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Volumn 20, Issue 1, 2013, Pages 39-46

Regulation of G protein-coupled receptor kinases by phospholipids

Author keywords

adrenergic receptor; Crystallography; G protein coupled receptor; Heterotrimeric G proteins; Kinase; Palmitoylation; Phosphatidylinositol 4,5 bisphosphate; Phospholipid; Phosphorylation; Prenylation; Rhodopsin

Indexed keywords

G PROTEIN COUPLED RECEPTOR KINASE 2; G PROTEIN COUPLED RECEPTOR KINASE 6; PHOSPHOLIPID; RHODOPSIN KINASE;

EID: 84872917955     PISSN: 09298673     EISSN: 1875533X     Source Type: Journal    
DOI: 10.2174/09298673130105     Document Type: Article
Times cited : (24)

References (77)
  • 1
    • 83555168220 scopus 로고    scopus 로고
    • G protein-coupled receptor kinases: More than just kinases and not only for gpcrs
    • Gurevich EV, Tesmer JJ, Mushegian A, Gurevich VV. G protein-coupled receptor kinases: more than just kinases and not only for GPCRs. Pharmacol Ther 2012, 133: 40-69
    • Pharmacol Ther , vol.2012 , Issue.133 , pp. 40-69
    • Gurevich, E.V.1    Tesmer, J.J.2    Mushegian, A.3    Gurevich, V.V.4
  • 2
    • 2942618584 scopus 로고    scopus 로고
    • Arrestins: Traffic cops of cell signaling
    • Lefkowitz RJ, Whalen E.J. α-Arrestins: traffic cops of cell signaling. Curr Opin Cell Biol 2004, 16: 162-168
    • (2004) Curr Opin Cell Biol , vol.16 , pp. 162-168
    • Lefkowitz, R.J.1    Whalen, E.J.2
  • 3
    • 84858611820 scopus 로고    scopus 로고
    • The origin and evolution of g protein-coupled receptor kinases
    • Mushegian A, Gurevich VV, Gurevich EV. The origin and evolution of G protein-coupled receptor kinases. PLoS One 2012, 7: e33806
    • PLoS One , vol.2012 , Issue.7
    • Mushegian, A.1    Gurevich, V.V.2    Gurevich, E.V.3
  • 4
    • 0026597126 scopus 로고
    • In vivo farnesylation of rat rhodopsin kinase
    • Anant JS, Fung B.K. In vivo farnesylation of rat rhodopsin kinase. Biochem Biophys Res Commun 1992, 183: 468-473
    • (1992) Biochem Biophys Res Commun , vol.183 , pp. 468-473
    • Anant, J.S.1    Fung, B.K.2
  • 5
    • 0026726050 scopus 로고
    • Isoprenylation in regulation of signal transduction by g-protein-coupled receptor kinases
    • Inglese J, Koch WJ, Caron MG, Lefkowitz R.J. Isoprenylation in regulation of signal transduction by G-protein-coupled receptor kinases. Nature 1992, 359: 147-150
    • (1992) Nature , vol.359 , pp. 147-150
    • Inglese, J.1    Koch, W.J.2    Caron, M.G.3    Lefkowitz, R.J.4
  • 6
    • 0032513146 scopus 로고    scopus 로고
    • A novel subtype of g-protein-coupled receptor kinase, grk7, in teleost cone photoreceptors
    • Hisatomi O, Matsuda S, Satoh T, Kotaka S, Imanishi Y, Tokunaga F. A novel subtype of G-protein-coupled receptor kinase, GRK7, in teleost cone photoreceptors. FEBS Lett 1998, 424: 159-164
    • (1998) FEBS Lett , vol.424 , pp. 159-164
    • Hisatomi, O.1    Matsuda, S.2    Satoh, T.3    Kotaka, S.4    Imanishi, Y.5    Tokunaga, F.6
  • 7
    • 0027481032 scopus 로고
    • The binding site for the Subunits of heterotrimeric g proteins on the α-adrenergic receptor kinase
    • Koch WJ, Inglese J, Stone WC, Lefkowitz R.J. The binding site for the subunits of heterotrimeric G proteins on the α-adrenergic receptor kinase. J Biol Chem 1993, 268: 8256-8260
    • (1993) J Biol Chem , vol.268 , pp. 8256-8260
    • Koch, W.J.1    Inglese, J.2    Stone, W.C.3    Lefkowitz, R.J.4
  • 8
    • 0037799206 scopus 로고    scopus 로고
    • Keeping g proteins at bay: A complex between g protein-coupled receptor kinase 2 and g
    • Lodowski DT, Pitcher JA, Capel WD, Lefkowitz RJ, Tesmer J.J. Keeping G proteins at bay: a complex between G protein-coupled receptor kinase 2 and G. Science 2003, 300: 1256-1262
    • (2003) Science , vol.300 , pp. 1256-1262
    • Lodowski, D.T.1    Pitcher, J.A.2    Capel, W.D.3    Lefkowitz, R.J.4    Tesmer, J.J.5
  • 10
    • 0032553549 scopus 로고    scopus 로고
    • Structure-function analysis of g protein-coupled receptor kinase-5. Role of the carboxyl terminus in kinase regulation
    • Pronin AN, Carman CV, Benovic J.L. Structure-function analysis of G protein-coupled receptor kinase-5. Role of the carboxyl terminus in kinase regulation. J Biol Chem 1998, 273: 31510-31518
    • (1998) J Biol Chem , vol.273 , pp. 31510-31518
    • Pronin, A.N.1    Carman, C.V.2    Benovic, J.L.3
  • 12
    • 0029915255 scopus 로고    scopus 로고
    • Characterization of the g protein-coupled receptor kinase grk4. Identification of four splice variants
    • Premont RT, Macrae AD, Stoffel RH, Chung N, Pitcher JA, Ambrose C, Inglese J, et al. Characterization of the G protein-coupled receptor kinase GRK4. Identification of four splice variants. J Biol Chem 1996, 271: 6403-6410
    • (1996) J Biol Chem , vol.271 , pp. 6403-6410
    • Premont, R.T.1    Macrae, A.D.2    Stoffel, R.H.3    Chung, N.4    Pitcher, J.A.5    Ambrose, C.6    Inglese, J.7
  • 13
    • 0028030060 scopus 로고
    • Palmitoylation of g protein-coupled receptor kinase, grk6. Lipid modification diversity in the grk family
    • Stoffel RH, Randall RR, Premont RT, Lefkowitz RJ, Inglese J. Palmitoylation of G protein-coupled receptor kinase, GRK6. Lipid modification diversity in the GRK family. J Biol Chem 1994, 269: 27791-27794
    • (1994) J Biol Chem , vol.269 , pp. 27791-27794
    • Stoffel, R.H.1    Randall, R.R.2    Premont, R.T.3    Lefkowitz, R.J.4    Inglese, J.5
  • 14
    • 79952796822 scopus 로고    scopus 로고
    • Activation of g protein-coupled receptor kinase 1 involves interactions between its nterminal region and its kinase domain
    • Huang CC, Orban T, Jastrzebska B, Palczewski K, Tesmer J.J. Activation of G protein-coupled receptor kinase 1 involves interactions between its Nterminal region and its kinase domain. Biochemistry 2011, 50: 1940-1949
    • (2011) Biochemistry , vol.50 , pp. 1940-1949
    • Huang, C.C.1    Orban, T.2    Jastrzebska, B.3    Palczewski, K.4    Tesmer, J.J.5
  • 15
    • 46649109793 scopus 로고    scopus 로고
    • Structures of rhodopsin kinase in different ligand states reveal key elements involved in g protein-coupled receptor kinase activation
    • Singh P, Wang B, Maeda T, Palczewski K, Tesmer J.J. Structures of rhodopsin kinase in different ligand states reveal key elements involved in G protein-coupled receptor kinase activation. J Biol Chem 2008, 283: 14053-14062
    • (2008) J Biol Chem , vol.283 , pp. 14053-14062
    • Singh, P.1    Wang, B.2    Maeda, T.3    Palczewski, K.4    Tesmer, J.J.5
  • 18
    • 77649218358 scopus 로고    scopus 로고
    • Structure of human g protein-coupled receptor kinase 2 in complex with the kinase inhibitor balanol
    • Tesmer JJ, Tesmer VM, Lodowski DT, Steinhagen H, Huber J. Structure of human G protein-coupled receptor kinase 2 in complex with the kinase inhibitor balanol. J Med Chem 2010, 53: 1867-1870
    • (2010) J Med Chem , vol.53 , pp. 1867-1870
    • Tesmer, J.J.1    Tesmer, V.M.2    Lodowski, D.T.3    Steinhagen, H.4    Huber, J.5
  • 19
  • 20
    • 79960223285 scopus 로고    scopus 로고
    • Molecular mechanism of selectivity among g protein-coupled receptor kinase 2 inhibitors
    • Thal DM, Yeow RY, Schoenau C, Huber J, Tesmer J.J. Molecular mechanism of selectivity among G protein-coupled receptor kinase 2 inhibitors. Mol Pharmacol 2011, 80: 294-303
    • (2011) Mol Pharmacol , vol.80 , pp. 294-303
    • Thal, D.M.1    Yeow, R.Y.2    Schoenau, C.3    Huber, J.4    Tesmer, J.J.5
  • 21
    • 84869435029 scopus 로고    scopus 로고
    • Paroxetine is a direct inhibitor of g protein-coupled receptor kinase 2 and increases myocardial contractility
    • In press
    • Thal DM, Homan KT, Chen J, Wu EK, Hinkle PM, Huang ZM, Chuprun JK, et al. Paroxetine is a direct inhibitor of G protein-coupled receptor kinase 2 and increases myocardial contractility. ACS Chem Bio 2012, In press
    • (2012) ACS Chem Bio
    • Thal, D.M.1    Homan, K.T.2    Chen, J.3    Wu, E.K.4    Hinkle, P.M.5    Huang, Z.M.6    Chuprun, J.K.7
  • 22
    • 77957778459 scopus 로고    scopus 로고
    • Molecular basis for activation of g protein-coupled receptor kinases
    • Boguth CA, Singh P, Huang CC, Tesmer J.J. Molecular basis for activation of G protein-coupled receptor kinases. EMBO J 2010, 29: 3249-3259
    • (2010) EMBO J , vol.29 , pp. 3249-3259
    • Boguth, C.A.1    Singh, P.2    Huang, C.C.3    Tesmer, J.J.4
  • 23
    • 33745207354 scopus 로고    scopus 로고
    • The structure of g protein-coupled receptor kinase (grk)-6 defines a second lineage of grks
    • Lodowski DT, Tesmer VM, Benovic JL, Tesmer J.J. The structure of G protein-coupled receptor kinase (GRK)-6 defines a second lineage of GRKs. J Biol Chem 2006, 281: 16785-16793
    • (2006) J Biol Chem , vol.281 , pp. 16785-16793
    • Lodowski, D.T.1    Tesmer, V.M.2    Benovic, J.L.3    Tesmer, J.J.4
  • 24
    • 33846590132 scopus 로고    scopus 로고
    • The hallmark of agc kinase functional divergence is its c-terminal tail, a cis-acting regulatory module
    • Kannan N, Haste N, Taylor SS, Neuwald A.F. The hallmark of AGC kinase functional divergence is its C-terminal tail, a cis-acting regulatory module. Proc Natl Acad Sci U S A 2007, 104: 1272-1277
    • (2007) Proc Natl Acad Sci U S A , vol.104 , pp. 1272-1277
    • Kannan, N.1    Haste, N.2    Taylor, S.S.3    Neuwald, A.F.4
  • 26
    • 0037458702 scopus 로고    scopus 로고
    • G protein-coupled receptor kinase 2/gq/11 interaction. A novel surface on a regulator of g protein signaling homology domain for binding g Subunits
    • Sterne-Marr R, Tesmer JJ, Day PW, Stracquatanio RP, Cilente JA, O'Connor KE, Pronin AN, et al. G protein-coupled receptor Kinase 2/Gq/11 interaction. A novel surface on a regulator of G protein signaling homology domain for binding G subunits. J Biol Chem 2003, 278: 6050-6058
    • (2003) J Biol Chem , vol.278 , pp. 6050-6058
    • Sterne-Marr, R.1    Tesmer, J.J.2    Day, P.W.3    Stracquatanio, R.P.4    Cilente, J.A.5    O'Connor, K.E.6    Pronin, A.N.7
  • 27
    • 0020020855 scopus 로고
    • Preparation of retinal rod outer segments
    • Papermaster D.S. Preparation of retinal rod outer segments. Methods Enzymol 1982, 81: 48-52
    • (1982) Methods Enzymol , vol.81 , pp. 48-52
    • Papermaster, D.S.1
  • 28
    • 0029039613 scopus 로고
    • Pleckstrin homology domain-mediated membrane association and activation of the α-adrenergic receptor kinase requires coordinate interaction with g Subunits and lipid
    • Pitcher JA, Touhara K, Payne ES, Lefkowitz R.J. Pleckstrin homology domain-mediated membrane association and activation of the α-adrenergic receptor kinase requires coordinate interaction with G subunits and lipid. J Biol Chem 1995, 270: 11707-11710
    • (1995) J Biol Chem , vol.270 , pp. 11707-11710
    • Pitcher, J.A.1    Touhara, K.2    Payne, E.S.3    Lefkowitz, R.J.4
  • 29
    • 0028982276 scopus 로고
    • The α-adrenergic receptor kinase (grk2) is regulated by phospholipids
    • Onorato JJ, Gillis ME, Liu Y, Benovic JL, Ruoho A.E. The α-adrenergic receptor kinase (GRK2) is regulated by phospholipids. J Biol Chem 1995, 270: 21346-21353
    • (1995) J Biol Chem , vol.270 , pp. 21346-21353
    • Onorato, J.J.1    Gillis, M.E.2    Liu, Y.3    Benovic, J.L.4    Ruoho, A.E.5
  • 30
    • 0024278380 scopus 로고
    • Rhodopsin kinase: Substrate specificity and factors that influence activity
    • Palczewski K, McDowell JH, Hargrave P.A. Rhodopsin kinase: substrate specificity and factors that influence activity. Biochemistry 1988, 27: 2306-2313
    • (1988) Biochemistry , vol.27 , pp. 2306-2313
    • Palczewski, K.1    McDowell, J.H.2    Hargrave, P.A.3
  • 31
    • 0027238553 scopus 로고
    • Phosphorylation of solubilised dark-adapted rhodopsin. Insights into the activation of rhodopsin kinase
    • Dean KR, Akhtar M. Phosphorylation of solubilised dark-adapted rhodopsin. Insights into the activation of rhodopsin kinase. Eur J Biochem 1993, 213: 881-890
    • (1993) Eur J Biochem , vol.213 , pp. 881-890
    • Dean, K.R.1    Akhtar, M.2
  • 32
    • 0031055598 scopus 로고    scopus 로고
    • Structure and function in rhodopsin: Peptide sequences in the cytoplasmic loops of rhodopsin are intimately involved in interaction with rhodopsin kinase
    • Thurmond RL, Creuzenet C, Reeves PJ, Khorana H.G. Structure and function in rhodopsin: peptide sequences in the cytoplasmic loops of rhodopsin are intimately involved in interaction with rhodopsin kinase. Proc Natl Acad Sci U S A 1997, 94: 1715-1720
    • (1997) Proc Natl Acad Sci U S A , vol.94 , pp. 1715-1720
    • Thurmond, R.L.1    Creuzenet, C.2    Reeves, P.J.3    Khorana, H.G.4
  • 33
    • 0028085776 scopus 로고
    • Cellular expression of the carboxyl terminus of a g protein-coupled receptor kinase attenuates gα-mediated signaling
    • Koch WJ, Hawes BE, Inglese J, Luttrell LM, Lefkowitz R.J. Cellular expression of the carboxyl terminus of a G protein-coupled receptor kinase attenuates Gα-mediated signaling. J Biol Chem 1994, 269: 6193-6197
    • (1994) J Biol Chem , vol.269 , pp. 6193-6197
    • Koch, W.J.1    Hawes, B.E.2    Inglese, J.3    Luttrell, L.M.4    Lefkowitz, R.J.5
  • 34
    • 0026542596 scopus 로고
    • Isoprenylation of a protein kinase. Requirement of farnesylation/α- carboxyl methylation for full enzymatic activity of rhodopsin kinase
    • Inglese J, Glickman JF, Lorenz W, Caron MG, Lefkowitz R.J. Isoprenylation of a protein kinase. Requirement of farnesylation/α-carboxyl methylation for full enzymatic activity of rhodopsin kinase. J Biol Chem 1992, 267: 1422-1425
    • (1992) J Biol Chem , vol.267 , pp. 1422-1425
    • Inglese, J.1    Glickman, J.F.2    Lorenz, W.3    Caron, M.G.4    Lefkowitz, R.J.5
  • 35
    • 33846010489 scopus 로고    scopus 로고
    • Structural basis for calcium-induced inhibition of rhodopsin kinase by recoverin
    • Ames JB, Levay K, Wingard JN, Lusin JD, Slepak VZ. Structural basis for calcium-induced inhibition of rhodopsin kinase by recoverin. J Biol Chem 2006, 281: 37237-37245
    • (2006) J Biol Chem , vol.281 , pp. 37237-37245
    • Ames, J.B.1    Levay, K.2    Wingard, J.N.3    Lusin, J.D.4    Slepak, V.Z.5
  • 36
    • 33745815637 scopus 로고    scopus 로고
    • Recoverin binds exclusively to an amphipathic peptide at the n terminus of rhodopsin kinase, inhibiting rhodopsin phosphorylation without affecting catalytic activity of the kinase
    • Higgins MK, Oprian DD, Schertler G.F. Recoverin binds exclusively to an amphipathic peptide at the N terminus of rhodopsin kinase, inhibiting rhodopsin phosphorylation without affecting catalytic activity of the kinase. J Biol Chem 2006, 281: 19426-19432
    • (2006) J Biol Chem , vol.281 , pp. 19426-19432
    • Higgins, M.K.1    Oprian, D.D.2    Schertler, G.F.3
  • 37
    • 0032578351 scopus 로고    scopus 로고
    • Localization of the sites for ca2+-binding proteins on g protein-coupled receptor kinases
    • Levay K, Satpaev DK, Pronin AN, Benovic JL, Slepak VZ. Localization of the sites for Ca2+-binding proteins on G protein-coupled receptor kinases. Biochemistry 1998, 37: 13650-13659
    • (1998) Biochemistry , vol.37 , pp. 13650-13659
    • Levay, K.1    Satpaev, D.K.2    Pronin, A.N.3    Benovic, J.L.4    Slepak, V.Z.5
  • 39
    • 33745876251 scopus 로고    scopus 로고
    • Grk1 and grk7: Unique cellular distribution and widely different activities of opsin phosphorylation in the zebrafish rods and cones
    • Wada Y, Sugiyama J, Okano T, Fukada Y. GRK1 and GRK7: unique cellular distribution and widely different activities of opsin phosphorylation in the zebrafish rods and cones. J Neurochem 2006, 98: 824-837
    • (2006) J Neurochem , vol.98 , pp. 824-837
    • Wada, Y.1    Sugiyama, J.2    Okano, T.3    Fukada, Y.4
  • 40
    • 21544468844 scopus 로고    scopus 로고
    • Highly effective phosphorylation by g protein-coupled receptor kinase 7 of light-activated visual pigment in cones
    • Tachibanaki S, Arinobu D, Shimauchi-Matsukawa Y, Tsushima S, Kawamura S. Highly effective phosphorylation by G protein-coupled receptor kinase 7 of light-activated visual pigment in cones. Proc Natl Acad Sci U S A 2005, 102: 9329-9334
    • (2005) Proc Natl Acad Sci U S A , vol.102 , pp. 9329-9334
    • Tachibanaki, S.1    Arinobu, D.2    Shimauchi-Matsukawa, Y.3    Tsushima, S.4    Kawamura, S.5
  • 41
    • 0027490599 scopus 로고
    • Phosphorylation and desensitization of human m2 muscarinic cholinergic receptors by two isoforms of the α-adrenergic receptor kinase
    • Richardson RM, Kim C, Benovic JL, Hosey M.M. Phosphorylation and desensitization of human m2 muscarinic cholinergic receptors by two isoforms of the α-adrenergic receptor kinase. J Biol Chem 1993, 268: 13650-13656
    • (1993) J Biol Chem , vol.268 , pp. 13650-13656
    • Richardson, R.M.1    Kim, C.2    Benovic, J.L.3    Hosey, M.U.4
  • 42
    • 0027563367 scopus 로고
    • Expression and characterization of two α-adrenergic receptor kinase isoforms using the baculovirus expression system
    • Kim CM, Dion SB, Onorato JJ, Benovic J.L. Expression and characterization of two α-adrenergic receptor kinase isoforms using the baculovirus expression system. Receptor 1993, 3: 39-55
    • (1993) Receptor , vol.3 , pp. 39-55
    • Kim, C.M.1    Dion, S.B.2    Onorato, J.J.3    Benovic, J.L.4
  • 43
    • 0028937671 scopus 로고
    • Agonist-dependent phosphorylation of human muscarinic receptors in spodoptera frugiperda insect cell membranes by g protein-coupled receptor kinases
    • Debburman SK, Kunapuli P, Benovic JL, Hosey M.M. Agonist-dependent phosphorylation of human muscarinic receptors in Spodoptera frugiperda insect cell membranes by G protein-coupled receptor kinases. Mol Pharmacol 1995, 47: 224-233
    • (1995) Mol Pharmacol , vol.47 , pp. 224-233
    • Debburman, S.K.1    Kunapuli, P.2    Benovic, J.L.3    Hosey, M.U.4
  • 44
    • 0026803164 scopus 로고
    • Role of Subunits of g proteins in targeting the α-adrenergic receptor kinase to membrane-bound receptors
    • Pitcher JA, Inglese J, Higgins JB, Arriza JL, Casey PJ, Kim C, Benovic JL, et al. Role of subunits of G proteins in targeting the α-adrenergic receptor kinase to membrane-bound receptors. Science 1992, 257: 1264-1267
    • (1992) Science , vol.257 , pp. 1264-1267
    • Pitcher, J.A.1    Inglese, J.2    Higgins, J.B.3    Arriza, J.L.4    Casey, P.J.5    Kim, C.6    Benovic, J.L.7
  • 45
    • 0027418322 scopus 로고
    • Activation by g protein Subunits of α-adrenergic and muscarinic receptor kinase
    • Kameyama K, Haga K, Haga T, Kontani K, Katada T, Fukada Y. Activation by G protein subunits of α-adrenergic and muscarinic receptor kinase. J Biol Chem 1993, 268: 7753-7758
    • (1993) J Biol Chem , vol.268 , pp. 7753-7758
    • Kameyama, K.1    Haga, K.2    Haga, T.3    Kontani, K.4    Katada, T.5    Fukada, Y.6
  • 46
    • 0025315797 scopus 로고
    • Dual regulation by g proteins of agonist-dependent phosphorylation of muscarinic acetylcholine receptors
    • Haga K, Haga T. Dual regulation by G proteins of agonist-dependent phosphorylation of muscarinic acetylcholine receptors. FEBS Lett 1990, 268: 43-47
    • (1990) FEBS Lett , vol.268 , pp. 43-47
    • Haga, K.1    Haga, T.2
  • 47
    • 0028331783 scopus 로고
    • An approach to the study of gprotein-coupled receptor kinases: An in vitro-purified membrane assay reveals differential receptor specificity and regulation by g Subunits
    • Pei G, Tiberi M, Caron MG, Lefkowitz R.J. An approach to the study of Gprotein-coupled receptor kinases: an in vitro-purified membrane assay reveals differential receptor specificity and regulation by G subunits. Proc Natl Acad Sci U S A 1994, 91: 3633-3636
    • (1994) Proc Natl Acad Sci U S A , vol.91 , pp. 3633-3636
    • Pei, G.1    Tiberi, M.2    Caron, M.G.3    Lefkowitz, R.J.4
  • 48
    • 0027185782 scopus 로고
    • Mechanism of α-adrenergic receptor kinase activation by g proteins
    • Kim CM, Dion SB, Benovic J.L. Mechanism of α-adrenergic receptor kinase activation by G proteins. J Biol Chem 1993, 268: 15412-15418
    • (1993) J Biol Chem , vol.268 , pp. 15412-15418
    • Kim, C.M.1    Dion, S.B.2    Benovic, J.L.3
  • 50
    • 0029788099 scopus 로고    scopus 로고
    • G protein-coupled receptor kinase grk2 is a phospholipid-dependent enzyme that can be conditionally activated by g protein Subunits
    • DebBurman SK, Ptasienski J, Benovic JL, Hosey M.M. G protein-coupled receptor kinase GRK2 is a phospholipid-dependent enzyme that can be conditionally activated by G protein subunits. J Biol Chem 1996, 271: 22552-22562
    • (1996) J Biol Chem , vol.271 , pp. 22552-22562
    • DebBurman, S.K.1    Ptasienski, J.2    Benovic, J.L.3    Hosey, M.U.4
  • 52
    • 77952840083 scopus 로고    scopus 로고
    • The complex g protein-coupled receptor kinase 2 (grk2) interactome unveils new physiopathological targets
    • Penela P, Murga C, Ribas C, Lafarga V, Mayor F, Jr. The complex G protein-coupled receptor kinase 2 (GRK2) interactome unveils new physiopathological targets. Br J Pharmacol 2010, 160: 821-832
    • (2010) Br J Pharmacol , vol.160 , pp. 821-832
    • Penela, P.1    Murga, C.2    Ribas, C.3    Lafarga, V.4    Mayor Jr., F.5
  • 53
    • 0029785214 scopus 로고    scopus 로고
    • Phosphatidylinositol 4,5-bisphosphate (pip2)-enhanced g protein-coupled receptor kinase (grk) activity. Location, structure, and regulation of the pip2 binding site distinguishes the grk subfamilies
    • Pitcher JA, Fredericks ZL, Stone WC, Premont RT, Stoffel RH, Koch WJ, Lefkowitz R.J. Phosphatidylinositol 4,5-bisphosphate (PIP2)-enhanced G protein-coupled receptor kinase (GRK) activity. Location, structure, and regulation of the PIP2 binding site distinguishes the GRK subfamilies. J Biol Chem 1996, 271: 24907-24913
    • (1996) J Biol Chem , vol.271 , pp. 24907-24913
    • Pitcher, J.A.1    Fredericks, Z.L.2    Stone, W.C.3    Premont, R.T.4    Stoffel, R.H.5    Koch, W.J.6    Lefkowitz, R.J.7
  • 54
    • 0028300574 scopus 로고
    • Identification, purification, and characterization of grk5, a member of the family of g protein-coupled receptor kinases
    • Premont RT, Koch WJ, Inglese J, Lefkowitz R.J. Identification, purification, and characterization of GRK5, a member of the family of G protein-coupled receptor kinases. J Biol Chem 1994, 269: 6832-6841
    • (1994) J Biol Chem , vol.269 , pp. 6832-6841
    • Premont, R.T.1    Koch, W.J.2    Inglese, J.3    Lefkowitz, R.J.4
  • 55
    • 37249040944 scopus 로고    scopus 로고
    • Phosphorylation of the 2-adrenergic receptor in plasma membranes by intrinsic grk5
    • Tran TM, Jorgensen R, Clark R.B. Phosphorylation of the 2-adrenergic receptor in plasma membranes by intrinsic GRK5. Biochemistry 2007, 46: 14438-14449
    • (2007) Biochemistry , vol.46 , pp. 14438-14449
    • Tran, T.M.1    Jorgensen, R.2    Clark, R.B.3
  • 56
    • 0028290815 scopus 로고
    • Phospholipid-stimulated autophosphorylation activates the g protein-coupled receptor kinase grk5
    • Kunapuli P, Gurevich VV, Benovic J.L. Phospholipid-stimulated autophosphorylation activates the G protein-coupled receptor kinase GRK5. J Biol Chem 1994, 269: 10209-10212
    • (1994) J Biol Chem , vol.269 , pp. 10209-10212
    • Kunapuli, P.1    Gurevich, V.V.2    Benovic, J.L.3
  • 57
    • 0033199408 scopus 로고    scopus 로고
    • Alternative splicing produces transcripts encoding four variants of mouse g-protein-coupled receptor kinase 6
    • Moepps B, Vatter P, Frodl R, Waechter F, Dixkens C, Hameister H, Gierschik P. Alternative splicing produces transcripts encoding four variants of mouse G-protein-coupled receptor kinase 6. Genomics 1999, 60: 199-209
    • (1999) Genomics , vol.60 , pp. 199-209
    • Moepps, B.1    Vatter, P.2    Frodl, R.3    Waechter, F.4    Dixkens, C.5    Hameister, H.6    Gierschik, P.7
  • 58
    • 28344450854 scopus 로고    scopus 로고
    • The variable cterminal extension of g-protein-coupled receptor kinase 6 constitutes an accessorial autoregulatory domain
    • Vatter P, Stoesser C, Samel I, Gierschik P, Moepps B. The variable Cterminal extension of G-protein-coupled receptor kinase 6 constitutes an accessorial autoregulatory domain. FEBS J 2005, 272: 6039-6051
    • (2005) FEBS J , vol.272 , pp. 6039-6051
    • Vatter, P.1    Stoesser, C.2    Samel, I.3    Gierschik, P.4    Moepps, B.5
  • 59
    • 0030777365 scopus 로고    scopus 로고
    • Altered activity of palmitoylation-deficient and isoprenylated forms of the g protein-coupled receptor kinase grk6
    • Loudon RP, Benovic J.L. Altered activity of palmitoylation-deficient and isoprenylated forms of the G protein-coupled receptor kinase GRK6. J Biol Chem 1997, 272: 27422-27427
    • (1997) J Biol Chem , vol.272 , pp. 27422-27427
    • Loudon, R.P.1    Benovic, J.L.2
  • 60
    • 34547781132 scopus 로고    scopus 로고
    • Plasma membrane and nuclear localization of g protein coupled receptor kinase 6a
    • Jiang X, Benovic JL, Wedegaertner P.B. Plasma membrane and nuclear localization of G protein coupled receptor kinase 6.A. Mol Biol Cell 2007, 18: 2960-2969
    • (2007) Mol Biol Cell , vol.18 , pp. 2960-2969
    • Jiang, X.1    Benovic, J.L.2    Wedegaertner, P.B.3
  • 61
    • 0032541974 scopus 로고    scopus 로고
    • Palmitoylation increases the kinase activity of the g protein-coupled receptor kinase, grk6
    • Stoffel RH, Inglese J, Macrae AD, Lefkowitz RJ, Premont R.T. Palmitoylation increases the kinase activity of the G protein-coupled receptor kinase, GRK6. Biochemistry 1998, 37: 16053-16059
    • (1998) Biochemistry , vol.37 , pp. 16053-16059
    • Stoffel, R.H.1    Inglese, J.2    Macrae, A.D.3    Lefkowitz, R.J.4    Premont, R.T.5
  • 62
    • 0030986964 scopus 로고    scopus 로고
    • G protein-coupled receptor kinase grk4. Molecular analysis of the four isoforms and ultrastructural localization in spermatozoa and germinal cells
    • Sallese M, Mariggio S, Collodel G, Moretti E, Piomboni P, Baccetti B, De Blasi A. G protein-coupled receptor kinase GRK4. Molecular analysis of the four isoforms and ultrastructural localization in spermatozoa and germinal cells. J Biol Chem 1997, 272: 10188-10195
    • (1997) J Biol Chem , vol.272 , pp. 10188-10195
    • Sallese, M.1    Mariggio, S.2    Collodel, G.3    Moretti, E.4    Piomboni, P.5    Baccetti, B.6    De Blasi, A.7
  • 63
    • 0001616166 scopus 로고    scopus 로고
    • Inhibition of g protein-coupled receptor kinase subtypes by ca2+/calmodulin
    • Chuang TT, Paolucci L, De Blasi A. Inhibition of G protein-coupled receptor kinase subtypes by Ca2+/calmodulin. J Biol Chem 1996, 271: 28691-28696
    • (1996) J Biol Chem , vol.271 , pp. 28691-28696
    • Chuang, T.T.1    Paolucci, L.2    De Blasi, A.3
  • 64
    • 0030800966 scopus 로고    scopus 로고
    • Regulation of g proteincoupled receptor kinases by calmodulin and localization of the calmodulin binding domain
    • Pronin AN, Satpaev DK, Slepak VZ, Benovic J.L. Regulation of G proteincoupled receptor kinases by calmodulin and localization of the calmodulin binding domain. J Biol Chem 1997, 272: 18273-18280
    • (1997) J Biol Chem , vol.272 , pp. 18273-18280
    • Pronin, A.N.1    Satpaev, D.K.2    Slepak, V.Z.3    Benovic, J.L.4
  • 65
    • 38549092474 scopus 로고    scopus 로고
    • Membrane recognition by phospholipid-binding domains
    • Lemmon M.A. Membrane recognition by phospholipid-binding domains. Nat Rev Mol Cell Biol 2008, 9: 99-111
    • (2008) Nat Rev Mol Cell Biol , vol.9 , pp. 99-111
    • Lemmon, M.A.1
  • 66
    • 0028891875 scopus 로고
    • Mutational analysis of the pleckstrin homology domain of the α-adrenergic receptor kinase. Differential effects on g And phosphatidylinositol 4,5-bisphosphate binding
    • Touhara K, Koch WJ, Hawes BE, Lefkowitz R.J. Mutational analysis of the pleckstrin homology domain of the α-adrenergic receptor kinase. Differential effects on G and phosphatidylinositol 4,5-bisphosphate binding. J Biol Chem 1995, 270: 17000-17005
    • (1995) J Biol Chem , vol.270 , pp. 17000-17005
    • Touhara, K.1    Koch, W.J.2    Hawes, B.E.3    Lefkowitz, R.J.4
  • 67
    • 80053089071 scopus 로고    scopus 로고
    • Heterotrimeric g protein 12 subunits change orientation upon complex formation with g protein-coupled receptor kinase 2 (grk2) on a model membrane
    • Boughton AP, Yang P, Tesmer VM, Ding B, Tesmer JJ, Chen Z. Heterotrimeric G protein 12 subunits change orientation upon complex formation with G protein-coupled receptor kinase 2 (GRK2) on a model membrane. Proc Natl Acad Sci U S A 2011, 108: E667-673
    • (2011) Proc Natl Acad Sci U S A , vol.108
    • Boughton, A.P.1    Yang, P.2    Tesmer, V.M.3    Ding, B.4    Tesmer, J.J.5    Chen, Z.6
  • 68
    • 79952784761 scopus 로고    scopus 로고
    • Recognition in the face of diversity: Interactions of heterotrimeric g proteins and g protein-coupled receptor (gpcr) kinases with activated gpcrs
    • Huang CC, Tesmer J.J. Recognition in the face of diversity: interactions of heterotrimeric G proteins and G protein-coupled receptor (GPCR) kinases with activated GPCRs. J Biol Chem 2011, 286: 7715-7721
    • (2011) J Biol Chem , vol.286 , pp. 7715-7721
    • Huang, C.C.1    Tesmer, J.J.2
  • 69
    • 68049097974 scopus 로고    scopus 로고
    • Role of the amino terminus of g proteincoupled receptor kinase 2 in receptor phosphorylation
    • Pao CS, Barker BL, Benovic J.L. Role of the amino terminus of G proteincoupled receptor kinase 2 in receptor phosphorylation. Biochemistry 2009, 48: 7325-7333
    • (2009) Biochemistry , vol.48 , pp. 7325-7333
    • Pao, C.S.1    Barker, B.L.2    Benovic, J.L.3
  • 70
    • 0036215864 scopus 로고    scopus 로고
    • Crystal structure of a transition state mimic of the catalytic subunit of camp-dependent protein kinase
    • Madhusudan, Akamine P, Xuong NH, Taylor S.S. Crystal structure of a transition state mimic of the catalytic subunit of cAMP-dependent protein kinase. Nat Struct Biol 2002, 9: 273-277
    • (2002) Nat Struct Biol , vol.9 , pp. 273-277
    • Madhusudan Akamine, P.1    Xuong, N.H.2    Taylor, S.S.3
  • 73
    • 66149178593 scopus 로고    scopus 로고
    • A surface of the kinase domain critical for the allosteric activation of g protein-coupled receptor kinases
    • Huang CC, Yoshino-Koh K, Tesmer J.J. A surface of the kinase domain critical for the allosteric activation of G protein-coupled receptor kinases. J Biol Chem 2009, 284: 17206-17215
    • (2009) J Biol Chem , vol.284 , pp. 17206-17215
    • Huang, C.C.1    Yoshino-Koh, K.2    Tesmer, J.J.3
  • 74
    • 84863148751 scopus 로고    scopus 로고
    • Membrane-localized α-subunits alter the pip2 regulation of high-voltage activated ca2+ channels
    • Suh BC, Kim DI, Falkenburger BH, Hille B. Membrane-localized α-subunits alter the PIP2 regulation of high-voltage activated Ca2+ channels. Proc Natl Acad Sci U S A 2012, 109: 3161-3166
    • Proc Natl Acad Sci U S A , vol.2012 , Issue.109 , pp. 3161-3166
    • Suh, B.C.1    Kim, D.I.2    Falkenburger, B.H.3    Hille, B.4
  • 77
    • 0027968068 scopus 로고
    • Clustal w: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
    • Thompson JD, Higgins DG, Gibson T.J. CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucleic Acids Res 1994, 22: 4673-4680
    • (1994) Nucleic Acids Res , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3


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