Abstract
The heterotrimeric GTP-binding proteins (G proteins) are the canonical cellular machinery used with the approximately 700 G protein-coupled receptors (GPCRs) in the human genome to transduce extracellular signals across the plasma membrane. The synthesis of the constituent G protein subunits, and their assembly into Gβγ dimers and G protein heterotrimers, determines the signaling repertoire for G-protein/GPCR signaling in cells. These synthesis/assembly processes are intimately related to two other overlapping events in the intricate pathway leading to formation of G protein signaling complexes, posttranslational modification and intracellular trafficking of G proteins. The assembly of the Gβγ dimer is a complex process involving multiple accessory proteins and organelles. The mechanisms involved are becoming increasingly appreciated, but are still incompletely understood. In vitro and in vivo (cellular) studies provide different perspectives of these processes, and a comparison of them can provide insight into both our current level of understanding and directions to be taken in future investigations.
Access this chapter
Tax calculation will be finalised at checkout
Purchases are for personal use only
References
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
Bayewitch ML, Avidor-Reiss T, Levy R, Pfeuffer T, Nevo I, Simonds WF, Vogel Z (1998) Inhibition of adenylyl cyclase isoforms V and VI by various Gßγ subunits. FASEB J 12:1019–1025
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
Birnbaumer L (1990) G proteins in signal transduction. Annu Rev Pharmacol Toxicol 30:675–705
Blaauw M, Knol JC, Kortholt A, Roelofs J, Ruchira PM, Visser AJWG, van Haastert PJM (2003) Phosducin-like proteins in dictyostelium discoideum: implications for the phosducin family of proteins. EMBO J 22:5047–5057
Bourne HR, Sanders DA, McCormick F (1990) The GTPase superfamily: a conserved switch for diverse cell functions. Nature 348:125–132
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
Cabrera-Vera TM, VanHauwe J, Thomas TO, Medkova M, Prieninger A, Mazzoni MR, Hamm HE (2003) Insights into G protein structure, function, and regulation. Endocr Rev 24:765–781
Cook LA, Schey KL, Wilcox MD, Dingus J, Ettling R, Nelson T, Knapp DR, Hildebrandt JD (2006) Proteomic analysis of bovine brain G protein gamma subunit processing heterogeneity. Mol Cell Proteomics 5:671–685
Craig E (2003) Eukaryotic chaperonins: lubricating the folding of WD-repeat proteins. Curr Biol 13:R904–R905
Craig E, Huang P, Aron R, Andrew A (2006) The diverse roles of J-proteins, the obligate Hsp70 co-chaperone. Rev Physiol Biochem Pharmacol 156:1–21
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
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
Downes GB, Gautam N (1999) The G protein subunit gene families. Genomics 62:544–552
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
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
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
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
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
Fletcher JE, Lindorfer MA, DeFilippo JM, Yasuda H, Guilmard M, Garrison JC (1998) The G protein b5 subunit interacts selectively with the Gq alpha subunit. J Biol Chem 273:636–644
Ford CE, Skiba NP, Bae H, Daaka Y, Reuveny E, Shekter LR, Rosal R, Weng G, Yang C-S, Iyengar R, Miller RJ, Jan LY, Lefkowitz RJ, Hamm HE (1998) Molecular basis for interactions of G protein beta-gamma subunits with effectors. Science 280:1271–1274
Fu H-W, Casey P (1999) Enzymology and biology of CaaX protein prenylation. Recent Prog Horm Res 54:315–343
Gabay M, Pinter ME, Wright FA, Chan P, Murphy AJ, Valenzuela DM, Yancopoulos GD, Tall GG (2011) Ric-8 proteins are molecular chaperones that direct nascent G protein alpha subunit membrane association. Sci Signal 4:1–13
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
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
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
Garritsen A, Simonds WF (1994) Multiple domains of G protein beta confer subunit specificity in bg interactions. J Biol Chem 269:24418–24423
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
Gilman AG (1987) G proteins: transducers of receptor-generated signals. Annu Rev Biochem 56:615–649
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
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
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
Hamm HE (1998) The many faces of G protein signaling. J Biol Chem 273:669–672
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
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
Higgins JB, Casey PJ (1996) The role of prenylation in G protein assembly and function. Cell Signal 8:433–437
Hildebrandt JD (1997) Role of subunit diversity in signaling by heterotrimeric G proteins. Biochem Pharmacol 54:325–339
Hildebrandt JD (2011) Heterogeneous prenyl processing of the heterotrimeric G protein gamma subunits. The Enzym Prot Prenylation Part A 29:97–124
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
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
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
Humrich J, Bermel C, Bunemann M, Harmark L, Frost R, Quitterer U, Lohse MJ (2005) Phosducin-like 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
Hynes TR, Tang L, Mervine SM, Sabo JL, Yost EA, Devreotes PN, Berlot CH (2004) Visualization of G protein betagamma dimers using bimolecular fluorescence complementation demonstrates roles for both beta and gamma in subcellular targeting. J Biol Chem 279:30279–30286
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
Jewett AI, Shea JE (2010) Reconciling theories of chaperonin accelerated folding with experimental evidence. Cell Mol Life Sci 67(2):255–276
Jones MB, Garrison JC (1999) Instability of the G protein beta5 subunit in detergent. Anal Biochem 268:126–133
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
Kilpatrick EL, Hildebrandt JD (2007) Sequence dependence and differential expression of Gγ5 subunit isoforms of the heterotrimeric G proteins variably processed after prenylation in mammalian cells. J Biol Chem 282:14038–14047
Kleuss C, Krause E (2003) Galpha(s) is palmitoylated at the N-terminal glycine. EMBO J 22:826–832
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
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
Lambright DG, Sondek J, Bohm A, Skiba NP, Hamm HE, Sigler PB (1996) The 2.0 Angstrom crystal structure of a heterotrimeric G protein. Nature 379:311–319
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
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
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
Loew A, Ho Y, Blundell T, Bax B (1998) Phosducin induces a structural change in transducin betagamma. Structure 8:1007–1019
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
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
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
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
Martin-Benito J, Bertrand S, Hu T, Ludtke PJ, McLaughlin JN, Willardson BM, Carrascosa JL, Valpuesta JM (2004) Structure of the complex between the cytosolic chaperonin CCT and phosducin-like protein. Proc Natl Acad Sci U S A 101:17410–17415
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
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
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
McLaughlin JN, Thulin CD, Hart SJ, Resing KA, Ahn NG, Willardson BM (2002) Regulatory interaction of phosducin-like protein with the cytosolic chaperonin complex. Proc Natl Acad Sci U S A 99:7962–7967
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
Mervine SM, Yost EA, Sabo JL, Hynes TR, Berlot CH (2006) Analysis of G protein betagamma dimer formation in live cells using multicolor bimolecular fluorescence complementation demonstrates preferences of beta1 for particular gamma subunits. Mol Pharmacol 70:194–205
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
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
Mumby SM, Casey PJ, Gilman AG, Gutowski S, Sternweis PC (1990) G protein gamma subunits contain a 20-carbon isoprenoid. Proc Natl Acad Sci U S A 87:5873–5877
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
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
Petersen TM, Brunak S, von Heijne G, Nielsen H (2011) SignalP 4.0: discriminating signal peptides from transmembrane regions. Nat Methods 8:785–786
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
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
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
Rehm A, Ploegh HL (1997) Assembly and intracellular targeting of the beta-gamma subunits of heterotrimer G proteins. J Cell Biol 137:305–317
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
Riggs DL, Cox MB, Cheung-Flynn J, Prapapanich V, Carrigan PE, Smith DF (2004) Functional specificity of co-chaperone interactions with Hsp90 client proteins. Crit Rev Biochem Mol Biol 39:279–295
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
Rosskopf D, Koch K, Habick C, Geerder J, Ludwig A, Wwilhelms S, Jakobs KH, Sifffert W (2003a) Interaction of Gbeta3s, a splice variant of the G-protein Gbeta3, with ggamma- and galpha-proteins. Cell Signal 5648:1–10
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
Saibil HR (2008) Chaperone machines in action. Curr Opin Struct Biol 18(1):35–42. doi:10.1016/j.sbi.2007.11.006
Schaber MD, O’Hara MB, Garsky VM, Mosser SC, Bergstrom JD, Moores SL, Marshall MS, Friedman PA, Dixon RA, Gibbs JB (1990) Polyisoprenylation of Ras in vitro by a farnesyl-protein transferase. J Biol Chem 265(25):14701–14704
Schmidt CJ, Neer EJ (1991) In vitro synthesis of G protein beta/gamma dimers. J Biol Chem 266:4538–4544
Schmidt CJ, Thomas TC, Levine MA, Neer EJ (1992) Specificity of G protein beta and gamma subunit interactions. J Biol Chem 267:13807–13810
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
Schwindinger WF, Robishaw JD (2001) Heterotrimeric G-protein betagamma dimers in growth and differentiation. Oncogene 20:1653–1660
Seabra MC, Goldstein JL, Sudhof TC, Brown MS (1992) Rab geranylgeranyl transferase. J Biol Chem 267:14497–14503
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
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
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
Smith T (2008) Diversity of WD-repeat proteins. Subcell Biochem Coronin Fam Protein 48:20–30
Smotrys JE, Linder ME (2004) Palmitoylation of intracellular signaling proteins: regulation and function. Annu Rev Biochem 73:559–587
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
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
Stirnimann CU, Petsalaki E, Russell RB, Muller CW (2010) WD40 Proteins propel cellular networks. Trends Biochem Sci 35:65–574
Takida S, Wedegaertner DP (2004) Exocytic pathway-independent plasma membrane targeting of heterotrimeric G proteins. FEBS Lett 567:2009–2213
Thibault C, Sganga MW, MIles MF (1997) Interaction of phosducin-like protein with G protein betagamma subunits. J Biol Chem 272:12253–12256
Ueda N, Iniguez-Lluhi JA, Lee E, Smrcka AV, Robishaw JD, Gilman AG (1994) G protein beta/gamma subunits. Simplified purification and properties of novel isoforms. J Biol Chem 269:4388–4395
Valpuesta JM, Martin-Benito J, Gomez-Puertas P, Carrascosa JL, Willison KR (2002) Structure and function of a protein folding machine: the eukaryotic cytosolic chaperonin CCT. FEBS Lett 529:11–16
Vane JR, Bakhle YS, Botting RM (1998) Cyclooxygenases 1 and 2. Annu Rev Pharmacol Toxicol 38:97–120
Wall MA, Coleman DE, Lee E, Iniguez-Lluhi JA, Posner BA, Gilman AG, Sprang SR (1995) The structure of the G protein heterotrimer G alpha-i1 beta-1 gamma-2. Cell 83:1047–1058
Wall MA, Posner BA, Sprang SR (1998) Structural basis of activity and subunit recognition in G protein heterotrimers. Structure 6:1169–1183
Watson AJ, Katz A, Simon MI (1994) A fifth member of the mammalian G-protein beta subunit family. J Biol Chem 269:22150–22156
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
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
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
Winter-Vann AM, Casey PJ (2005) Post-prenylation-processing enzymes as new targets in oncogenesis. Nat Rev Cancer 5:407–412
Witherow DS, Wang Q, Levay K, Cabera JL, Chen J, Willars GB, Slepak VZ (2000) Complexes of the G protein gbeta 5 with the regulators of G protein signaling RGS7 and RGS9. J Biol Chem 275:24872–24880
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
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
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
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
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
Author information
Authors and Affiliations
Corresponding author
Editor information
Editors and Affiliations
Rights and permissions
Copyright information
© 2012 Springer Science+Business Media Dordrecht
About this chapter
Cite this chapter
Dingus, J., Hildebrandt, J.D. (2012). Synthesis and Assembly of G Protein βγ Dimers: Comparison of In Vitro and In Vivo Studies. In: Dupré, D., Hébert, T., Jockers, R. (eds) GPCR Signalling Complexes – Synthesis, Assembly, Trafficking and Specificity. Subcellular Biochemistry, vol 63. Springer, Dordrecht. https://doi.org/10.1007/978-94-007-4765-4_9
Download citation
DOI: https://doi.org/10.1007/978-94-007-4765-4_9
Published:
Publisher Name: Springer, Dordrecht
Print ISBN: 978-94-007-4764-7
Online ISBN: 978-94-007-4765-4
eBook Packages: Biomedical and Life SciencesBiomedical and Life Sciences (R0)