Dopamine Receptor-interacting Protein 78 Acts as a Molecular Chaperone for Gγ Subunits before Assembly with Gβ

Heterotrimeric G proteins play a central role in intracellular communication mediated by extracellular signals, and both Gα and Gβγ subunits regulate effectors downstream of activated receptors. The particular constituents of the G protein heterotrimer affect both specificity and efficiency of signal transduction. However, little is known about mechanistic aspects of G protein assembly in the cell that would certainly contribute to formation of heterotrimers of specific composition. It was recently shown that phosducin-like protein (PhLP) modulated both Gβγ expression and subsequent signaling by chaperoning nascent Gβ and facilitating heterodimer formation with Gγ subunits (Lukov, G. L., Hu, T., McLaughlin, J. N., Hamm, H. E., and Willardson, B. M. (2005) EMBO J. 24, 1965-1975; Humrich, J., Bermel, C., Bunemann, M., Harmark, L., Frost, R., Quitterer, U., and Lohse, M. J. (2005) J. Biol. Chem. 280, 20042-20050). Here we demonstrate using a variety of techniques that DRiP78, an endoplasmic reticulum resident protein known to regulate the trafficking of several seven transmembrane receptors, interacts specifically with the Gγ subunit but not Gβ or Gα subunits. Furthermore, we demonstrate that DRiP78 and the Gβ subunit can compete for the Gγ subunit. DRiP78 also protects Gγ from degradation until a stable partner such as Gβ is provided. Furthermore, DRiP78 interaction may represent a mechanism for assembly of specific Gβγ heterodimers, as selectivity was observed among Gγ isoforms for interaction with DRiP78 depending on the presence of particular Gβ subunits. Interestingly, we could detect an interaction between DRiP78 and PhLP, suggesting a role of DRiP78 in the assembly of Gβγ by linking Gγ to PhLP·Gβ complexes. Our results, therefore, suggest a role of DRiP78 as a chaperone in the assembly of Gβγ subunits of the G protein. Heterotrimeric G proteins play a central role in intracellular communication mediated by extracellular signals, and both Gα and Gβγ subunits regulate effectors downstream of activated receptors. The particular constituents of the G protein heterotrimer affect both specificity and efficiency of signal transduction. However, little is known about mechanistic aspects of G protein assembly in the cell that would certainly contribute to formation of heterotrimers of specific composition. It was recently shown that phosducin-like protein (PhLP) modulated both Gβγ expression and subsequent signaling by chaperoning nascent Gβ and facilitating heterodimer formation with Gγ subunits (Lukov, G. L., Hu, T., McLaughlin, J. N., Hamm, H. E., and Willardson, B. M. (2005) EMBO J. 24, 1965-1975; Humrich, J., Bermel, C., Bunemann, M., Harmark, L., Frost, R., Quitterer, U., and Lohse, M. J. (2005) J. Biol. Chem. 280, 20042-20050). Here we demonstrate using a variety of techniques that DRiP78, an endoplasmic reticulum resident protein known to regulate the trafficking of several seven transmembrane receptors, interacts specifically with the Gγ subunit but not Gβ or Gα subunits. Furthermore, we demonstrate that DRiP78 and the Gβ subunit can compete for the Gγ subunit. DRiP78 also protects Gγ from degradation until a stable partner such as Gβ is provided. Furthermore, DRiP78 interaction may represent a mechanism for assembly of specific Gβγ heterodimers, as selectivity was observed among Gγ isoforms for interaction with DRiP78 depending on the presence of particular Gβ subunits. Interestingly, we could detect an interaction between DRiP78 and PhLP, suggesting a role of DRiP78 in the assembly of Gβγ by linking Gγ to PhLP·Gβ complexes. Our results, therefore, suggest a role of DRiP78 as a chaperone in the assembly of Gβγ subunits of the G protein. Seven transmembrane receptors (7TM-Rs) 3The abbreviations used are: 7TM-R, 7 transmembrane receptor; PhLP, phosducin-like protein; DRiP78, dopamine receptor-interacting protein 78; ER, endoplasmic reticulum; HA, hemagglutinin; GFP, green fluorescent protein; eGFP, enhanced GFP; BRET, bioluminescence resonance energy transfer; β2AR, β2-adrenergic receptor; shRNA, short hairpin RNA; YFP, yellow fluorescent protein; BiFC, bimolecular fluorescence complementation; HEK cells, human embryonic kidney cells; PBS, phosphate-buffered saline; Tricine, N-[2-hydroxy-1,1-bis(hydroxymethyl)ethyl]glycine; RFU, relative fluorescence units. 3The abbreviations used are: 7TM-R, 7 transmembrane receptor; PhLP, phosducin-like protein; DRiP78, dopamine receptor-interacting protein 78; ER, endoplasmic reticulum; HA, hemagglutinin; GFP, green fluorescent protein; eGFP, enhanced GFP; BRET, bioluminescence resonance energy transfer; β2AR, β2-adrenergic receptor; shRNA, short hairpin RNA; YFP, yellow fluorescent protein; BiFC, bimolecular fluorescence complementation; HEK cells, human embryonic kidney cells; PBS, phosphate-buffered saline; Tricine, N-[2-hydroxy-1,1-bis(hydroxymethyl)ethyl]glycine; RFU, relative fluorescence units. mediate a large variety of physiological events, from simple responses to endocrine mediators to complex behavioral events. Many diverse extracellular signals transduce signals via heterotrimeric G proteins (1Gainetdinov R.R. Premont R.T. Bohn L.M. Lefkowitz R.J. Caron M.G. Annu. Rev. Neurosci. 2004; 27: 107-144Crossref PubMed Scopus (676) Google Scholar). G protein heterotrimers are composed of α, β, and γ subunits. To date, 16 Gα, 5β, and 11γ human genes have been identified, and splice variants for many of these gene products exist (2Hurowitz E.H. Melnyk J.M. Chen Y.J. Kouros-Mehr H. Simon M.I. Shizuya H. DNA Res. 2000; 7: 111-120Crossref PubMed Scopus (135) Google Scholar). Interest originally was centered on Gα since it possesses the switch that activates and deactivates signal transduction through guanylyl nucleotide exchange and hydrolysis, respectively. Furthermore, the interaction of G proteins with receptors and effectors is dependent on the subtype of Gα in the G protein heterotrimer. Evidence supporting an increasing contribution of Gβγ subunits to receptor and effector interaction has accumulated (for review, see Ref. 3Robishaw J.D. Berlot C.H. Curr. Opin. Cell Biol. 2004; 16: 206-209Crossref PubMed Scopus (89) Google Scholar). Gβ and Gγ subunits tightly associate as a constitutive heterodimer (4Hildebrandt J.D. Codina J. Risinger R. Birnbaumer L. J. Biol. Chem. 1984; 259: 2039-2042Abstract Full Text PDF PubMed Google Scholar). Human Gγ isoforms are well conserved among vertebrates, although they differ considerably from each other, especially in the N-terminal region (5Cook L.A. Schey K.L. Cleator J.H. Wilcox M.D. Dingus J. Hildebrandt J.D. Protein Sci. 2001; 10: 2548-2555Crossref PubMed Scopus (23) Google Scholar). Reports suggest that Gγ subunits differ in their ability to interact with Gβ to form specific heterodimers, to interact with 7TM-Rs, and to modulate effectors (6Akgoz M. Azpiazu I. Kalyanaraman V. Gautam N. J. Biol. Chem. 2002; 277: 19573-19578Abstract Full Text Full Text PDF PubMed Scopus (32) Google Scholar, 7Azpiazu I. Gautam N. Methods Enzymol. 2002; 344: 112-125Crossref PubMed Scopus (8) Google Scholar, 8Chinault S.L. Blumer K.J. J. Biol. Chem. 2003; 278: 20638-20644Abstract Full Text Full Text PDF PubMed Scopus (5) Google Scholar, 9Wang Q. Jolly J.P. Surmeier J.D. Mullah B.M. Lidow M.S. Bergson C.M. Robishaw J.D. J. Biol. Chem. 2001; 276: 39386-39393Abstract Full Text Full Text PDF PubMed Scopus (61) Google Scholar). Gγ subunits are post-translationally modified by isoprenylation (10Gelb M.H. Scholten J.D. Sebolt-Leopold J.S. Curr. Opin. Chem. Biol. 1998; 2: 40-48Crossref PubMed Scopus (83) Google Scholar, 11Fu H.W. Casey P.J. Recent Prog. Horm. Res. 1999; 54: 313-342Google Scholar), and it has been suggested that Gβγ assembly into a stable heterodimeric complex precedes cytosolic prenylation of the C-terminal CAAX motif on Gγ (12Takida S. Wedegaertner P.B. J. Biol. Chem. 2003; 278: 17284-17290Abstract Full Text Full Text PDF PubMed Scopus (78) Google Scholar). It is also generally agreed that both isoprenylation of Gγ and association with Gα are essential for plasma membrane targeting of the Gβγ dimer (12Takida S. Wedegaertner P.B. J. Biol. Chem. 2003; 278: 17284-17290Abstract Full Text Full Text PDF PubMed Scopus (78) Google Scholar, 13Michaelson D. Ahearn I. Bergo M. Young S. Philips M. Mol. Biol. Cell. 2002; 13: 3294-3302Crossref PubMed Scopus (109) Google Scholar, 14Takida S. Wedegaertner P.B. FEBS Lett. 2004; 567: 209-213Crossref PubMed Scopus (28) Google Scholar). To date little is known about mechanistic aspects of Gβγ heterodimer formation, i.e. what facilitates their initial meeting and determines are in been that phosducin-like protein (PhLP) interacts with Gβγ subunits J. Biol. Chem. Full Text Full Text PDF PubMed Scopus Google Scholar, C.M. J. B. 1998; PubMed Scopus Google Scholar). has as a chaperone for the subunit as can in the of Gγ J. M. L. R. J. Biol. Chem. Full Text Full Text PDF PubMed Scopus Google Scholar, B.M. EMBO J. PubMed Scopus Google Scholar). the in using in an of Gβγ expression and signaling to a in the ability to form between nascent Gβ and Gγ subunits B.M. EMBO J. PubMed Scopus Google Scholar). of is to Gγ suggesting that the assembly of Gβγ may a B.M. EMBO J. PubMed Scopus Google Scholar, C.M. P.J. M.D. B.M. J. Biol. Chem. Full Text Full Text PDF PubMed Scopus Google Scholar). also in since Gβ and Gγ association was in a R. M. P.J. Mol. Cell. Biol. PubMed Scopus Google as well as in of the Gβ subunit of in a of G protein signaling V. M. M. Biol. PubMed Scopus Google Scholar). for between proteins and of G or we observed that the dopamine receptor-interacting protein could interact specifically with subunits in the of DRiP78 for is an protein known to regulate the to plasma membrane of and receptors M. Cell Biol. 2001; PubMed Scopus Google Scholar, M. R. G. 2002; PubMed Scopus Google Scholar). DRiP78 a conserved motif in these particular and motif is in a of we suggest that DRiP78 also as a chaperone with Gγ to modulate Gβγ from the modified and from and protein from and from and from of and from receptor and used as N. N. L. M. J. Biol. Chem. 2002; 277: Full Text Full Text PDF PubMed Scopus Google Scholar, M. M. 2: PubMed Scopus Google Scholar). and from the for with to their M.I. J. J. B. R.J. J. Biol. Chem. 2004; Full Text Full Text PDF PubMed Scopus (28) Google from of The was a from and was from and into using The human was from the human R. R. S. EMBO 2000; PubMed Scopus Google Scholar). also a specific for the of DRiP78 known as protein with or in the also to the a from M. N. J. 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PubMed Scopus Google Scholar), we a interaction between and was by but not by the that is specific for and The of on the Gβγ subunit was not by of of However, the of DRiP78 on Gβγ suggesting that heterotrimeric G protein assembly may have for or they may with each that proteins interact with G protein subunits may play a role in formation of specific signaling of DRiP78 and on Gβγ using a of with increasing of in the presence of PhLP, or and for with and and respectively. are as the of and using or both with and and bimolecular fluorescence are as of The with using using a of with increasing of in the presence of or and for with or respectively. are as the of and using or both with and and bimolecular fluorescence are as of The with using is known about the physiological that Gβγ subunits play in is known about the heterotrimeric G protein is It has in that signaling specificity may in by the formation of protein composed of of G and (for review, see Ref. 2003; PubMed Scopus Google Scholar). have recently shown that Gβγ formation that they interact the the M. N. J. Biol. Chem. Full Text Full Text PDF PubMed Scopus Google Scholar). in that the initial interaction of Gβγ with the receptor also in the The Gβγ complex heterotrimer formation with isoprenylation of the Gγ for plasma membrane targeting (12Takida S. Wedegaertner P.B. J. Biol. Chem. 2003; 278: 17284-17290Abstract Full Text Full Text PDF PubMed Scopus (78) Google Scholar). Gβγ of Gα to plasma membrane of the heterotrimer (12Takida S. Wedegaertner P.B. J. Biol. Chem. 2003; 278: 17284-17290Abstract Full Text Full Text PDF PubMed Scopus (78) Google Scholar, 14Takida S. Wedegaertner P.B. FEBS Lett. 2004; 567: 209-213Crossref PubMed Scopus (28) Google Scholar, Wedegaertner P.B. J. Biol. Chem. 2001; 276: Full Text Full Text PDF PubMed Scopus Google Scholar, J. J. Biol. Chem. 1999; Full Text Full Text PDF PubMed Scopus Google Scholar). Gα subunits to interact with nascent they the on their to the M. N. J. Biol. Chem. Full Text Full Text PDF PubMed Scopus Google Scholar). However, it has that assembly of the Gβγ complex may also an by proteins as it was suggested that in with the cytosolic complex as a chaperone for the Gβγ assembly by specifically with the Gβ subunit J. M. L. R. J. Biol. Chem. Full Text Full Text PDF PubMed Scopus Google Scholar, B.M. EMBO J. PubMed Scopus Google Scholar, R. M. P.J. Mol. Cell. Biol. PubMed Scopus Google Scholar). Furthermore, it has been shown that Gγ subunits may of Gβ from we demonstrate using a variety of techniques that DRiP78 an role by with Gγ may also regulate the assembly of the Gβγ DRiP78 is an protein known to regulate the to plasma membrane via a motif of seven transmembrane receptors such as dopamine and receptors R. M. P.J. Mol. Cell. Biol. PubMed Scopus Google Scholar, M. Cell Biol. 2001; PubMed Scopus Google Scholar, M. R. G. 2002; PubMed Scopus Google Scholar). or of DRiP78 to of dopamine receptors in the ER, and of receptor M. Cell Biol. 2001; PubMed Scopus Google for review, see Ref. Cell. PubMed Scopus Google Scholar). To date DRiP78 is known for role in the of the of from the also demonstrate that DRiP78 can interact with the β2AR, the motif in C-terminal suggesting a role for DRiP78 in It is that DRiP78 as a chaperone for the assembly as well since also in the M. N. J. Biol. Chem. Full Text Full Text PDF PubMed Scopus Google Scholar). Gγ subunits and DRiP78 in the endoplasmic the cytosolic they can interact with interaction is not by to the DRiP78 with Gβ for the interaction with Gγ and may from the chaperone as The that of DRiP78 in also formation of Gβγ and in a of is that DRiP78 the of Gγ in the of heterotrimeric DRiP78 therefore, as a chaperone for Gβγ assembly by Gγ from degradation until it with of Gγ subunits to compete for the interaction However, we Gβ subunits not interact with DRiP78 not of the to may suggest that DRiP78 is in the formation of of specific Gβγ it may suggest that are DRiP78 in the formation of DRiP78 is a of a large of proteins (for review, see Ref. D. D. EMBO 2004; PubMed Scopus Google Scholar). of the of a interaction of the as their The protein is to DRiP78, suggesting that it or proteins may but in the assembly of specific G proteins J. H. H. J. S. G. J. 2003; PubMed Scopus Google Scholar). are in the Gγ suggesting that the interaction may mediated through on would the DRiP78 or proteins to of signaling complexes. of is that and DRiP78 interact and both specificity of the formation of Gβγ or and has little on or DRiP78 can interact with several Gγ subunits by of the that several Gγ subunits can compete for interaction with it is that DRiP78 not interact with of the Gβ are is may suggest that the complex is also in formation of Gβγ expression of the Gα subunit may also we demonstrate that DRiP78 not interact with that may for Gα subunits the protein Ref. M. B. S. J. Biol. Chem. Full Text Full Text PDF PubMed Scopus Google Scholar), and H. I. L. M.G. J. Biol. Chem. Full Text Full Text PDF PubMed Scopus Google Scholar). proteins may specifically in G protein heterotrimers and may also represent proteins for that Gβγ subunits also with the cytosolic chaperone PubMed Scopus Google Scholar), suggesting that may in the formation of Gβγ as that may the selectivity of specific signaling complex formation of the chaperone by signaling by the of the PhLP·Gβ from the cytosolic complex C.M. P.J. M.D. B.M. J. Biol. Chem. Full Text Full Text PDF PubMed Scopus Google Scholar). we have recently that Gβγ subunits can interact with their effector such as to the cell and that these in as well M. N. M. J. Cell Sci. PubMed Scopus Google Scholar). The that such as or DRiP78 can also interact with effector such as J.M. M.I. 2000; Full Text Full Text PDF PubMed Scopus Google Scholar, L.A. Chen L. P.J. J. Biol. Chem. 2003; 278: Full Text Full Text PDF PubMed Scopus Google Scholar, L.A. J. Cell Sci. 2003; PubMed Scopus Google or such as such as dopamine and receptors R. M. P.J. Mol. Cell. Biol. PubMed Scopus Google Scholar, M. Cell Biol. 2001; PubMed Scopus Google Scholar, M. R. G. 2002; PubMed Scopus Google and the that these may also in the formation or trafficking of or specific of G protein and the mechanistic aspects of signaling complex formation trafficking to their would certainly of specificity and in and R. for and of The and from Wedegaertner and from Berlot and from and from was from from we for the specific for DRiP78 as well as with

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