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Volumn 1-3, Issue , 2003, Pages 651-656

Reversible Palmitoylation in G-Protein Signaling

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EID: 33947364776     PISSN: None     EISSN: None     Source Type: Book    
DOI: 10.1016/B978-012124546-7/50589-1     Document Type: Chapter
Times cited : (4)

References (65)
  • 1
    • 0035952690 scopus 로고    scopus 로고
    • Regulation of G proteins by covalent modification
    • C.A. Chen and D.R. Manning (2001) Regulation of G proteins by covalent modification. Oncogene 20 1643-1652.
    • (2001) Oncogene , vol.20 , pp. 1643-1652
    • Chen, C.A.1    Manning, D.R.2
  • 2
    • 0032497835 scopus 로고    scopus 로고
    • Signalling functions of protein palmitoylation
    • J.T. Dunphy and M.E. Linder (1998) Signalling functions of protein palmitoylation. Biochim. Biophys. Acta 1436 245-261.
    • (1998) Biochim. Biophys. Acta , vol.1436 , pp. 245-261
    • Dunphy, J.T.1    Linder, M.E.2
  • 3
    • 0032875098 scopus 로고    scopus 로고
    • Fatty acylation of proteins: new insights into membrane targeting of myristoylated and palmitoylated proteins
    • M.D. Resh (1999) Fatty acylation of proteins: new insights into membrane targeting of myristoylated and palmitoylated proteins. Biochim. Biophys. Acta 1451 1-16.
    • (1999) Biochim. Biophys. Acta , vol.1451 , pp. 1-16
    • Resh, M.D.1
  • 4
    • 0031752275 scopus 로고    scopus 로고
    • Lipid modifications and membrane targeting of Gα
    • P.B. Wedegaertner (1998) Lipid modifications and membrane targeting of Gα. Biol. Signal Recept. 7 125-135.
    • (1998) Biol. Signal Recept , vol.7 , pp. 125-135
    • Wedegaertner, P.B.1
  • 5
    • 0032695888 scopus 로고    scopus 로고
    • Dual lipid modification of the yeast Gγ subunit Ste18p determines membrane localization of Gβγ
    • J.E. Hirschman and D.D. Jenness (1999) Dual lipid modification of the yeast Gγ subunit Ste18p determines membrane localization of Gβγ. Mol. Cell. Biol. 19 7705-7711.
    • (1999) Mol. Cell. Biol , vol.19 , pp. 7705-7711
    • Hirschman, J.E.1    Jenness, D.D.2
  • 6
    • 0034098922 scopus 로고    scopus 로고
    • Dual lipid modification motifs in G(α) and G(γ) subunits are required for full activity of the pheromone response pathway in Saccharomyces cerevisiae
    • C.L. Manahan, M. Patnana, K.J. Blumer and M.E. Linder (2000) Dual lipid modification motifs in G(α) and G(γ) subunits are required for full activity of the pheromone response pathway in Saccharomyces cerevisiae. Mol. Biol. Cell 11 957-968.
    • (2000) Mol. Biol. Cell , vol.11 , pp. 957-968
    • Manahan, C.L.1    Patnana, M.2    Blumer, K.J.3    Linder, M.E.4
  • 7
    • 0033603315 scopus 로고    scopus 로고
    • Amino-terminal cysteine residues of RGS16 are required for palmitoylation and modulation of Gi- and Gq-mediated signaling
    • K.M. Druey, O. Ugur, J.M. Caron, C.K. Chen, P.S. Backlund and T.L. Jones (1999) Amino-terminal cysteine residues of RGS16 are required for palmitoylation and modulation of Gi- and Gq-mediated signaling. J. Biol. Chem. 274 18836-18842.
    • (1999) J. Biol. Chem , vol.274 , pp. 18836-18842
    • Druey, K.M.1    Ugur, O.2    Caron, J.M.3    Chen, C.K.4    Backlund, P.S.5    Jones, T.L.6
  • 8
    • 0032510737 scopus 로고    scopus 로고
    • Plasma membrane localization is required for RGS4 function in Saccharomyces cerevisiae
    • S.P. Srinivasa, L.S. Bernstein, K.J. Blumer and M.E. Linder (1998) Plasma membrane localization is required for RGS4 function in Saccharomyces cerevisiae. Proc. Natl. Acad. Sci. USA 95 5584-5589.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 5584-5589
    • Srinivasa, S.P.1    Bernstein, L.S.2    Blumer, K.J.3    Linder, M.E.4
  • 10
    • 0033621480 scopus 로고    scopus 로고
    • Palmitoylation of a conserved cysteine in the regulator of G protein signaling (RGS) domain modulates the GTPase-activating activity of RGS4 and RGS10
    • Y. Tu, S. Popov, C. Slaughter and E.M. Ross (1999) Palmitoylation of a conserved cysteine in the regulator of G protein signaling (RGS) domain modulates the GTPase-activating activity of RGS4 and RGS10. J. Biol. Chem. 274 38260-38267.
    • (1999) J. Biol. Chem , vol.274 , pp. 38260-38267
    • Tu, Y.1    Popov, S.2    Slaughter, C.3    Ross, E.M.4
  • 11
    • 0030346309 scopus 로고    scopus 로고
    • Palmitoylation: a post-translational modification that regulates signalling from G-protein coupled receptors
    • J.P. Morello and M. Bouvier (1996) Palmitoylation: a post-translational modification that regulates signalling from G-protein coupled receptors. Biochem. Cell Biol. 74 449-457.
    • (1996) Biochem. Cell Biol , vol.74 , pp. 449-457
    • Morello, J.P.1    Bouvier, M.2
  • 12
    • 0031747997 scopus 로고    scopus 로고
    • The role of receptor kinases and arrestins in G protein-coupled receptor regulation
    • J.G. Krupnick and J.L. Benovic (1998) The role of receptor kinases and arrestins in G protein-coupled receptor regulation. Annu. Rev. Pharmacol. 38 289-319.
    • (1998) Annu. Rev. Pharmacol , vol.38 , pp. 289-319
    • Krupnick, J.G.1    Benovic, J.L.2
  • 13
    • 0027340389 scopus 로고
    • Increased palmitoylation of the Gs protein alpha subunit after activation by the beta-adrenergic receptor or cholera toxin
    • M.Y. Degtyarev, A.M. Spiegel and T.L. Jones (1993) Increased palmitoylation of the Gs protein alpha subunit after activation by the beta-adrenergic receptor or cholera toxin. J. Biol. Chem. 268 23769-23772.
    • (1993) J. Biol. Chem , vol.268 , pp. 23769-23772
    • Degtyarev, M.Y.1    Spiegel, A.M.2    Jones, T.L.3
  • 15
    • 0028173706 scopus 로고
    • Activation and depalmitoylation of Gsα
    • P.B. Wedegaertner and H.R. Bourne (1994) Activation and depalmitoylation of Gsα. Cell 77 1063-1070.
    • (1994) Cell , vol.77 , pp. 1063-1070
    • Wedegaertner, P.B.1    Bourne, H.R.2
  • 16
    • 0030936823 scopus 로고    scopus 로고
    • tiReversible palmitoylation of signaling proteins
    • S.M. Mumby (1997 tiReversible palmitoylation of signaling proteins) Curr. Opin. Cell Biol. 9 148-154.
    • (1997) Curr. Opin. Cell Biol , vol.9 , pp. 148-154
    • Mumby, S.M.1
  • 17
    • 0034604292 scopus 로고    scopus 로고
    • 1 palmitoylation by activation of the 5-hydroxytryptamine-1A receptor
    • C.A. Chen and D.R. Manning (2000) Regulation of Gα1 palmitoylation by activation of the 5-hydroxytryptamine-1A receptor. J. Biol. Chem. 275 23516-23522.
    • (2000) J. Biol. Chem , vol.275 , pp. 23516-23522
    • Chen, C.A.1    Manning, D.R.2
  • 18
    • 0030998329 scopus 로고    scopus 로고
    • Regulation of G(q/11)alpha by the gonadotropin-releasing hormone receptor
    • D. Stanislaus, J.A. Janovick, S. Brothers and P.M. Conn (1997) Regulation of G(q/11)alpha by the gonadotropin-releasing hormone receptor. Mol. Endocrinol. 11 738-746.
    • (1997) Mol. Endocrinol , vol.11 , pp. 738-746
    • Stanislaus, D.1    Janovick, J.A.2    Brothers, S.3    Conn, P.M.4
  • 19
    • 0031877855 scopus 로고    scopus 로고
    • Gonadotropin-releasing hormone receptor couples to multiple G proteins in rat gonadotrophs and in GGH3 cells: Evidence from palmitoylation and overexpression of G proteins
    • D. Stanislaus, S. Ponder, T.H. Ji and P.M. Conn (1998) Gonadotropin-releasing hormone receptor couples to multiple G proteins in rat gonadotrophs and in GGH3 cells: Evidence from palmitoylation and overexpression of G proteins. Biol. Reprod. 59 579-586.
    • (1998) Biol. Reprod , vol.59 , pp. 579-586
    • Stanislaus, D.1    Ponder, S.2    Ji, T.H.3    Conn, P.M.4
  • 20
    • 0031468128 scopus 로고    scopus 로고
    • o proteins in alpha 1-adrenoceptor subtype-mediated responses in Fischer 344 rat aorta
    • H. Gurdal, T.M. Seasholtz, H.Y. Wang, R.D. Brown, M.D. Johnson and E. Friedman (1997) Role of Gαq or Gαo proteins in alpha 1-adrenoceptor subtype-mediated responses in Fischer 344 rat aorta. Mol. Pharmacol. 52 1064-1070.
    • (1997) Mol. Pharmacol , vol.52 , pp. 1064-1070
    • Gurdal, H.1    Seasholtz, T.M.2    Wang, H.Y.3    Brown, R.D.4    Johnson, M.D.5    Friedman, E.6
  • 21
    • 0032159286 scopus 로고    scopus 로고
    • Serotonin-mediated palmitoylation and depalmitoylation of G alpha proteins in rat brain cortical membranes
    • S. Bhamre, H.Y. Wang and E. Friedman (1998) Serotonin-mediated palmitoylation and depalmitoylation of G alpha proteins in rat brain cortical membranes. J. Pharmacol. Exp. Ther. 286 1482-1489.
    • (1998) J. Pharmacol. Exp. Ther , vol.286 , pp. 1482-1489
    • Bhamre, S.1    Wang, H.Y.2    Friedman, E.3
  • 22
    • 0032747133 scopus 로고    scopus 로고
    • Activation of the beta(2)-adrenergic receptor-Gα(s) complex leads to rapid depalmitoylation and inhibition of repalmitoylation of both the receptor and Gα(s)
    • T.P. Loisel, H. Ansanay, L. Adam, S. Marullo, R. Seifert, M. Lagace and M. Bouvier (1999) Activation of the beta(2)-adrenergic receptor-Gα(s) complex leads to rapid depalmitoylation and inhibition of repalmitoylation of both the receptor and Gα(s). J. Biol. Chem. 274 31014-31019.
    • (1999) J. Biol. Chem , vol.274 , pp. 31014-31019
    • Loisel, T.P.1    Ansanay, H.2    Adam, L.3    Marullo, S.4    Seifert, R.5    Lagace, M.6    Bouvier, M.7
  • 23
    • 0035929656 scopus 로고    scopus 로고
    • * gamma complex
    • P.A. Stevens, J. Pediani, J.J. Carrillo and G. Milligan (2001) Coordinated agonist regulation of receptor and G protein palmitoylation and functional rescue of palmitoylation-deficient mutants of the G protein G11 alpha following fusion to the alpha 1b-adrenoreceptor: palmitoylation of G11 alpha is not required for interaction with beta* gamma complex. J. Biol. Chem. 276 35883-35890.
    • (2001) J. Biol. Chem , vol.276 , pp. 35883-35890
    • Stevens, P.A.1    Pediani, J.2    Carrillo, J.J.3    Milligan, G.4
  • 24
    • 0026806492 scopus 로고
    • Agonist-modulated palmitoylation of beta 2-adrenergic receptor in Sf9 cells
    • B. Mouillac, M. Caron, H. Bonin, M. Dennis and M. Bouvier (1992) Agonist-modulated palmitoylation of beta 2-adrenergic receptor in Sf9 cells. J. Biol. Chem. 267 21733-21737.
    • (1992) J. Biol. Chem , vol.267 , pp. 21733-21737
    • Mouillac, B.1    Caron, M.2    Bonin, H.3    Dennis, M.4    Bouvier, M.5
  • 25
    • 0029753014 scopus 로고    scopus 로고
    • Agonist stimulation increases the turnover rate of beta 2AR-bound palmitate and promotes receptor depalmitoylation
    • T.P. Loisel, L. Adam, T.E. Hebert and M. Bouvier (1996) Agonist stimulation increases the turnover rate of beta 2AR-bound palmitate and promotes receptor depalmitoylation. Biochemistry 35 15923-15932.
    • (1996) Biochemistry , vol.35 , pp. 15923-15932
    • Loisel, T.P.1    Adam, L.2    Hebert, T.E.3    Bouvier, M.4
  • 26
    • 0029814190 scopus 로고    scopus 로고
    • Autoacylation of G protein alpha subunits
    • J.A. Duncan and A.G. Gilman (1996) Autoacylation of G protein alpha subunits. J. Biol. Chem. 271 23594-23600.
    • (1996) J. Biol. Chem , vol.271 , pp. 23594-23600
    • Duncan, J.A.1    Gilman, A.G.2
  • 27
    • 0030955679 scopus 로고    scopus 로고
    • Acyl-CoA binding proteins inhibit the nonenzymatic S-acylation of cysteinylcontaining peptide sequences by long-chain acyl-CoAs
    • R. Leventis, G. Juel, J.K. Knudsen and J.R. Silvius (1997) Acyl-CoA binding proteins inhibit the nonenzymatic S-acylation of cysteinylcontaining peptide sequences by long-chain acyl-CoAs. Biochemistry 36 5546-5553.
    • (1997) Biochemistry , vol.36 , pp. 5546-5553
    • Leventis, R.1    Juel, G.2    Knudsen, J.K.3    Silvius, J.R.4
  • 29
    • 0037174987 scopus 로고    scopus 로고
    • Identification of a Ras palmitoyltransferase in Saccharomyces cerevisiae
    • S. Lobo, W.K. Greentree, M.E. Linder and R.J. Deschenes (2002) Identification of a Ras palmitoyltransferase in Saccharomyces cerevisiae. J. Biol. Chem. 277 41268-41273.
    • (2002) J. Biol. Chem , vol.277 , pp. 41268-41273
    • Lobo, S.1    Greentree, W.K.2    Linder, M.E.3    Deschenes, R.J.4
  • 30
    • 0037078323 scopus 로고    scopus 로고
    • The yeast DHHC cysteine-rich domain protein Akr1p is a palmitoyl transferase
    • A.F. Roth, Y. Feng, L. Chen and N.G. Davis (2002) The yeast DHHC cysteine-rich domain protein Akr1p is a palmitoyl transferase. J. Cell Biol. 159 23-28.
    • (2002) J. Cell Biol , vol.159 , pp. 23-28
    • Roth, A.F.1    Feng, Y.2    Chen, L.3    Davis, N.G.4
  • 31
    • 0032546946 scopus 로고    scopus 로고
    • A cytoplasmic acyl-protein thioesterase that removes palmitate from G protein alpha subunits and p21(RAS)
    • J.A. Duncan and A.G. Gilman (1998) A cytoplasmic acyl-protein thioesterase that removes palmitate from G protein alpha subunits and p21(RAS). J. Biol. Chem. 273 15830-15837.
    • (1998) J. Biol. Chem , vol.273 , pp. 15830-15837
    • Duncan, J.A.1    Gilman, A.G.2
  • 32
    • 0029927840 scopus 로고    scopus 로고
    • G-protein palmitoyltransferase activity is enriched in plasma membranes
    • J.T. Dunphy, W.K. Greentree, C.L. Manahan and M.E. Linder (1996) G-protein palmitoyltransferase activity is enriched in plasma membranes. J. Biol. Chem. 271 7154-7159.
    • (1996) J. Biol. Chem , vol.271 , pp. 7154-7159
    • Dunphy, J.T.1    Greentree, W.K.2    Manahan, C.L.3    Linder, M.E.4
  • 33
    • 0028075456 scopus 로고
    • i subunit requires membrane localization not myristoylation
    • M.Y. Degtyarev, A.M. Spiegel and T.L. Jones (1994) Palmitoylation of a G protein αi subunit requires membrane localization not myristoylation. J. Biol. Chem. 269 30898-30903.
    • (1994) J. Biol. Chem , vol.269 , pp. 30898-30903
    • Degtyarev, M.Y.1    Spiegel, A.M.2    Jones, T.L.3
  • 35
    • 0033621812 scopus 로고    scopus 로고
    • Interaction with Gβγ is required for membrane targeting and palmitoylation of Gα(s) and Gα(q)
    • D.S. Evanko, M.M. Thiyagarajan and P.B. Wedegaertner (2000) Interaction with Gβγ is required for membrane targeting and palmitoylation of Gα(s) and Gα(q). J. Biol. Chem. 275 1327-1336.
    • (2000) J. Biol. Chem , vol.275 , pp. 1327-1336
    • Evanko, D.S.1    Thiyagarajan, M.M.2    Wedegaertner, P.B.3
  • 37
    • 0033601127 scopus 로고    scopus 로고
    • N-Myristoylation and βγ play roles beyond anchorage in the palmitoylation of the G protein alpha(o) subunit
    • Y. Wang, R.T. Windh, C.A. Chen and D.R. Manning (1999) N-Myristoylation and βγ play roles beyond anchorage in the palmitoylation of the G protein alpha(o) subunit. J. Biol. Chem. 274 37435-37442.
    • (1999) J. Biol. Chem , vol.274 , pp. 37435-37442
    • Wang, Y.1    Windh, R.T.2    Chen, C.A.3    Manning, D.R.4
  • 39
    • 0034614557 scopus 로고    scopus 로고
    • Inhibition of protein palmitoylation, raft localization, and T cell signaling by 2-bromopalmitate and polyunsaturated fatty acids
    • Y. Webb, L. Hermida-Matsumoto and M.D. Resh (2000) Inhibition of protein palmitoylation, raft localization, and T cell signaling by 2-bromopalmitate and polyunsaturated fatty acids. J. Biol. Chem. 275 261-270.
    • (2000) J. Biol. Chem , vol.275 , pp. 261-270
    • Webb, Y.1    Hermida-Matsumoto, L.2    Resh, M.D.3
  • 40
    • 0033518174 scopus 로고    scopus 로고
    • Structure-activity studies of cerulenin analogues as protein palmitoylation inhibitors
    • D.S. Lawrence, J.T. Zilfou and C.D. Smith (1999) Structure-activity studies of cerulenin analogues as protein palmitoylation inhibitors. J. Med. Chem. 42 4932-4941.
    • (1999) J. Med. Chem , vol.42 , pp. 4932-4941
    • Lawrence, D.S.1    Zilfou, J.T.2    Smith, C.D.3
  • 41
    • 0035501459 scopus 로고    scopus 로고
    • Cellular pharmacology of cerulenin analogs that inhibit protein palmitoylation
    • M.L. De Vos, D.S. Lawrence and C.D. Smith (2001) Cellular pharmacology of cerulenin analogs that inhibit protein palmitoylation. Biochem. Pharmacol. 62 985-995.
    • (2001) Biochem. Pharmacol , vol.62 , pp. 985-995
    • De Vos, M.L.1    Lawrence, D.S.2    Smith, C.D.3
  • 42
    • 0028968896 scopus 로고
    • Doubly lipid-modified protein sequence motifs exhibit long-lived anchorage to liqid bilayer membranes
    • S. Shahinian and J.R. Silvius (1995) Doubly lipid-modified protein sequence motifs exhibit long-lived anchorage to liqid bilayer membranes. Biochemistry 34 3813-3822.
    • (1995) Biochemistry , vol.34 , pp. 3813-3822
    • Shahinian, S.1    Silvius, J.R.2
  • 43
    • 0029058605 scopus 로고
    • The myristoyl-electrostatic switch: A modulator of reversible protein-membrane interactions
    • S. McLaughlin and A. Aderem (1995) The myristoyl-electrostatic switch: A modulator of reversible protein-membrane interactions. Trends Biochem. Sci. 20 272-280.
    • (1995) Trends Biochem. Sci , vol.20 , pp. 272-280
    • McLaughlin, S.1    Aderem, A.2
  • 44
    • 0028234577 scopus 로고
    • N-terminally myrisoylated ras proteins require palmitoylation or a polybasic domain for plasma membrane localization
    • K.A. Cadwallader, H. Paterson, S.G. MacDonald and J.F. Hancock (1994) N-terminally myrisoylated ras proteins require palmitoylation or a polybasic domain for plasma membrane localization. Mol. Cell. Biol. 14 4722-4730.
    • (1994) Mol. Cell. Biol , vol.14 , pp. 4722-4730
    • Cadwallader, K.A.1    Paterson, H.2    MacDonald, S.G.3    Hancock, J.F.4
  • 46
    • 0033961742 scopus 로고    scopus 로고
    • Localization of a peripheral membrane protein: Gβγ targets Gα(z)
    • C.S. Fishburn, S.K. Pollitt and H.R. Bourne (2000) Localization of a peripheral membrane protein: Gβγ targets Gα(z). Proc. Natl. Acad. Sci. USA 97 1085-1090.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 1085-1090
    • Fishburn, C.S.1    Pollitt, S.K.2    Bourne, H.R.3
  • 47
    • 0027490954 scopus 로고
    • Palmitoylation is required for signaling functions and membrane attachment of Gq alpha and Gs alpha
    • P.B. Wedegaertner, D.H. Chu, P.T. Wilson, M.J. Levis and H.R. Bourne (1993) Palmitoylation is required for signaling functions and membrane attachment of Gq alpha and Gs alpha. J. Biol. Chem. 268 25001-25008.
    • (1993) J. Biol. Chem , vol.268 , pp. 25001-25008
    • Wedegaertner, P.B.1    Chu, D.H.2    Wilson, P.T.3    Levis, M.J.4    Bourne, H.R.5
  • 49
    • 0031006587 scopus 로고    scopus 로고
    • Interaction of the G-protein G11alpha with receptors and phosphoinositidase C: The contribution of G-protein palmitoylation and membrane association
    • A. Wise, M. Parenti and G. Milligan (1997) Interaction of the G-protein G11alpha with receptors and phosphoinositidase C: The contribution of G-protein palmitoylation and membrane association. FEBS Lett. 407 257-260.
    • (1997) FEBS Lett , vol.407 , pp. 257-260
    • Wise, A.1    Parenti, M.2    Milligan, G.3
  • 50
    • 0034685541 scopus 로고    scopus 로고
    • Gα 13 requires palmitoylation for plasma membrane localization, Rho-dependent signaling, and promotion of p115-RhoGEF membrane binding
    • R. Bhattacharyya and P.B. Wedegaertner (2000) Gα 13 requires palmitoylation for plasma membrane localization, Rho-dependent signaling, and promotion of p115-RhoGEF membrane binding. J. Biol. Chem. 275 14992-14999.
    • (2000) J. Biol. Chem , vol.275 , pp. 14992-14999
    • Bhattacharyya, R.1    Wedegaertner, P.B.2
  • 51
    • 0035830890 scopus 로고    scopus 로고
    • Visualization of a functional Galpha q-green fluorescent protein fusion in living cells. Association with the plasma membrane is disrupted by mutational activation and by elimination of palmitoylation sites, but not be activation mediated by receptors or AlF4
    • T.E. Hughes, H. Zhang, D.E. Logothetis and C.H. Berlot (2001) Visualization of a functional Galpha q-green fluorescent protein fusion in living cells. Association with the plasma membrane is disrupted by mutational activation and by elimination of palmitoylation sites, but not be activation mediated by receptors or AlF4. J. Biol. Chem. 276 4227-4235.
    • (2001) J. Biol. Chem , vol.276 , pp. 4227-4235
    • Hughes, T.E.1    Zhang, H.2    Logothetis, D.E.3    Berlot, C.H.4
  • 52
    • 0027303086 scopus 로고
    • 3H]palmitic acid and mutation of cysteine-3 prevents this modification
    • M.Y. Degtyarev, A.M. Spiegel and T.L.Z. Jones (1993) The G protein αs subunit incorporates [3H]palmitic acid and mutation of cysteine-3 prevents this modification. Biochemistry 32 8057-8061.
    • (1993) Biochemistry , vol.32 , pp. 8057-8061
    • Degtyarev, M.Y.1    Spiegel, A.M.2    Jones, T.L.Z.3
  • 54
    • 0033582326 scopus 로고    scopus 로고
    • Persistent membrane association of activated and depalmitoylated G protein ]ga subunits
    • C. Huang, J.A. Duncan, A.G. Gilman and S.M. Mumby (1999) Persistent membrane association of activated and depalmitoylated G protein ]ga subunits. Proc. Natl. Acad. Sci. USA 96 412-417.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 412-417
    • Huang, C.1    Duncan, J.A.2    Gilman, A.G.3    Mumby, S.M.4
  • 55
    • 0032477949 scopus 로고    scopus 로고
    • Gα12 requires acylation for its transforming activity
    • T.L. Jones and J.S. Gutkind (1998) Gα12 requires acylation for its transforming activity. Biochemistry 37 3196-3202.
    • (1998) Biochemistry , vol.37 , pp. 3196-3202
    • Jones, T.L.1    Gutkind, J.S.2
  • 56
    • 0040142258 scopus 로고    scopus 로고
    • The membrane association domain of RGS16 contains unique amphipathic features that are conserved in RGS4 and RGS5
    • C. Chen, K.T. Seow, K. Guo, L.P. Yaw and S.C. Lin (1999) The membrane association domain of RGS16 contains unique amphipathic features that are conserved in RGS4 and RGS5. J. Biol. Chem. 274 19799-19806.
    • (1999) J. Biol. Chem , vol.274 , pp. 19799-19806
    • Chen, C.1    Seow, K.T.2    Guo, K.3    Yaw, L.P.4    Lin, S.C.5
  • 57
    • 0026474549 scopus 로고
    • s in intact cells alters its abundance, rate of degradation, and membrane avidity
    • M.J. Levis and H.R. Bourne (1992) Activation of the α subunit of Gs in intact cells alters its abundance, rate of degradation, and membrane avidity. J. Cell Biol. 119 1297-1307.
    • (1992) J. Cell Biol , vol.119 , pp. 1297-1307
    • Levis, M.J.1    Bourne, H.R.2
  • 58
    • 0028167863 scopus 로고
    • Gsα stimulates transcytosis and apical secretion in MDCK cells through cAMP and protein kinase A
    • S.H. Hansen and J.E. Casanova (1994) Gsα stimulates transcytosis and apical secretion in MDCK cells through cAMP and protein kinase A. J. Cell Biol. 126 677-687.
    • (1994) J. Cell Biol , vol.126 , pp. 677-687
    • Hansen, S.H.1    Casanova, J.E.2
  • 59
    • 0026785967 scopus 로고
    • Translocation of α subunits of stimulatory guanine nucleotide-binding proteins through stimulation of the prostacyclin receptor in mouse mastocytoma cells
    • M. Negishi, H. Hashimoto and A. Ichikawa (1992) Translocation of α subunits of stimulatory guanine nucleotide-binding proteins through stimulation of the prostacyclin receptor in mouse mastocytoma cells. J. Biol. Chem. 267 2367-2369.
    • (1992) J. Biol. Chem , vol.267 , pp. 2367-2369
    • Negishi, M.1    Hashimoto, H.2    Ichikawa, A.3
  • 60
    • 0343079334 scopus 로고
    • Stimulation of β-adrenergic receptors of S49 lymphoma cells redistributes the α subunit of the stimulatory G protein between cytosol and membranes
    • L.A. Ransnäs, P. Svoboda, J.R. Jasper and P.A. Insel (1989) Stimulation of β-adrenergic receptors of S49 lymphoma cells redistributes the α subunit of the stimulatory G protein between cytosol and membranes. Proc. Natl. Acad. Sci. USA 86 7900-7903.
    • (1989) Proc. Natl. Acad. Sci. USA , vol.86 , pp. 7900-7903
    • Ransnäs, L.A.1    Svoboda, P.2    Jasper, J.R.3    Insel, P.A.4
  • 61
    • 0036151483 scopus 로고    scopus 로고
    • Real-time visualization of a fluorescent Gαs: Dissociation of the activated G protein from plasma membrane
    • J.-Z. Yu and M.M. Rasenick (2002) Real-time visualization of a fluorescent Gαs: Dissociation of the activated G protein from plasma membrane. Mol. Pharmacol. 61 352-359.
    • (2002) Mol. Pharmacol , vol.61 , pp. 352-359
    • Yu, J.-Z.1    Rasenick, M.M.2
  • 63
    • 0030611942 scopus 로고    scopus 로고
    • Inhibition of brain Gz GAP and other RGS proteins by palmitoylation of G protein α subunits
    • Y. Tu, J. Wang and E.M. Ross (1997) Inhibition of brain Gz GAP and other RGS proteins by palmitoylation of G protein α subunits. Science 278 1132-1135.
    • (1997) Science , vol.278 , pp. 1132-1135
    • Tu, Y.1    Wang, J.2    Ross, E.M.3
  • 64
    • 0035827527 scopus 로고    scopus 로고
    • Binding of regulator of G protein signaling (RGS) proteins to phospholipid bilayers. Contribution of location and/or orientation to GTPase-activating protein activity
    • Y. Tu, J. Woodson and E.M. Ross (2001) Binding of regulator of G protein signaling (RGS) proteins to phospholipid bilayers. Contribution of location and/or orientation to GTPase-activating protein activity. J. Biol. Chem. 276 20160-20166.
    • (2001) J. Biol. Chem , vol.276 , pp. 20160-20166
    • Tu, Y.1    Woodson, J.2    Ross, E.M.3
  • 65
    • 0033783132 scopus 로고    scopus 로고
    • GTPase-activating proteins for heterotrimeric G proteins: regulators of G protein signaling (RGS) and RGS-like proteins
    • E.M. Ross and T.M. Wilkie (2000) GTPase-activating proteins for heterotrimeric G proteins: regulators of G protein signaling (RGS) and RGS-like proteins. Annu. Rev. Biochem. 69 795-827.
    • (2000) Annu. Rev. Biochem , vol.69 , pp. 795-827
    • Ross, E.M.1    Wilkie, T.M.2


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