin CCT/TRiC complex in G protein betagamma dimer assembly. J Biol Chem 281: 20221-20232.
    • (2006) J Biol Chem , vol.281 , pp. 20221-20232
    • Wells, C.A.1    Dingus, J.2    Hildebrandt, J.D.3
  • 108
    • 35148868765 scopus 로고    scopus 로고
    • Function of phosducin-like proteins in G protein signaling and chaperone-assisted protein folding
    • Willardson BM, Howlett AC (2007) Function of phosducin-like proteins in G protein signaling and chaperone-assisted protein folding. Cell Signal 19(12): 2417-2427. doi: 10. 1016/j. cellsig. 2007. 06. 013.
    • (2007) Cell Signal , vol.19 , Issue.12 , pp. 2417-2427
    • Willardson, B.M.1    Howlett, A.C.2
  • 109
    • 18344394166 scopus 로고    scopus 로고
    • Post-prenylation-processing enzymes as new targets in oncogenesis
    • Winter-Vann AM, Casey PJ (2005) Post-prenylation-processing enzymes as new targets in oncogenesis. Nat Rev Cancer 5: 407-412.
    • (2005) Nat Rev Cancer , vol.5 , pp. 407-412
    • Winter-Vann, A.M.1    Casey, P.J.2
  • 110
  • 111
    • 0037481887 scopus 로고    scopus 로고
    • T-type calcium channel regulation by specific G-protein bold betabig gamma subunits
    • Wolfe JT, Wang H, Howard J, Garrison JC, Barrett PQ (2003) T-type calcium channel regulation by specific G-protein bold betabig gamma subunits. Nature 424: 209-213.
    • (2003) Nature , vol.424 , pp. 209-213
    • Wolfe, J.T.1    Wang, H.2    Howard, J.3    Garrison, J.C.4    Barrett, P.Q.5
  • 112
    • 0030002944 scopus 로고    scopus 로고
    • Differential ability to form the G protein beta/gamma complex among members of the beta and gamma subunit families
    • Yan K, Kalyanaraman V, Gautam N (1996) Differential ability to form the G protein beta/gamma complex among members of the beta and gamma subunit families. J Biol Chem 271: 7141-7146.
    • (1996) J Biol Chem , vol.271 , pp. 7141-7146
    • Yan, K.1    Kalyanaraman, V.2    Gautam, N.3
  • 113
    • 34748916964 scopus 로고    scopus 로고
    • Live cell analysis of G protein beta5 complex formation, function, and targeting
    • Yost EA, Mervine SM, Sabo JL, Hynes TR, Berlot CH (2007) Live cell analysis of G protein beta5 complex formation, function, and targeting. Mol Pharmacol 72: 812-825.
    • (2007) Mol Pharmacol , vol.72 , pp. 812-825
    • Yost, E.A.1    Mervine, S.M.2    Sabo, J.L.3    Hynes, T.R.4    Berlot, C.H.5
  • 114
    • 0030468336 scopus 로고    scopus 로고
    • Selective activation of effector pathways by brain specific G protein beta-5
    • Zhang S, Coso OA, Lee C, Gutkind S, Simonds WF (1996) Selective activation of effector pathways by brain specific G protein beta-5. J Biol Chem 271: 33575-33579.
    • (1996) J Biol Chem , vol.271 , pp. 33575-33579
    • Zhang, S.1    Coso, O.A.2    Lee, C.3    Gutkind, S.4    Simonds, W.F.5
  • 115
    • 0034307596 scopus 로고    scopus 로고
    • Selective regulation of N-type Ca channels by different combinations of G-protein beta/gamma subunits and RGS proteins
    • Zhou JY, Siderovski DP, Miller RJ (2000) Selective regulation of N-type Ca channels by different combinations of G-protein beta/gamma subunits and RGS proteins. J Neurosci 20: 7143-7148.
    • (2000) J Neurosci , vol.20 , pp. 7143-7148
    • Zhou, J.Y.1    Siderovski, D.P.2    Miller, R.J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.