메뉴 건너뛰기




Volumn 32, Issue C, 1997, Pages 99-120

5 Regulation of cAMP signaling by phosphorylation

Author keywords

[No Author keywords available]

Indexed keywords

ADENYLATE CYCLASE; BETA ADRENERGIC RECEPTOR; CYCLIC AMP; GUANINE NUCLEOTIDE BINDING PROTEIN; ISOENZYME; PROTEIN KINASE C;

EID: 0031602881     PISSN: 10407952     EISSN: None     Source Type: Book Series    
DOI: 10.1016/S1040-7952(98)80007-4     Document Type: Article
Times cited : (18)

References (133)
  • 1
    • 0019293605 scopus 로고
    • The calcium and magnesium binding sites on cardiac troponin and their role in the regulation of myofibrillar adenosine triphosphatase
    • Holroyde, MJ, Robertson, SP, Johnson, JD, et al. The calcium and magnesium binding sites on cardiac troponin and their role in the regulation of myofibrillar adenosine triphosphatase. J Biol Chem 255 (1980), 11668-11693.
    • (1980) J Biol Chem , vol.255 , pp. 11668-11693
    • Holroyde, M.J.1    Robertson, S.P.2    Johnson, J.D.3
  • 2
    • 0025012601 scopus 로고
    • Functional reconstitution of the cardiac sarcoplasmic reticulum Ca-ATPase with phospholamban in phospholipid vesicles
    • Kim, HW, Steenaart, NAE, Ferguson, DG, Kranias, EG, Functional reconstitution of the cardiac sarcoplasmic reticulum Ca-ATPase with phospholamban in phospholipid vesicles. J Biol Chem 265 (1990), 1702-1709.
    • (1990) J Biol Chem , vol.265 , pp. 1702-1709
    • Kim, H.W.1    Steenaart, N.A.E.2    Ferguson, D.G.3    Kranias, E.G.4
  • 3
    • 0021885588 scopus 로고
    • The phosphorylation of proteins: a major mechanism for biological regulation
    • Krebs, EG, The phosphorylation of proteins: a major mechanism for biological regulation. Biochem Soc Trans 13 (1985), 813-820.
    • (1985) Biochem Soc Trans , vol.13 , pp. 813-820
    • Krebs, E.G.1
  • 4
    • 0002491966 scopus 로고
    • Cyclic nucleotide phosphodiesterases: structure, regulation
    • Wiley Press Chichester
    • Beavo, JA, Houslay, MD, Cyclic nucleotide phosphodiesterases: structure, regulation. 1990, Wiley Press, Chichester.
    • (1990)
    • Beavo, J.A.1    Houslay, M.D.2
  • 5
    • 0025810398 scopus 로고
    • Cyclic nucleotide-dependent protein kinases
    • Scott, JD, Cyclic nucleotide-dependent protein kinases. Pharmacol Ther 50 (1991), 123-145.
    • (1991) Pharmacol Ther , vol.50 , pp. 123-145
    • Scott, J.D.1
  • 6
    • 0023666159 scopus 로고
    • Regulation of transmembrane signaling by receptor phosphorylation
    • Sibley, DR, Benovic, JL, Caron, MG, Lefkowitz, RJ, Regulation of transmembrane signaling by receptor phosphorylation. Cell 48 (1987), 913-922.
    • (1987) Cell , vol.48 , pp. 913-922
    • Sibley, D.R.1    Benovic, J.L.2    Caron, M.G.3    Lefkowitz, R.J.4
  • 7
    • 0029057061 scopus 로고
    • Phosphorylation and desensitization of the human beta 1-adrenergic receptor. Involvement of G protein-coupled receptor kinases and cAMP-dependent protein kinase
    • Freedman, NJ, Liggett, SB, Drachman, DE, et al. Phosphorylation and desensitization of the human beta 1-adrenergic receptor. Involvement of G protein-coupled receptor kinases and cAMP-dependent protein kinase. J Biol Chem 270 (1995), 17953-17961.
    • (1995) J Biol Chem , vol.270 , pp. 17953-17961
    • Freedman, N.J.1    Liggett, S.B.2    Drachman, D.E.3
  • 8
    • 0025350916 scopus 로고
    • Role of phosphorylation in desensitization of the beta adrenoceptor
    • Lefkowitz, RJ, Hausdorff, WP, Caron, MG, Role of phosphorylation in desensitization of the beta adrenoceptor. Trends Pharmacol Sci 11 (1990), 190-194.
    • (1990) Trends Pharmacol Sci , vol.11 , pp. 190-194
    • Lefkowitz, R.J.1    Hausdorff, W.P.2    Caron, M.G.3
  • 9
    • 0026040191 scopus 로고
    • Consensus sequences as substrate specificity determinants for protein kinases and protein phosphatases
    • Kennelly, PJ, Krebs, EG, Consensus sequences as substrate specificity determinants for protein kinases and protein phosphatases. J Biol Chem 266 (1991), 1555-15558.
    • (1991) J Biol Chem , vol.266 , pp. 1555-15558
    • Kennelly, P.J.1    Krebs, E.G.2
  • 10
    • 0023815680 scopus 로고
    • Site-directed mutagenesis of the cytoplasmic domains of the human beta 2-adrenergic receptor. Localization of regions involved in G protein-receptor c
    • O'Dowd, BF, Hnatowich, M, Regan, JW, et al. Site-directed mutagenesis of the cytoplasmic domains of the human beta 2-adrenergic receptor. Localization of regions involved in G protein-receptor c. J Biol Chem 263 (1988), 15985-15992.
    • (1988) J Biol Chem , vol.263 , pp. 15985-15992
    • O'Dowd, B.F.1    Hnatowich, M.2    Regan, J.W.3
  • 11
    • 0024397065 scopus 로고
    • Phosphorylation sites on two domains of the β2-adrenergic receptor are involved in distinct pathways of receptor desensitization
    • Hausdorff, WP, Bouvier, M, O'Dowd, BF, et al. Phosphorylation sites on two domains of the β2-adrenergic receptor are involved in distinct pathways of receptor desensitization. J Biol Chem 264 (1989), 12657-12665.
    • (1989) J Biol Chem , vol.264 , pp. 12657-12665
    • Hausdorff, W.P.1    Bouvier, M.2    O'Dowd, B.F.3
  • 12
    • 0024440843 scopus 로고
    • Altered patterns of agonist-stimulated cAMP accumulation in cells expressing mutant beta 2-adrenergic receptors lacking phosphorylation sites
    • Liggett, SB, Bouvier, M, Hausdorff, WP, et al. Altered patterns of agonist-stimulated cAMP accumulation in cells expressing mutant beta 2-adrenergic receptors lacking phosphorylation sites. Mol Pharmacol 36 (1989), 641-646.
    • (1989) Mol Pharmacol , vol.36 , pp. 641-646
    • Liggett, S.B.1    Bouvier, M.2    Hausdorff, W.P.3
  • 13
    • 0024367312 scopus 로고
    • Identification of a specific site required for rapid heterologous desensitization of the β-adrenergic receptor by cAMP-dependent protein kinase
    • Clark, RB, Friedman, J, Dixon, RAF, Strader, CD, Identification of a specific site required for rapid heterologous desensitization of the β-adrenergic receptor by cAMP-dependent protein kinase. Mol Pharmacol 36 (1989), 343-348.
    • (1989) Mol Pharmacol , vol.36 , pp. 343-348
    • Clark, R.B.1    Friedman, J.2    Dixon, R.A.F.3    Strader, C.D.4
  • 14
    • 0025250147 scopus 로고
    • Multiple pathways of rapid beta 2-adrenergic receptor desensitization: delineation with specific inhibitors
    • Lohse, MJ, Benovic, JL, Caron, MG, Lefkowitz, RJ, Multiple pathways of rapid beta 2-adrenergic receptor desensitization: delineation with specific inhibitors. J Biol Chem 265 (1990), 3202-3211.
    • (1990) J Biol Chem , vol.265 , pp. 3202-3211
    • Lohse, M.J.1    Benovic, J.L.2    Caron, M.G.3    Lefkowitz, R.J.4
  • 15
    • 0344812247 scopus 로고
    • β-adrenergic receptor kinase: identification of a novel protein kinase that phosphorylates the agonist occupied form of the receptor
    • Benovic, JL, Strasser, RH, Caron, MG, Lefkowitz, RJ, β-adrenergic receptor kinase: identification of a novel protein kinase that phosphorylates the agonist occupied form of the receptor. Proc Natl Acad Sci USA 83 (1986), 2797-2801.
    • (1986) Proc Natl Acad Sci USA , vol.83 , pp. 2797-2801
    • Benovic, J.L.1    Strasser, R.H.2    Caron, M.G.3    Lefkowitz, R.J.4
  • 16
    • 0027368165 scopus 로고
    • Structure and Mechanism of the G protein-coupled receptor kinases
    • Inglese, J, Freedman, NJ, Koch, WJ, Lefkowitz, RJ, Structure and Mechanism of the G protein-coupled receptor kinases. J Biol Chem 268:32 (1993), 23735-23738.
    • (1993) J Biol Chem , vol.268 , Issue.32 , pp. 23735-23738
    • Inglese, J.1    Freedman, N.J.2    Koch, W.J.3    Lefkowitz, R.J.4
  • 17
    • 0023610955 scopus 로고
    • Agonist-dependent phosphorylation of the alpha 2-adrenergic receptor by the beta-adrenergic receptor kinase
    • Benovic, JL, Regan, JW, Matsui, H, et al. Agonist-dependent phosphorylation of the alpha 2-adrenergic receptor by the beta-adrenergic receptor kinase. J Biol Chem 262 (1987), 17251-17253.
    • (1987) J Biol Chem , vol.262 , pp. 17251-17253
    • Benovic, J.L.1    Regan, J.W.2    Matsui, H.3
  • 18
    • 0030066616 scopus 로고    scopus 로고
    • Phosphorylation of human m1 muscarinic acetylcholine receptors by G protein-coupled receptor kinase 2 and protein kinase C
    • Haga, K, Kameyama, K, Haga, T, et al. Phosphorylation of human m1 muscarinic acetylcholine receptors by G protein-coupled receptor kinase 2 and protein kinase C. J Biol Chem 271 (1996), 2776-2782.
    • (1996) J Biol Chem , vol.271 , pp. 2776-2782
    • Haga, K.1    Kameyama, K.2    Haga, T.3
  • 19
    • 0027399999 scopus 로고
    • Phosphorylation of muscarinic receptors: regulation by G proteins
    • Haga, T, Haga, K, Kameyama, K, Nakata, H, Phosphorylation of muscarinic receptors: regulation by G proteins. Life Sci 52 (1993), 421-428.
    • (1993) Life Sci , vol.52 , pp. 421-428
    • Haga, T.1    Haga, K.2    Kameyama, K.3    Nakata, H.4
  • 20
    • 0026803164 scopus 로고
    • Role of beta gamma subunits of G proteins in targeting the beta-adrenergic receptor kinase to membrane-bound receptors
    • Pitcher, JA, Inglese, J, Higgins, JB, et al. Role of beta gamma subunits of G proteins in targeting the beta-adrenergic receptor kinase to membrane-bound receptors. Science 257 (1992), 1264-1267.
    • (1992) Science , vol.257 , pp. 1264-1267
    • Pitcher, J.A.1    Inglese, J.2    Higgins, J.B.3
  • 21
    • 0028085776 scopus 로고
    • Cellular expression of the carboxyl terminus of a G protein coupled receptor kinase attenuates Gßγ-mediated signaling
    • Koch, WJ, Hawes, BE, Inglese, J, et al. Cellular expression of the carboxyl terminus of a G protein coupled receptor kinase attenuates Gßγ-mediated signaling. J Biol Chem 269 (1994), 6193-6197.
    • (1994) J Biol Chem , vol.269 , pp. 6193-6197
    • Koch, W.J.1    Hawes, B.E.2    Inglese, J.3
  • 22
    • 0028860268 scopus 로고
    • Heterotrimeric G proteins: organizers of transmembrane signals
    • Neer, EJ, Heterotrimeric G proteins: organizers of transmembrane signals. Cell 80 (1995), 249-257.
    • (1995) Cell , vol.80 , pp. 249-257
    • Neer, E.J.1
  • 23
    • 0027288910 scopus 로고
    • A putative modular domain present in diverse signaling proteins
    • Mayer, BJ, Ren, R, Clark, KL, Baltimore, D, A putative modular domain present in diverse signaling proteins. Cell 73 (1993), 629-630.
    • (1993) Cell , vol.73 , pp. 629-630
    • Mayer, B.J.1    Ren, R.2    Clark, K.L.3    Baltimore, D.4
  • 24
    • 0027183541 scopus 로고
    • The PH domain: a common piece in the structural patchwork of signaling proteins
    • Musacchio, A, Gibson, T, Rice, P, et al. The PH domain: a common piece in the structural patchwork of signaling proteins. TIBS 18 (1993), 343-349.
    • (1993) TIBS , vol.18 , pp. 343-349
    • Musacchio, A.1    Gibson, T.2    Rice, P.3
  • 25
    • 0027528961 scopus 로고
    • Overexpression of β-arrestin and β-adrenergic receptor kinase augment desensitization of β2-adrenergic receptors
    • Piping, S, Andexinger, S, Daniel, K, et al. Overexpression of β-arrestin and β-adrenergic receptor kinase augment desensitization of β2-adrenergic receptors. J Biol Chem 268 (1993), 3201-3208.
    • (1993) J Biol Chem , vol.268 , pp. 3201-3208
    • Piping, S.1    Andexinger, S.2    Daniel, K.3
  • 26
    • 0028181709 scopus 로고
    • A β-adrenergic receptor kinase dominant negative mutant attenuates desensitization of the β2-adrenergic receptor
    • Kong, G, Penn, R, Benovic, JL, A β-adrenergic receptor kinase dominant negative mutant attenuates desensitization of the β2-adrenergic receptor. J Biol Chem 269 (1994), 13084-13087.
    • (1994) J Biol Chem , vol.269 , pp. 13084-13087
    • Kong, G.1    Penn, R.2    Benovic, J.L.3
  • 27
    • 0028330142 scopus 로고
    • Rapid desensitization of neonatal rat liver beta-adrenergic receptors: a role for beta-adrenergic receptor kinase
    • Garcia-Higuera, P, Mayor, FJ, Rapid desensitization of neonatal rat liver beta-adrenergic receptors: a role for beta-adrenergic receptor kinase. J Clin Invest 93 (1994), 937-943.
    • (1994) J Clin Invest , vol.93 , pp. 937-943
    • Garcia-Higuera, P.1    Mayor, F.J.2
  • 28
    • 0028985998 scopus 로고
    • Reduced β-adrenergic receptor activation decreases G protein expression and β-adrenergic receptor kinase activity in porcine heart
    • Ping, P, Gelzer-Bell, R, Roth, DA, et al. Reduced β-adrenergic receptor activation decreases G protein expression and β-adrenergic receptor kinase activity in porcine heart. J Clin Invest 95 (1995), 1271-1280.
    • (1995) J Clin Invest , vol.95 , pp. 1271-1280
    • Ping, P.1    Gelzer-Bell, R.2    Roth, D.A.3
  • 29
    • 0029061324 scopus 로고
    • Cardiac function in mice overexpressing the β-adrenergic receptor kinase or a ßARK inhibitor
    • Koch, WJ, Rockman, HA, Samama, P, et al. Cardiac function in mice overexpressing the β-adrenergic receptor kinase or a ßARK inhibitor. Science 268 (1995), 1350-1353.
    • (1995) Science , vol.268 , pp. 1350-1353
    • Koch, W.J.1    Rockman, H.A.2    Samama, P.3
  • 30
    • 0003476769 scopus 로고
    • The synapse: function, plasticity, and neutrophism
    • Oxford University Press Oxford
    • Kuno, M, The synapse: function, plasticity, and neutrophism. 1995, Oxford University Press, Oxford.
    • (1995)
    • Kuno, M.1
  • 31
    • 0025223081 scopus 로고
    • Turning of the signal: desensitization of β-adrenergic receptor function
    • Hausdorff, WP, Caron, MG, Lefkowitz, RJ, Turning of the signal: desensitization of β-adrenergic receptor function. FASEB J 4 (1990), 2881-2889.
    • (1990) FASEB J , vol.4 , pp. 2881-2889
    • Hausdorff, W.P.1    Caron, M.G.2    Lefkowitz, R.J.3
  • 32
    • 0023515309 scopus 로고
    • Functional desensitization of the isolated beta-adrenergic re ceptor by the beta-adrenergic kinase: potential role of and analog of the retinal protein arrestin (48-kDa protein)
    • Benovic, JL, Kuhn, H, Weyand, I, et al. Functional desensitization of the isolated beta-adrenergic re ceptor by the beta-adrenergic kinase: potential role of and analog of the retinal protein arrestin (48-kDa protein). Proc Natl Acad Sci U S A 84 (1987), 8879-8882.
    • (1987) Proc Natl Acad Sci U S A , vol.84 , pp. 8879-8882
    • Benovic, J.L.1    Kuhn, H.2    Weyand, I.3
  • 33
    • 0025352299 scopus 로고
    • beta-Arrestin: a protein that regulates beta-adrenergic receptor function
    • Lohse, MJ, Benovic, JL, Codina, J, et al. beta-Arrestin: a protein that regulates beta-adrenergic receptor function. Science 248 (1990), 1547-1550.
    • (1990) Science , vol.248 , pp. 1547-1550
    • Lohse, M.J.1    Benovic, J.L.2    Codina, J.3
  • 34
    • 0030593035 scopus 로고    scopus 로고
    • Role of β-arrestin in mediating agonist-promoted G protein-coupled receptor internalization
    • Ferguson, SSG, Downey, WE III, Colapietro, A, et al. Role of β-arrestin in mediating agonist-promoted G protein-coupled receptor internalization. Science 271 (1996), 363-366.
    • (1996) Science , vol.271 , pp. 363-366
    • Ferguson, S.S.G.1    Downey, W.E.2    Colapietro, A.3
  • 35
    • 0028024714 scopus 로고
    • Phosphoinositide metabolism in air way smooth muscle
    • Chilvers, ER, Lynch, BJ, Challiss, RAJ, Phosphoinositide metabolism in air way smooth muscle. Pharmacol Ther 62 (1994), 221-245.
    • (1994) Pharmacol Ther , vol.62 , pp. 221-245
    • Chilvers, E.R.1    Lynch, B.J.2    Challiss, R.A.J.3
  • 36
    • 0026523050 scopus 로고
    • Assessment of signal transduction mechanisms regulating airway smooth muscle contractility
    • Schramm, CM, Grunstein, MM, Assessment of signal transduction mechanisms regulating airway smooth muscle contractility. Am J Physiol 262 (1992), L119–L139.
    • (1992) Am J Physiol , vol.262 , pp. L119-L139
    • Schramm, C.M.1    Grunstein, M.M.2
  • 37
    • 0018880134 scopus 로고
    • Tumor promoter uncouples β-adrenergic receptor from adenylyl cyclase in mouse epidermis
    • Garte, S, Belman, S, Tumor promoter uncouples β-adrenergic receptor from adenylyl cyclase in mouse epidermis. Nature 284 (1980), 171-173.
    • (1980) Nature , vol.284 , pp. 171-173
    • Garte, S.1    Belman, S.2
  • 38
    • 0021232137 scopus 로고
    • Phorbol ester induces desensitization of adenylyl cyclase and phosphorylation of the β-adrenergic receptor in turkey erythrocyte
    • Kelleher, DJ, Pessin, JE, Ruoho, AE, Johnson, GL, Phorbol ester induces desensitization of adenylyl cyclase and phosphorylation of the β-adrenergic receptor in turkey erythrocyte. Proc Natl Acad Sci U S A 81 (1984), 4316-4320.
    • (1984) Proc Natl Acad Sci U S A , vol.81 , pp. 4316-4320
    • Kelleher, D.J.1    Pessin, J.E.2    Ruoho, A.E.3    Johnson, G.L.4
  • 39
    • 0025146356 scopus 로고
    • Identification of a specific domain in the beta-adrenergic receptor required for phorbol ester-induced inhibition of catecholamine-stimulated adenylyl cyclase
    • Johnson, JA, Clark, RB, Friedman, J, et al. Identification of a specific domain in the beta-adrenergic receptor required for phorbol ester-induced inhibition of catecholamine-stimulated adenylyl cyclase. Mol Pharmacol 38 (1990), 289-293.
    • (1990) Mol Pharmacol , vol.38 , pp. 289-293
    • Johnson, J.A.1    Clark, R.B.2    Friedman, J.3
  • 40
    • 0022919229 scopus 로고
    • Phorbol ester-induced augmentation and inhibition of epinephrine-stimulated adenylate cyclase in S49 lymphoma cells
    • Johnson, JA, Goka, TJ, Clark, RB, Phorbol ester-induced augmentation and inhibition of epinephrine-stimulated adenylate cyclase in S49 lymphoma cells. J Cyclic Nucl Protein Phosphor Res 11 (1986), 199-215.
    • (1986) J Cyclic Nucl Protein Phosphor Res , vol.11 , pp. 199-215
    • Johnson, J.A.1    Goka, T.J.2    Clark, R.B.3
  • 41
    • 0024243880 scopus 로고
    • Homologous and heterologous beta-adrenergic desensitization in hepatocytes: additivity and effect of pertussis toxin
    • Hernandez-Sotomayor, SM, Macias-Silva, M, Plebanski, M, Garcia-Sainz, JA, Homologous and heterologous beta-adrenergic desensitization in hepatocytes: additivity and effect of pertussis toxin. Biochim Biophys Acta 972 (1988), 311-319.
    • (1988) Biochim Biophys Acta , vol.972 , pp. 311-319
    • Hernandez-Sotomayor, S.M.1    Macias-Silva, M.2    Plebanski, M.3    Garcia-Sainz, J.A.4
  • 42
    • 0026776880 scopus 로고
    • Desensitization of the isolated beta 2-adrenergic receptor by beta-adrenergic receptor kinase cAMP-dependent protein kinase, and protein kinase C occurs via distinct molecular mechanisms
    • Pitcher, J, Lohse, MJ, Codina, J, et al. Desensitization of the isolated beta 2-adrenergic receptor by beta-adrenergic receptor kinase cAMP-dependent protein kinase, and protein kinase C occurs via distinct molecular mechanisms. Biochemistry 31 (1992), 3193-3197.
    • (1992) Biochemistry , vol.31 , pp. 3193-3197
    • Pitcher, J.1    Lohse, M.J.2    Codina, J.3
  • 43
    • 0028064817 scopus 로고
    • cAMP-dependent protein kinase and protein kinase C consensus site mutations of the beta-adrenergic receptor: effect on desensitization and stimulation of adenylylcyclase
    • Yuan, N, Friedman, J, Whaley, BS, Clark, RB, cAMP-dependent protein kinase and protein kinase C consensus site mutations of the beta-adrenergic receptor: effect on desensitization and stimulation of adenylylcyclase. J Biol Chem 269 (1994), 23032-23038.
    • (1994) J Biol Chem , vol.269 , pp. 23032-23038
    • Yuan, N.1    Friedman, J.2    Whaley, B.S.3    Clark, R.B.4
  • 44
    • 0027101956 scopus 로고
    • Cross-talk between tyrosine kinase and G protein linked receptors
    • Hadcock, JR, Port, JD, Gelman, MS, Malbon, CC, Cross-talk between tyrosine kinase and G protein linked receptors. J Biol Chem 267 (1992), 26017-26022.
    • (1992) J Biol Chem , vol.267 , pp. 26017-26022
    • Hadcock, J.R.1    Port, J.D.2    Gelman, M.S.3    Malbon, C.C.4
  • 45
    • 0028845339 scopus 로고
    • Phosphorylation of tyrosyl residues 350/354 of the beta-adrenergic receptor is obligatory for counterregulatory effects of insulin
    • Karoor, V, Baltensperger, K, Paul, H, et al. Phosphorylation of tyrosyl residues 350/354 of the beta-adrenergic receptor is obligatory for counterregulatory effects of insulin. J Biol Chem 270 (1995), 25305-25308.
    • (1995) J Biol Chem , vol.270 , pp. 25305-25308
    • Karoor, V.1    Baltensperger, K.2    Paul, H.3
  • 46
    • 0029670792 scopus 로고    scopus 로고
    • The beta-adrenergic receptor is a substrate for the insulin receptor tyrosine kinase
    • Baltensperger, K, Karoor, V, Paul, H, et al. The beta-adrenergic receptor is a substrate for the insulin receptor tyrosine kinase. J Biol Chem 271 (1996), 1061-1064.
    • (1996) J Biol Chem , vol.271 , pp. 1061-1064
    • Baltensperger, K.1    Karoor, V.2    Paul, H.3
  • 47
    • 0019951471 scopus 로고
    • Different mechanisms of desensitization of adenylate cyclase by isoproterenol and prostaglandin E1 in human fibroblasts: role of regulatory components in densensitization
    • Kassis, S, Fishman, PH, Different mechanisms of desensitization of adenylate cyclase by isoproterenol and prostaglandin E1 in human fibroblasts: role of regulatory components in densensitization. J Biol Chem 257 (1982), 5312-5318.
    • (1982) J Biol Chem , vol.257 , pp. 5312-5318
    • Kassis, S.1    Fishman, P.H.2
  • 48
    • 0024456629 scopus 로고
    • Heterologous densensitization of the liver adenylyl cyclase: analysis of the role of G-proteins
    • Premont, RT, Iyengar, R, Heterologous densensitization of the liver adenylyl cyclase: analysis of the role of G-proteins. Endocrinology 125 (1989), 1151-1160.
    • (1989) Endocrinology , vol.125 , pp. 1151-1160
    • Premont, R.T.1    Iyengar, R.2
  • 49
    • 0020523519 scopus 로고
    • Human chorionic gonadotropin-induced heterologous desensitization of adenyl cyclase from highly luteinized rat ovaries: attenuation of regulatory N component activity
    • Kirchick, HJ, Iyengar, R, Birnbaumer, L, Human chorionic gonadotropin-induced heterologous desensitization of adenyl cyclase from highly luteinized rat ovaries: attenuation of regulatory N component activity. Endocrinology 113 (1983), 1638-1646.
    • (1983) Endocrinology , vol.113 , pp. 1638-1646
    • Kirchick, H.J.1    Iyengar, R.2    Birnbaumer, L.3
  • 51
    • 0022527455 scopus 로고
    • Gonadotropin-mediated densensitization in a murine Leydig tumor cell line does not alter the regulatory and catalytic components of adenylyl cyclase
    • Rebois, RV, Fishman, PH, Gonadotropin-mediated densensitization in a murine Leydig tumor cell line does not alter the regulatory and catalytic components of adenylyl cyclase. Endocrinology 118 (1986), 2340-2348.
    • (1986) Endocrinology , vol.118 , pp. 2340-2348
    • Rebois, R.V.1    Fishman, P.H.2
  • 52
    • 0025133362 scopus 로고
    • Overexpression of c-src enhances beta-adrenergic-induced cAMP accumulation
    • Bushman, WA, Wilson, LK, Luttrell, DK, et al. Overexpression of c-src enhances beta-adrenergic-induced cAMP accumulation. Proc Natl Acad Sci U S A 87 (1990), 7462-7466.
    • (1990) Proc Natl Acad Sci U S A , vol.87 , pp. 7462-7466
    • Bushman, W.A.1    Wilson, L.K.2    Luttrell, D.K.3
  • 53
    • 0026668305 scopus 로고
    • Tyrosine phosphorylation of G protein α subunit by pp60c-src
    • Haudorff, WP, Pitcher, JA, Luttrell, DK, et al. Tyrosine phosphorylation of G protein α subunit by pp60c-src. Proc Natl Acad Sci U S A 89 (1992), 5720-5724.
    • (1992) Proc Natl Acad Sci U S A , vol.89 , pp. 5720-5724
    • Haudorff, W.P.1    Pitcher, J.A.2    Luttrell, D.K.3
  • 55
    • 0026008747 scopus 로고
    • Genetic and structural analysis of G protein alpha subunit regulatory domains
    • Johnson, GL, Dhanasekaran, N, Gupta, SK, et al. Genetic and structural analysis of G protein alpha subunit regulatory domains. J Cell Biochem 47 (1991), 136-146.
    • (1991) J Cell Biochem , vol.47 , pp. 136-146
    • Johnson, G.L.1    Dhanasekaran, N.2    Gupta, S.K.3
  • 56
    • 0023576039 scopus 로고
    • Identification of receptor contact site involved in receptor-G protein coupling
    • Sullivan, KA, Miller, RT, Masters, SB, et al. Identification of receptor contact site involved in receptor-G protein coupling. Nature 330 (1987), 758-760.
    • (1987) Nature , vol.330 , pp. 758-760
    • Sullivan, K.A.1    Miller, R.T.2    Masters, S.B.3
  • 57
    • 0029664393 scopus 로고    scopus 로고
    • Activation of G by the epidermal growth factor receptor involves phosphorylation
    • Poppleton, H, Sun, H, Fulgham, D, et al. Activation of G by the epidermal growth factor receptor involves phosphorylation. J Biol Chem 271 (1996), 6947-6951.
    • (1996) J Biol Chem , vol.271 , pp. 6947-6951
    • Poppleton, H.1    Sun, H.2    Fulgham, D.3
  • 58
    • 0022357080 scopus 로고
    • Protein kinase C phosphorylates the inhibitory guanine-nucleotide-binding regulatory component and apparently, suppresses its function in hormonal inhibition of adenylate cyclase
    • Katada, T, Gilman, AG, Watanabe, Y, et al. Protein kinase C phosphorylates the inhibitory guanine-nucleotide-binding regulatory component and apparently, suppresses its function in hormonal inhibition of adenylate cyclase. Eur J Biochem 151 (1985), 431-437.
    • (1985) Eur J Biochem , vol.151 , pp. 431-437
    • Katada, T.1    Gilman, A.G.2    Watanabe, Y.3
  • 59
    • 0024506753 scopus 로고
    • i, which is inactivated upon challenge of hepatocytes with glucagon
    • i, which is inactivated upon challenge of hepatocytes with glucagon. Biochem J 259 (1989), 191-197.
    • (1989) Biochem J , vol.259 , pp. 191-197
    • Murphy, G.J.1    Gawler, D.J.2    Milligan, G.3
  • 60
    • 0024402896 scopus 로고
    • Protein kinase C stimulates adenylyl cyclase activity in prolactin-secreting rat adenoma (GH4C 1) pituicytes by inactivating the inhibitory GTP-binding protein Gi
    • Gordeladze, JO, Bjoro, T, Torjesen, PA, et al. Protein kinase C stimulates adenylyl cyclase activity in prolactin-secreting rat adenoma (GH4C 1) pituicytes by inactivating the inhibitory GTP-binding protein Gi. Eur J Biochem 183 (1989), 397-406.
    • (1989) Eur J Biochem , vol.183 , pp. 397-406
    • Gordeladze, J.O.1    Bjoro, T.2    Torjesen, P.A.3
  • 61
    • 0024417310 scopus 로고
    • Facilitative actions of the protein kinase C effector system on hormonally stimulated adenosine 3′ 5′-monophosphate production by swine luteal cells
    • Wheeler, MB, Veldhuis, JD, Facilitative actions of the protein kinase C effector system on hormonally stimulated adenosine 3′ 5′-monophosphate production by swine luteal cells. Endocrinology 125 (1989), 2414-2420.
    • (1989) Endocrinology , vol.125 , pp. 2414-2420
    • Wheeler, M.B.1    Veldhuis, J.D.2
  • 62
    • 0023717456 scopus 로고
    • Modulation of adenylate cyclase in human keratinocytes by protein kinase C
    • Choi, EJ, Toscano, WAJ, Modulation of adenylate cyclase in human keratinocytes by protein kinase C. J Biol Chem 263 (1988), 17167-17172.
    • (1988) J Biol Chem , vol.263 , pp. 17167-17172
    • Choi, E.J.1    Toscano, W.A.J.2
  • 63
    • 0024471885 scopus 로고
    • Regulation of GH3 pituitary tumor cell adenylyl cyclase activity by activators of protein kinase C
    • Quilliam, LA, Dobson, PRM, Brown, BL, Regulation of GH3 pituitary tumor cell adenylyl cyclase activity by activators of protein kinase C. Biochem J 262 (1989), 829-834.
    • (1989) Biochem J , vol.262 , pp. 829-834
    • Quilliam, L.A.1    Dobson, P.R.M.2    Brown, B.L.3
  • 64
    • 0025967118 scopus 로고
    • Selective effects of activation of protein kinase C isozymes on cyclic AMP accumulation
    • Gusovsky, F, Gutkind, JS, Selective effects of activation of protein kinase C isozymes on cyclic AMP accumulation. Mol Pharmacol 39 (1991), 124-129.
    • (1991) Mol Pharmacol , vol.39 , pp. 124-129
    • Gusovsky, F.1    Gutkind, J.S.2
  • 65
    • 0026451081 scopus 로고
    • Intracellular by hydrolysis of phospholipids and activation of protein kinase C
    • Nishizuka, Y, Intracellular by hydrolysis of phospholipids and activation of protein kinase C. Science 258 (1992), 607-614.
    • (1992) Science , vol.258 , pp. 607-614
    • Nishizuka, Y.1
  • 67
    • 0028174325 scopus 로고
    • i alpha 2 attenuates inhibitory adenylyl cyclase in neuroblastoma/glioma hybrid (NG-108-15) cells
    • i alpha 2 attenuates inhibitory adenylyl cyclase in neuroblastoma/glioma hybrid (NG-108-15) cells. J Biol Chem 269 (1994), 14307-14313.
    • (1994) J Biol Chem , vol.269 , pp. 14307-14313
    • Strassheim, D.1    Malbon, C.C.2
  • 69
    • 0021278290 scopus 로고
    • The phorbol ester, TPA inhibits glucagonstimulated adenylyl cyclase activity
    • Heyworth, CM, Whetton, AP, Kinsella, AR, Houslay, MD, The phorbol ester, TPA inhibits glucagonstimulated adenylyl cyclase activity. FEBS Lett 170 (1984), 38-42.
    • (1984) FEBS Lett , vol.170 , pp. 38-42
    • Heyworth, C.M.1    Whetton, A.P.2    Kinsella, A.R.3    Houslay, M.D.4
  • 70
    • 0022363890 scopus 로고
    • Phorbol ester causes desensitization of gonadotropin-responsive adenylate cyclase in a murine Leydig tumor cell line
    • Rebois, RV, Patel, J, Phorbol ester causes desensitization of gonadotropin-responsive adenylate cyclase in a murine Leydig tumor cell line. J Biol Chem 260 (1985), 8026-8031.
    • (1985) J Biol Chem , vol.260 , pp. 8026-8031
    • Rebois, R.V.1    Patel, J.2
  • 71
    • 0021993026 scopus 로고
    • Activation of protein kinase C potentiates isoprenaline-induced cyclic AMP accumulation in rat pinealocytes
    • Sugden, D, Vanacek, J, Klein, DC, et al. Activation of protein kinase C potentiates isoprenaline-induced cyclic AMP accumulation in rat pinealocytes. Nature 314 (1985), 359-361.
    • (1985) Nature , vol.314 , pp. 359-361
    • Sugden, D.1    Vanacek, J.2    Klein, D.C.3
  • 72
    • 0021987216 scopus 로고
    • Enhancement of adenylate cyclase activity in S49 lymphoma cells by phorbol esters
    • Bell, JD, Buxton, ILO, Brunton, LL, Enhancement of adenylate cyclase activity in S49 lymphoma cells by phorbol esters. J Biol Chem 260 (1985), 2625-2628.
    • (1985) J Biol Chem , vol.260 , pp. 2625-2628
    • Bell, J.D.1    Buxton, I.L.O.2    Brunton, L.L.3
  • 73
    • 0026692158 scopus 로고
    • Regulation of the cAMP signal transduction pathway by protein kinase C in rat submandibular cells
    • Fleming, N, Mellow, L, Bhullar, D, Regulation of the cAMP signal transduction pathway by protein kinase C in rat submandibular cells. Eur J Physiol 421 (1992), 82-89.
    • (1992) Eur J Physiol , vol.421 , pp. 82-89
    • Fleming, N.1    Mellow, L.2    Bhullar, D.3
  • 74
    • 0022429416 scopus 로고
    • An activator, of protein kinase C (phobol-12-myristrate-13-acetate) augments 2-chloroadenosine elicited accumulation of cAMP in guinea cerebral cortical particulate preparations
    • Hollingsworth, EB, Sears, EB, Daly, JW, An activator, of protein kinase C (phobol-12-myristrate-13-acetate) augments 2-chloroadenosine elicited accumulation of cAMP in guinea cerebral cortical particulate preparations. FEBS Lett 184 (1895), 339-342.
    • (1895) FEBS Lett , vol.184 , pp. 339-342
    • Hollingsworth, E.B.1    Sears, E.B.2    Daly, J.W.3
  • 75
    • 0022844854 scopus 로고
    • Activation of adipocyte adenylate cyclase by protein kinase C
    • Naghshineh, S, Noguchi, M, Huang, KP, Londos, C, Activation of adipocyte adenylate cyclase by protein kinase C. J Biol Chem 261 (1986), 14534-14538.
    • (1986) J Biol Chem , vol.261 , pp. 14534-14538
    • Naghshineh, S.1    Noguchi, M.2    Huang, K.P.3    Londos, C.4
  • 76
    • 0023647144 scopus 로고
    • Cross-talk between cellular signaling pathways suggested by phorbol-ester-induced adenylate cyclase phosphorylation
    • Yoshimasa, T, Sibley, DR, Bouvier, M, et al. Cross-talk between cellular signaling pathways suggested by phorbol-ester-induced adenylate cyclase phosphorylation. Nature 327 (1987), 67-70.
    • (1987) Nature , vol.327 , pp. 67-70
    • Yoshimasa, T.1    Sibley, D.R.2    Bouvier, M.3
  • 77
    • 0023666012 scopus 로고
    • Cross-talk between PKC and cyclic AMP pathways
    • Levitzki, A, Cross-talk between PKC and cyclic AMP pathways. Nature 330 (1987), 319-320.
    • (1987) Nature , vol.330 , pp. 319-320
    • Levitzki, A.1
  • 78
    • 0025860174 scopus 로고
    • Chemical and functional analysis of components of adenylyl cyclase from human platelets treated with phorbol esters
    • Simmoteit, R, Schulzki, HD, Palm, D, et al. Chemical and functional analysis of components of adenylyl cyclase from human platelets treated with phorbol esters. FEBS Lett 285 (1991), 99-103.
    • (1991) FEBS Lett , vol.285 , pp. 99-103
    • Simmoteit, R.1    Schulzki, H.D.2    Palm, D.3
  • 79
    • 0027535742 scopus 로고
    • Activation of the ζ isoenzyme of protein kinase C by phosphatidylinositol 3,4,5-triphosphate
    • Nakanishi, H, Brewer, KA, Exton, JH, Activation of the ζ isoenzyme of protein kinase C by phosphatidylinositol 3,4,5-triphosphate. J Biol Chem 268 (1993), 13-16.
    • (1993) J Biol Chem , vol.268 , pp. 13-16
    • Nakanishi, H.1    Brewer, K.A.2    Exton, J.H.3
  • 80
    • 0026552516 scopus 로고
    • Tissue and cellular distribution of the extended family of protein kinase C isoenzymes
    • Westel, WC, Khan, WA, Merchenthaler, I, et al. Tissue and cellular distribution of the extended family of protein kinase C isoenzymes. J Cell Biol 117 (1992), 121-133.
    • (1992) J Cell Biol , vol.117 , pp. 121-133
    • Westel, W.C.1    Khan, W.A.2    Merchenthaler, I.3
  • 81
    • 0028158867 scopus 로고
    • Protein kinase C isoform expression and regulation in the developing rat heart
    • Rybin, VO, Steinberg, SF, Protein kinase C isoform expression and regulation in the developing rat heart. Circ Res 74 (1994), 299-309.
    • (1994) Circ Res , vol.74 , pp. 299-309
    • Rybin, V.O.1    Steinberg, S.F.2
  • 82
    • 0028036338 scopus 로고
    • Cloning of an intracellular receptor for protein kinase C: a homologue of the beta subunit of G proteins
    • Ron, D, Chen, CH, Caldwell, J, et al. Cloning of an intracellular receptor for protein kinase C: a homologue of the beta subunit of G proteins. Proc Natl Acad Sci U S A 91 (1994), 839-843.
    • (1994) Proc Natl Acad Sci U S A , vol.91 , pp. 839-843
    • Ron, D.1    Chen, C.H.2    Caldwell, J.3
  • 83
    • 0026094755 scopus 로고
    • Human vitamin D receptor is selectively phosphorylated by protein kinase C on serine 51, a residue crucial to its trans-activation function
    • Hsieh, JC, Jurutka, PW, Galligan, MA, et al. Human vitamin D receptor is selectively phosphorylated by protein kinase C on serine 51, a residue crucial to its trans-activation function. Proc Natl Acad Sci U S A 88 (1991), 9315-9319.
    • (1991) Proc Natl Acad Sci U S A , vol.88 , pp. 9315-9319
    • Hsieh, J.C.1    Jurutka, P.W.2    Galligan, M.A.3
  • 84
    • 0023652675 scopus 로고
    • Phosphorylation of the EGF receptor from A431 epidermoid carcinoma cells by three distinct types of protein kinase C
    • Ido, M, Sekiguchi, K, Kikkawa, U, Nishizuka, Y, Phosphorylation of the EGF receptor from A431 epidermoid carcinoma cells by three distinct types of protein kinase C. FEBS Lett 219 (1987), 215-218.
    • (1987) FEBS Lett , vol.219 , pp. 215-218
    • Ido, M.1    Sekiguchi, K.2    Kikkawa, U.3    Nishizuka, Y.4
  • 85
    • 0025062069 scopus 로고
    • Neuron-specific protein F1/GAP-43 shows substrate specificity for the beta subtype of protein kinase C
    • Sheu, FS, Marais, RM, Parker, PJ, et al. Neuron-specific protein F1/GAP-43 shows substrate specificity for the beta subtype of protein kinase C. Biochem Biophys Res Commun 171 (1990), 1236-1243.
    • (1990) Biochem Biophys Res Commun , vol.171 , pp. 1236-1243
    • Sheu, F.S.1    Marais, R.M.2    Parker, P.J.3
  • 86
    • 0025663760 scopus 로고
    • Identification of a specialized adenylyl cyclase that may mediate odorant detection
    • Bakalyar, HA, Reed, RR, Identification of a specialized adenylyl cyclase that may mediate odorant detection. Science 250 (1990), 1403-1406.
    • (1990) Science , vol.250 , pp. 1403-1406
    • Bakalyar, H.A.1    Reed, R.R.2
  • 88
    • 0025719492 scopus 로고
    • Cloning and expression of a widely distributed (type IV) adenylyl cyclase
    • Gao, BN, Gilman, AG, Cloning and expression of a widely distributed (type IV) adenylyl cyclase. Proc Natl Acad Sci U S A 88 (1991), 10178-10182.
    • (1991) Proc Natl Acad Sci U S A , vol.88 , pp. 10178-10182
    • Gao, B.N.1    Gilman, A.G.2
  • 89
    • 0026680815 scopus 로고
    • Isolation and characterization of a novel cardiac adenylyl-cyclase cDNA
    • Ishikawa, Y, Katsushika, S, Chen, L, et al. Isolation and characterization of a novel cardiac adenylyl-cyclase cDNA. J Biol Chem 267 (1992), 13553-13557.
    • (1992) J Biol Chem , vol.267 , pp. 13553-13557
    • Ishikawa, Y.1    Katsushika, S.2    Chen, L.3
  • 90
    • 0026662548 scopus 로고
    • Cloning and characterization of a sixth adenylyl cyclase isoform: types V, VI constitute a subgroup within the mammalian adenylyl cyclase family
    • Katsushika, S, Chen, L, Kawabe, J, et al. Cloning and characterization of a sixth adenylyl cyclase isoform: types V, VI constitute a subgroup within the mammalian adenylyl cyclase family. Proc Natl Acad Sci U S A 89 (1992), 8774-8778.
    • (1992) Proc Natl Acad Sci U S A , vol.89 , pp. 8774-8778
    • Katsushika, S.1    Chen, L.2    Kawabe, J.3
  • 91
    • 0026744081 scopus 로고
    • Two members of a widely expressed subfamily of hormone-stimulated adenylyl cyclases
    • Premont, RT, Chen, J, Ma, HW, et al. Two members of a widely expressed subfamily of hormone-stimulated adenylyl cyclases. Proc Natl Acad Sci U S A 89 (1992), 9809-9813.
    • (1992) Proc Natl Acad Sci U S A , vol.89 , pp. 9809-9813
    • Premont, R.T.1    Chen, J.2    Ma, H.W.3
  • 93
    • 0026684825 scopus 로고
    • Cloning and expression of a Ca inhibitable adenylyl cyclase from NCB-20 cells
    • Yoshimura, M, Cooper, DMF, Cloning and expression of a Ca inhibitable adenylyl cyclase from NCB-20 cells. Proc Natl Acad Sci U S A 89 (1992), 6716-6720.
    • (1992) Proc Natl Acad Sci U S A , vol.89 , pp. 6716-6720
    • Yoshimura, M.1    Cooper, D.M.F.2
  • 94
    • 0028010777 scopus 로고
    • Molecular cloning and expression of a novel type V adenylyl cyclase from rabbit myocardium
    • Wallach, J, Droste, M, Kluxen, FW, et al. Molecular cloning and expression of a novel type V adenylyl cyclase from rabbit myocardium. FEBS Lett 338 (1994), 257-263.
    • (1994) FEBS Lett , vol.338 , pp. 257-263
    • Wallach, J.1    Droste, M.2    Kluxen, F.W.3
  • 95
    • 0027973059 scopus 로고
    • Molecular cloning and characterization of the type VII isoform of mammalian adenylyl cyclase expressed widely in mouse tissues and in S49 mouse lymphoma cells
    • Watson, PA, Krupinski, J, Kempinski, AM, Frankefield, CD, Molecular cloning and characterization of the type VII isoform of mammalian adenylyl cyclase expressed widely in mouse tissues and in S49 mouse lymphoma cells. J Biol Chem 269 (1994), 28893-28898.
    • (1994) J Biol Chem , vol.269 , pp. 28893-28898
    • Watson, P.A.1    Krupinski, J.2    Kempinski, A.M.3    Frankefield, C.D.4
  • 96
    • 0027253845 scopus 로고
    • Cloning, chromosomal mapping, and expression of human fetal brain type I adenylyl cyclase
    • Villacres, EC, Xia, Z, Bookbinder, LH, et al. Cloning, chromosomal mapping, and expression of human fetal brain type I adenylyl cyclase. Genomics 16 (1993), 473-478.
    • (1993) Genomics , vol.16 , pp. 473-478
    • Villacres, E.C.1    Xia, Z.2    Bookbinder, L.H.3
  • 97
    • 0027497599 scopus 로고
    • Cloning and expression of an adenylyl cyclase localized to the corpus striatum
    • Glatt, CE, Snyder, SH, Cloning and expression of an adenylyl cyclase localized to the corpus striatum. Nature 361 (1993), 536-538.
    • (1993) Nature , vol.361 , pp. 536-538
    • Glatt, C.E.1    Snyder, S.H.2
  • 98
    • 0027969059 scopus 로고
    • Molecular cloning of the human type VIII adenylyl cyclase
    • Defer, N, Marinx, O, Stengel, D, et al. Molecular cloning of the human type VIII adenylyl cyclase. FEBS Lett 351 (1994), 109-113.
    • (1994) FEBS Lett , vol.351 , pp. 109-113
    • Defer, N.1    Marinx, O.2    Stengel, D.3
  • 99
    • 0028685657 scopus 로고
    • Prediction of the coding sequences of unidentified human genes. I. The coding sequences of 40 new genes (KIAA0001-KIAA0040) deduced by analysis of randomly sampled cDNA clones from human immature myeloid cell line KG-1
    • Nomura, N, Miyajima, N, Sazuka, T, et al. Prediction of the coding sequences of unidentified human genes. I. The coding sequences of 40 new genes (KIAA0001-KIAA0040) deduced by analysis of randomly sampled cDNA clones from human immature myeloid cell line KG-1. DNA Res 1 (1994), 27-35.
    • (1994) DNA Res , vol.1 , pp. 27-35
    • Nomura, N.1    Miyajima, N.2    Sazuka, T.3
  • 100
    • 0028344138 scopus 로고
    • Down-regulation of adenylylclase types V, VI mRNA levels in pacing-induced heart failure
    • Ishikawa, Y, Sorota, S, Kiuchi, K, et al. Down-regulation of adenylylclase types V, VI mRNA levels in pacing-induced heart failure. J Clin Invest 93 (1994), 2224-2229.
    • (1994) J Clin Invest , vol.93 , pp. 2224-2229
    • Ishikawa, Y.1    Sorota, S.2    Kiuchi, K.3
  • 101
    • 0028271413 scopus 로고
    • Changes in type VI adenylylcyclase isoform expression correlate with a decreased capacity for cyclic AMP generation in the aging ventricle
    • Tobise, K, Ishikawa, Y, Holmer, SR, et al. Changes in type VI adenylylcyclase isoform expression correlate with a decreased capacity for cyclic AMP generation in the aging ventricle. Circ Res 74 (1994), 596-603.
    • (1994) Circ Res , vol.74 , pp. 596-603
    • Tobise, K.1    Ishikawa, Y.2    Holmer, S.R.3
  • 103
    • 0027513980 scopus 로고
    • Type-specific stimulation of adenylylcyclase by protein kinase C
    • Yoshimura, M, Cooper, DM, Type-specific stimulation of adenylylcyclase by protein kinase C. J Biol Chem 268 (1993), 4604-4607.
    • (1993) J Biol Chem , vol.268 , pp. 4604-4607
    • Yoshimura, M.1    Cooper, D.M.2
  • 104
    • 0027528490 scopus 로고
    • Phorbol ester stimulation of the type I, type III adenylyl cyclases in whole cells
    • Choi, EJ, Wong, ST, Dittman, AH, Storm, DR, Phorbol ester stimulation of the type I, type III adenylyl cyclases in whole cells. Biochemistry 32 (1993), 1891-1894.
    • (1993) Biochemistry , vol.32 , pp. 1891-1894
    • Choi, E.J.1    Wong, S.T.2    Dittman, A.H.3    Storm, D.R.4
  • 105
    • 0028029718 scopus 로고
    • Regulation of forskolin interaction with type I, II, V, VI adenylyl cyclases
    • Sutkowski, EM, Tang, W-J, Broome, CW, et al. Regulation of forskolin interaction with type I, II, V, VI adenylyl cyclases. Biochemistry 33 (1994), 12852-12859.
    • (1994) Biochemistry , vol.33 , pp. 12852-12859
    • Sutkowski, E.M.1    Tang, W.-J.2    Broome, C.W.3
  • 106
    • 0027200238 scopus 로고
    • i-alpha and specific suppression of type 2 adenylyl cyclase inhibition by phorbol ester treatment
    • i-alpha and specific suppression of type 2 adenylyl cyclase inhibition by phorbol ester treatment. J Biol Chem 268 (1993), 12253-12256.
    • (1993) J Biol Chem , vol.268 , pp. 12253-12256
    • Chen, J.1    Iyengar, R.2
  • 107
    • 0027984236 scopus 로고
    • Type I adenylyl cyclase functions as a coincidence detector for control of cyclic AMP response element-mediated transcription: synergistic regulation of transcription by Ca and isoproterenol
    • Impey, S, Wayman, G, Wu, Z, Storm, DR, Type I adenylyl cyclase functions as a coincidence detector for control of cyclic AMP response element-mediated transcription: synergistic regulation of transcription by Ca and isoproterenol. Mol Cell Biol 14 (1994), 8272-8281.
    • (1994) Mol Cell Biol , vol.14 , pp. 8272-8281
    • Impey, S.1    Wayman, G.2    Wu, Z.3    Storm, D.R.4
  • 108
    • 0027458559 scopus 로고
    • Regulation of purified type I, type II adenylylcyclases by G protein beta gamma subunits
    • Taussig, R, Quarmby, LM, Gilman, AG, Regulation of purified type I, type II adenylylcyclases by G protein beta gamma subunits. J Biol Chem 268 (1993), 9-12.
    • (1993) J Biol Chem , vol.268 , pp. 9-12
    • Taussig, R.1    Quarmby, L.M.2    Gilman, A.G.3
  • 110
    • 0028049921 scopus 로고
    • Conditional activation of cAMP signal transduction by protein kinase C: the effect of phorbol esters on adenylyl cyclase in permeabilized and intact cells
    • Morimoto, BH, Koshland, DEJ, Conditional activation of cAMP signal transduction by protein kinase C: the effect of phorbol esters on adenylyl cyclase in permeabilized and intact cells. J Biol Chem 269 (1994), 4065-4069.
    • (1994) J Biol Chem , vol.269 , pp. 4065-4069
    • Morimoto, B.H.1    Koshland, D.E.J.2
  • 112
    • 0027948988 scopus 로고
    • Phorbol ester-induced stimulation and phosphorylation of adenylyl cyclase 2
    • Jacobowitz, O, Iyengar, R, Phorbol ester-induced stimulation and phosphorylation of adenylyl cyclase 2. Proc Natl Acad Sci USA 91 (1994), 10630-10634.
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 10630-10634
    • Jacobowitz, O.1    Iyengar, R.2
  • 113
    • 0028239791 scopus 로고
    • Differential activation of adenylylcyclase by protein kinase C isoenzymes
    • Kawabe, J, Iwani, G, Ebina, T, et al. Differential activation of adenylylcyclase by protein kinase C isoenzymes. J Biol Chem 269 (1994), 16554-16558.
    • (1994) J Biol Chem , vol.269 , pp. 16554-16558
    • Kawabe, J.1    Iwani, G.2    Ebina, T.3
  • 114
    • 0031025684 scopus 로고    scopus 로고
    • Conformation-dependent activation of type II adenylyl cyclase by protein kinase C
    • Ebina, T, Kawabe, J, Ishikawa, Y, Conformation-dependent activation of type II adenylyl cyclase by protein kinase C. J Cell Biochem 64 (1997), 492-498.
    • (1997) J Cell Biochem , vol.64 , pp. 492-498
    • Ebina, T.1    Kawabe, J.2    Ishikawa, Y.3
  • 115
    • 0029998598 scopus 로고    scopus 로고
    • Protein kinase C alters the responsiveness of a denylyl cyclase to G protein α and βγ subunits
    • Zimmermann, G, Taussig, R, Protein kinase C alters the responsiveness of a denylyl cyclase to G protein α and βγ subunits. J Biol Chem 271 (1996), 27161-27166.
    • (1996) J Biol Chem , vol.271 , pp. 27161-27166
    • Zimmermann, G.1    Taussig, R.2
  • 116
    • 0025874613 scopus 로고
    • Expression and characterization of calmodulin-activated (type I) adenylyl cyclase
    • Tang, WJ, Krupinski, J, Gilman, AG, Expression and characterization of calmodulin-activated (type I) adenylyl cyclase. J Biol Chem 266 (1991), 8595-8603.
    • (1991) J Biol Chem , vol.266 , pp. 8595-8603
    • Tang, W.J.1    Krupinski, J.2    Gilman, A.G.3
  • 117
    • 0026658539 scopus 로고
    • Purification and characterization of the ξ isoform of protein kinase from bovine kidney
    • Nakanishi, H, Exton, JH, Purification and characterization of the ξ isoform of protein kinase from bovine kidney. J Biol Chem 267 (1992), 16347-16354.
    • (1992) J Biol Chem , vol.267 , pp. 16347-16354
    • Nakanishi, H.1    Exton, J.H.2
  • 118
    • 0027255130 scopus 로고
    • Activation and substrate specificity of the human protein kinase C alpha and zeta isoenzymes
    • Kochs, G, Hummel, R, Meyer, D, et al. Activation and substrate specificity of the human protein kinase C alpha and zeta isoenzymes. Eur J Biochem 216 (1993), 597-606.
    • (1993) Eur J Biochem , vol.216 , pp. 597-606
    • Kochs, G.1    Hummel, R.2    Meyer, D.3
  • 119
    • 0028264058 scopus 로고
    • Involvement of phosphoinositotide 3-kinase in insulin- or IGF-1-induced membrane ruffling
    • Kotani, K, Yonezawa, K, Hara, K, et al. Involvement of phosphoinositotide 3-kinase in insulin- or IGF-1-induced membrane ruffling. EMBO J 13 (1994), 2313-2321.
    • (1994) EMBO J , vol.13 , pp. 2313-2321
    • Kotani, K.1    Yonezawa, K.2    Hara, K.3
  • 120
    • 0026746481 scopus 로고
    • Evidence for a role of protein kinase C ζ subspecies in maturation of Xenopus laevis oocytes
    • Domingesz, I, Diaz-Meco, MT, Municio, MM, et al. Evidence for a role of protein kinase C ζ subspecies in maturation of Xenopus laevis oocytes. Mol Cell Biol 12 (1992), 3776-3783.
    • (1992) Mol Cell Biol , vol.12 , pp. 3776-3783
    • Domingesz, I.1    Diaz-Meco, M.T.2    Municio, M.M.3
  • 121
    • 0029995139 scopus 로고    scopus 로고
    • Regulation of type V adenylyl cyclase by PMA-sensitive and-insensitive protein kinase C isoenzymes in intact cells
    • Kawabe, J, Ebina, T, Toya, Y, et al. Regulation of type V adenylyl cyclase by PMA-sensitive and-insensitive protein kinase C isoenzymes in intact cells. FEBS Lett 384 (1996), 273-276.
    • (1996) FEBS Lett , vol.384 , pp. 273-276
    • Kawabe, J.1    Ebina, T.2    Toya, Y.3
  • 122
    • 84989067397 scopus 로고
    • Regulation of the adenylyl cyclase signaling pathway: potential role for the phosphorylation of the catalytic unit by protein kinase A and protein kinase C
    • KW McKerns M Chretien Plenum New York
    • Yoshimasa, T, Bouvier, M, Benovic, JL, et al. Regulation of the adenylyl cyclase signaling pathway: potential role for the phosphorylation of the catalytic unit by protein kinase A and protein kinase C. McKerns, KW, Chretien, M, (eds.) Molecular biology of brain and endocrine peptidergic systems, 1988, Plenum, New York, 123-139.
    • (1988) Molecular biology of brain and endocrine peptidergic systems , pp. 123-139
    • Yoshimasa, T.1    Bouvier, M.2    Benovic, J.L.3
  • 123
    • 0026460414 scopus 로고
    • Lowered responsiveness of the catalyst of adenylyl cyclase to stimulation by GS in heterologous desensitization: a role for adenosine 3′, 5′-monophosphate-dependent phosphorylation
    • Premont, RT, Jacobowitz, O, Iyengar, R, Lowered responsiveness of the catalyst of adenylyl cyclase to stimulation by GS in heterologous desensitization: a role for adenosine 3′, 5′-monophosphate-dependent phosphorylation. Endocrinology 131 (1992), 2774-2784.
    • (1992) Endocrinology , vol.131 , pp. 2774-2784
    • Premont, R.T.1    Jacobowitz, O.2    Iyengar, R.3
  • 124
    • 0029074406 scopus 로고
    • Regulation of adenylyl cyclase by protein kinase A
    • Iwami, G, Kawabe, J, Ebina, T, et al. Regulation of adenylyl cyclase by protein kinase A. J Biol Chem 270 (1995), 12481-12484.
    • (1995) J Biol Chem , vol.270 , pp. 12481-12484
    • Iwami, G.1    Kawabe, J.2    Ebina, T.3
  • 126
    • 0028286755 scopus 로고
    • Differential regulation by cAMP dependent protein kinase and protein kinase C of the μ opioid receptor coupling to a G protein-activated K channel
    • Chen, Y, Yu, L, Differential regulation by cAMP dependent protein kinase and protein kinase C of the μ opioid receptor coupling to a G protein-activated K channel. J Biol Chem 269 (1994), 7839-7842.
    • (1994) J Biol Chem , vol.269 , pp. 7839-7842
    • Chen, Y.1    Yu, L.2
  • 127
    • 0024815622 scopus 로고
    • Epidermal growth factor stimulates rat cardiac adenylate cyclase through a GTP-binding regulatory protein
    • Nair, BG, Rashed, HM, Patel, TB, Epidermal growth factor stimulates rat cardiac adenylate cyclase through a GTP-binding regulatory protein. Biochem J 264 (1989), 563-571.
    • (1989) Biochem J , vol.264 , pp. 563-571
    • Nair, B.G.1    Rashed, H.M.2    Patel, T.B.3
  • 128
    • 0025572744 scopus 로고
    • sα mediates epidermal growth factor elicited stimulation of rat cardiac adenylate cyclase
    • sα mediates epidermal growth factor elicited stimulation of rat cardiac adenylate cyclase. J Biol Chem 265 (1990), 21317-21322.
    • (1990) J Biol Chem , vol.265 , pp. 21317-21322
    • Nair, B.G.1    Parikh, B.2    Milligan, G.3    Patel, T.B.4
  • 129
    • 0027414643 scopus 로고
    • Epidermal growth factor produces inotropic and chronotropic effects in rat hearts by increasing cyclic AMP accumulation
    • Nair, BG, Rashed, HM, Patel, TB, Epidermal growth factor produces inotropic and chronotropic effects in rat hearts by increasing cyclic AMP accumulation. Growth Factors 8 (1993), 41-48.
    • (1993) Growth Factors , vol.8 , pp. 41-48
    • Nair, B.G.1    Rashed, H.M.2    Patel, T.B.3
  • 130
    • 0028867206 scopus 로고
    • Expression of type V adenylyl cyclase is required for epidermal growth factor-mediated stimulation of cAMP accumulation
    • Chen, Z, Nield, HS, Sun, H, et al. Expression of type V adenylyl cyclase is required for epidermal growth factor-mediated stimulation of cAMP accumulation. J Biol Chem 270 (1995), 27525-27530.
    • (1995) J Biol Chem , vol.270 , pp. 27525-27530
    • Chen, Z.1    Nield, H.S.2    Sun, H.3
  • 131
    • 0026681492 scopus 로고
    • Stimulation of the type III olfactory adenylyl cyclase by calcium and calmodulin
    • Choi, EJ, Xia, Z, Storm, DR, Stimulation of the type III olfactory adenylyl cyclase by calcium and calmodulin. Biochemistry 31 (1992), 6492-6498.
    • (1992) Biochemistry , vol.31 , pp. 6492-6498
    • Choi, E.J.1    Xia, Z.2    Storm, D.R.3
  • 132
    • 0028982257 scopus 로고
    • Ca inhibition of type III adenylyl cyclase in vivo
    • Wayman, GA, Impey, S, Storm, DR, Ca inhibition of type III adenylyl cyclase in vivo. J Biol Chem 270 (1995), 21480-21486.
    • (1995) J Biol Chem , vol.270 , pp. 21480-21486
    • Wayman, G.A.1    Impey, S.2    Storm, D.R.3
  • 133
    • 0028285191 scopus 로고
    • Caveolae, caveolin and caveolin-rich membrane domains: a signaling hypothesis
    • Lisanti, MP, Scherer, PE, Tang, Z, Sargiacomo, M, Caveolae, caveolin and caveolin-rich membrane domains: a signaling hypothesis. Trends Cell Biol 4 (1994), 231-235.
    • (1994) Trends Cell Biol , vol.4 , pp. 231-235
    • Lisanti, M.P.1    Scherer, P.E.2    Tang, Z.3    Sargiacomo, M.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.