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Volumn 58, Issue 4, 2011, Pages 345-353

Local termination of 3′-5′-cyclic adenosine monophosphate signals: The role of a kinase anchoring protein-tethered phosphodiesterases

Author keywords

AKAP; cAMP; compartmentalization; heart; PDE; PKA; signaling

Indexed keywords

CYCLIC AMP; CYCLIC AMP DEPENDENT PROTEIN KINASE; CYCLIC AMP DEPENDENT PROTEIN KINASE ANCHORING PROTEIN; MEMBRANE PROTEIN; MICROTUBULE ASSOCIATED PROTEIN 2; MITOGEN ACTIVATED PROTEIN KINASE; MITOGEN ACTIVATED PROTEIN KINASE 7; MUSCLE SPECIFIC A KINASE ANCHORING PROTEIN; PHOSPHODIESTERASE; PHOSPHODIESTERASE 4D3; PHOSPHODIESTERASE IV; UNCLASSIFIED DRUG; YOTIAO PROTEIN;

EID: 80053974395     PISSN: 01602446     EISSN: 15334023     Source Type: Journal    
DOI: 10.1097/FJC.0b013e3182214f2b     Document Type: Review
Times cited : (12)

References (139)
  • 1
    • 0013886529 scopus 로고
    • The role of cyclic-3′,5′-AMP in responses to catecholamines and other hormones
    • Sutherland EW, Robison GA. The role of cyclic-3′,5′-AMP in responses to catecholamines and other hormones. Pharmacol Rev. 1966;18: 145-161.
    • (1966) Pharmacol Rev , vol.18 , pp. 145-161
    • Sutherland, E.W.1    Robison, G.A.2
  • 2
    • 0014409394 scopus 로고
    • An adenosine 3′,5′-monophosphatedependant protein kinase from rabbit skeletal muscle
    • Walsh DA, Perkins JP, Krebs EG. An adenosine 3′,5′- monophosphatedependant protein kinase from rabbit skeletal muscle. J Biol Chem. 1968;243:3763-3765.
    • (1968) J Biol Chem , vol.243 , pp. 3763-3765
    • Walsh, D.A.1    Perkins, J.P.2    Krebs, E.G.3
  • 3
    • 0015040105 scopus 로고
    • Interconversion of cyclic nucleotide-activated and cyclic nucleotide-independent forms of a protein kinase from beef heart
    • Erlichman J, Hirsch AH, Rosen OM. Interconversion of cyclic nucleotide-activated and cyclic nucleotide-independent forms of a protein kinase from beef heart. Proc Natl Acad Sci U S A. 1971;68:731-735.
    • (1971) Proc Natl Acad Sci U S A , vol.68 , pp. 731-735
    • Erlichman, J.1    Hirsch, A.H.2    Rosen, O.M.3
  • 4
    • 0015501756 scopus 로고
    • Cyclic adenosine 3′,5′-monophosphate- dependent protein kinase of human erythrocyte membranes
    • Rubin CS, Erlichman J, Rosen OM. Cyclic adenosine 3′,5′- monophosphate- dependent protein kinase of human erythrocyte membranes. J Biol Chem. 1972;247:6135-6139.
    • (1972) J Biol Chem , vol.247 , pp. 6135-6139
    • Rubin, C.S.1    Erlichman, J.2    Rosen, O.M.3
  • 5
    • 0015499968 scopus 로고
    • Molecular forms and subunit composition of a cyclic adenosine 3′,5′-monophosphate-dependent protein kinase purified from bovine heart muscle
    • Rubin CS, Erlichman J, Rosen OM. Molecular forms and subunit composition of a cyclic adenosine 3′,5′-monophosphate-dependent protein kinase purified from bovine heart muscle. J Biol Chem. 1972; 247:36-44.
    • (1972) J Biol Chem , vol.247 , pp. 36-44
    • Rubin, C.S.1    Erlichman, J.2    Rosen, O.M.3
  • 6
    • 0016417543 scopus 로고
    • Molecular structure and characterization of bovine heart protein kinase
    • Rosen OM, Erlichman J, Rubin CS. Molecular structure and characterization of bovine heart protein kinase. Adv Cyclic Nucleotide Res. 1975;5:253-263.
    • (1975) Adv Cyclic Nucleotide Res , vol.5 , pp. 253-263
    • Rosen, O.M.1    Erlichman, J.2    Rubin, C.S.3
  • 7
    • 0014690595 scopus 로고
    • An adenosine 3′,5′-monophosphate-dependent protein kinase from Escherichia coli
    • Kuo JF, Greengard P. An adenosine 3′,5′-monophosphate- dependent protein kinase from Escherichia coli. J Biol Chem. 1969;244:3417-3419.
    • (1969) J Biol Chem , vol.244 , pp. 3417-3419
    • Kuo, J.F.1    Greengard, P.2
  • 8
    • 0016430836 scopus 로고
    • The distribution and dissociation of cyclic adenosine 3′:5′-monophosphate-dependent protein kinases in adipose, cardiac, and other tissues
    • Corbin JD, Keely SL, Park CR. The distribution and dissociation of cyclic adenosine 3′:5′-monophosphate-dependent protein kinases in adipose, cardiac, and other tissues. J Biol Chem. 1975;250:218-225.
    • (1975) J Biol Chem , vol.250 , pp. 218-225
    • Corbin, J.D.1    Keely, S.L.2    Park, C.R.3
  • 9
    • 0016772776 scopus 로고
    • Comparison of adenosine 3′:5′- monophosphate-dependent protein kinases from rabbit skeletal and bovine heart muscle
    • Hofmann F, Beavo JA, Bechtel PJ, et al. Comparison of adenosine 3′:5′- monophosphate-dependent protein kinases from rabbit skeletal and bovine heart muscle. J Biol Chem. 1975;250:7795-7801.
    • (1975) J Biol Chem , vol.250 , pp. 7795-7801
    • Hofmann, F.1    Beavo, J.A.2    Bechtel, P.J.3
  • 10
    • 0017870723 scopus 로고
    • Phosphorylated proteins as physiological effectors
    • Greengard P. Phosphorylated proteins as physiological effectors. Science. 1978;199:146-152.
    • (1978) Science , vol.199 , pp. 146-152
    • Greengard, P.1
  • 11
    • 0017684387 scopus 로고
    • Compartmentalization of adenosine 3':5' monophosphate and adenosine 3':5' monophosphate dependent protein kinase in heart tissue
    • Corbin JD, Sugden PH, Lincoln TM, et al. Compartmentalization of adenosine 3′:5′-monophosphate and adenosine 3′:5′- monophosphate-dependent protein kinase in heart tissue. J Biol Chem. 1977;252:3854-3861. (Pubitemid 8127237)
    • (1977) Journal of Biological Chemistry , vol.252 , Issue.11 , pp. 3854-3861
    • Corbin, J.D.1    Sugden, P.H.2    Lincoln, T.M.3    Keely, S.L.4
  • 12
    • 0018361511 scopus 로고
    • Hormonally specific phosphorylation of cardiac troponin I and activation of glycogen phosphorylase
    • DOI 10.1038/280078a0
    • Brunton LL, Hayes JS, Mayer SE. Hormonally specific phosphorylation of cardiac troponin I and activation of glycogen phosphorylase. Nature. 1979;280:78-80. (Pubitemid 9221184)
    • (1979) Nature , vol.280 , Issue.5717 , pp. 78-80
    • Brunton, L.L.1    Hayes, J.S.2    Mayer, S.E.3
  • 13
    • 0021023294 scopus 로고
    • Compartments of cyclic AMP and protein kinase in mammalian cardiomyocytes
    • Buxton IL, Brunton LL. Compartments of cyclic AMP and protein kinase in mammalian cardiomyocytes. J Biol Chem. 1983;258: 10233-10239. (Pubitemid 14241179)
    • (1983) Journal of Biological Chemistry , vol.258 , Issue.17 , pp. 10233-10239
    • Buxton, I.L.O.1    Brunton, L.L.2
  • 15
    • 0017752640 scopus 로고
    • Activation of cAMP-dependent protein kinase without a corresponding increase in phosphorylase activity
    • Keely SL. Activation of cAMP-dependent protein kinase without a corresponding increase in phosphorylase activity. Res Commun Chem Pathol Pharmacol. 1977;18:283-290. (Pubitemid 8203511)
    • (1977) Research Communications in Chemical Pathology and Pharmacology , vol.18 , Issue.2 , pp. 283-290
    • Keely, S.L.1
  • 17
    • 0033618343 scopus 로고    scopus 로고
    • G (i) protein-mediated functional compartmentalization of cardiac beta (2)-adrenergic signaling
    • Kuschel M, Zhou YY, Cheng H, et al. G(i) protein-mediated functional compartmentalization of cardiac beta(2)-adrenergic signaling. J Biol Chem. 1999;274:22048-22052.
    • (1999) J Biol Chem , vol.274 , pp. 22048-22052
    • Kuschel, M.1    Zhou, Y.Y.2    Cheng, H.3
  • 18
    • 0028175901 scopus 로고
    • 2+ dynamics, contractility, or phospholamban phosphorylation
    • 2+ dynamics, contractility, or phospholamban phosphorylation. J Biol Chem. 1994;269:19151-19156.
    • (1994) J Biol Chem , vol.269 , pp. 19151-19156
    • Xiao, R.P.1    Hohl, C.2    Altschuld, R.3
  • 19
    • 0035980166 scopus 로고    scopus 로고
    • Glucagon-like peptide-1 increases cAMP but fails to augment contraction in adult rat cardiac myocytes
    • Vila Petroff MG, Egan JM, Wang X, et al. Glucagon-like peptide-1 increases cAMP but fails to augment contraction in adult rat cardiac myocytes. Circ Res. 2001;89:445-452. (Pubitemid 34132661)
    • (2001) Circulation Research , vol.89 , Issue.5 , pp. 445-452
    • Vila Petroff, M.G.1    Egan, J.M.2    Wang, X.3    Sollott, S.J.4
  • 21
    • 33646776455 scopus 로고    scopus 로고
    • A specific pattern of phosphodiesterases controls the cAMP signals generated by different Gscoupled receptors in adult rat ventricular myocytes
    • Rochais F, Abi-Gerges A, Horner K, et al. A specific pattern of phosphodiesterases controls the cAMP signals generated by different Gscoupled receptors in adult rat ventricular myocytes. Circ Res. 2006;98: 1081-1088.
    • (2006) Circ Res , vol.98 , pp. 1081-1088
    • Rochais, F.1    Abi-Gerges, A.2    Horner, K.3
  • 22
    • 0033622319 scopus 로고    scopus 로고
    • A genetically encoded, fluorescent indicator for cyclic AMP in living cells
    • Zaccolo M, De Giorgi F, Cho CY, et al. A genetically encoded, fluorescent indicator for cyclic AMP in living cells. Nat Cell Biol. 2000; 2:25-29.
    • (2000) Nat Cell Biol , vol.2 , pp. 25-29
    • Zaccolo, M.1    De Giorgi, F.2    Cho, C.Y.3
  • 23
    • 0036500494 scopus 로고    scopus 로고
    • Discrete microdomains with high concentration of cAMP in stimulated rat neonatal cardiac myocytes
    • DOI 10.1126/science.1069982
    • Zaccolo M, Pozzan T. Discrete microdomains with high concentration of cAMP in stimulated rat neonatal cardiac myocytes. Science. 2002;295: 1711-1715. (Pubitemid 34202906)
    • (2002) Science , vol.295 , Issue.5560 , pp. 1711-1715
    • Zaccolo, M.1    Pozzan, T.2
  • 25
    • 0021196319 scopus 로고
    • Regulation of the cellular and subcellular concentrations and distribution of cyclic nucleotide-dependent protein kinases
    • Lohmann SM, Walter U. Regulation of the cellular and subcellular concentrations and distribution of cyclic nucleotide-dependent protein kinases. Adv Cyclic Nucleotide Protein Phosphorylation Res. 1984;18: 63-117.
    • (1984) Adv Cyclic Nucleotide Protein Phosphorylation Res , vol.18 , pp. 63-117
    • Lohmann, S.M.1    Walter, U.2
  • 26
    • 0026680801 scopus 로고
    • Association of the type II cAMPdependent protein kinase with a human thyroid RII-anchoring protein. Cloning and characterization of the RII-binding domain
    • Carr DW, Hausken ZE, Fraser ID, et al. Association of the type II cAMPdependent protein kinase with a human thyroid RII-anchoring protein. Cloning and characterization of the RII-binding domain. J Biol Chem. 1992;267:13376-13382.
    • (1992) J Biol Chem , vol.267 , pp. 13376-13382
    • Carr, D.W.1    Hausken, Z.E.2    Fraser, I.D.3
  • 27
    • 77952170820 scopus 로고    scopus 로고
    • Specificity and spatial dynamics of protein kinase A signaling organized by A-kinase-anchoring proteins
    • Pidoux G, Tasken K. Specificity and spatial dynamics of protein kinase A signaling organized by A-kinase-anchoring proteins. J Mol Endocrinol. 2010;44:271-284.
    • (2010) J Mol Endocrinol , vol.44 , pp. 271-284
    • Pidoux, G.1    Tasken, K.2
  • 31
    • 0024544243 scopus 로고
    • High affinity binding protein for the regulatory subunit of cAMP-dependent protein kinase II-B. Cloning, characterization, and expression of cDNAs for rat brain P150
    • Bregman DB, Bhattacharyya N, Rubin CS. High affinity binding protein for the regulatory subunit of cAMP-dependent protein kinase II-B. Cloning, characterization, and expression of cDNAs for rat brain P150. J Biol Chem. 1989;264:4648-4656. (Pubitemid 19081372)
    • (1989) Journal of Biological Chemistry , vol.264 , Issue.8 , pp. 4648-4656
    • Bregman, D.B.1    Bhattacharyya, N.2    Rubin, C.S.3
  • 32
    • 0032842848 scopus 로고    scopus 로고
    • MAKAP: An A-kinase anchoring protein targeted to the nuclear membrane of differentiated myocytes
    • Kapiloff MS, Schillace RV, Westphal AM, et al. mAKAP: an A-kinase anchoring protein targeted to the nuclear membrane of differentiated myocytes. J Cell Sci. 1999;112(pt 16):2725-2736. (Pubitemid 29429795)
    • (1999) Journal of Cell Science , vol.112 , Issue.16 , pp. 2725-2736
    • Kapiloff, M.S.1    Schillace, R.V.2    Westphal, A.M.3    Scott, J.D.4
  • 35
    • 0027393093 scopus 로고
    • Ezrin contains cytoskeleton and membrane binding domains accounting for its proposed role as a membrane-cytoskeletal linker
    • Algrain M, Turunen O, Vaheri A, et al. Ezrin contains cytoskeleton and membrane binding domains accounting for its proposed role as a membrane-cytoskeletal linker. J Cell Biol. 1993;120:129-139.
    • (1993) J Cell Biol , vol.120 , pp. 129-139
    • Algrain, M.1    Turunen, O.2    Vaheri, A.3
  • 37
    • 77951745863 scopus 로고    scopus 로고
    • Sphingosine kinase interacting protein is an A-kinase anchoring protein specific for type i cAMP-dependent protein kinase
    • Kovanich D, van der Heyden MA, Aye TT, et al. Sphingosine kinase interacting protein is an A-kinase anchoring protein specific for type I cAMP-dependent protein kinase. Chembiochem. 2010;11:963-971.
    • (2010) Chembiochem , vol.11 , pp. 963-971
    • Kovanich, D.1    Van Der Heyden, M.A.2    Aye, T.T.3
  • 38
    • 0030903895 scopus 로고    scopus 로고
    • Identification of a novel protein kinase A anchoring protein that binds both type I and type II regulatory subunits
    • DOI 10.1074/jbc.272.12.8057
    • Huang LJ, Durick K, Weiner JA, et al. Identification of a novel protein kinase A anchoring protein that binds both type I and type II regulatory subunits. J Biol Chem. 1997;272:8057-8064. (Pubitemid 27137372)
    • (1997) Journal of Biological Chemistry , vol.272 , Issue.12 , pp. 8057-8064
    • Huang, L.J.-S.1    Durick, K.2    Weiner, J.A.3    Chun, J.4    Taylor, S.S.5
  • 40
    • 33748292994 scopus 로고    scopus 로고
    • Compartmentalized cAMP/PKA signalling regulates cardiac excitation-contraction coupling
    • DOI 10.1007/s10974-006-9077-2
    • Lissandron V, Zaccolo M. Compartmentalized cAMP/PKA signalling regulates cardiac excitation-contraction coupling. J Muscle Res Cell Motil. 2006;27:399-403. (Pubitemid 44325618)
    • (2006) Journal of Muscle Research and Cell Motility , vol.27 , Issue.5-7 , pp. 399-403
    • Lissandron, V.1    Zaccolo, M.2
  • 41
    • 77950473713 scopus 로고    scopus 로고
    • A-kinase anchoring proteins: Getting to the heart of the matter
    • Scott JD, Santana LF. A-kinase anchoring proteins: getting to the heart of the matter. Circulation. 2010;121:1264-1271.
    • (2010) Circulation , vol.121 , pp. 1264-1271
    • Scott, J.D.1    Santana, L.F.2
  • 42
    • 78650950328 scopus 로고    scopus 로고
    • Cardiac troponin T, a sarcomeric AKAP, tethers protein kinase A at the myofilaments
    • Sumandea CA, Garcia-Cazarin ML, Bozio CH, et al. Cardiac troponin T, a sarcomeric AKAP, tethers protein kinase A at the myofilaments. J Biol Chem. 2011;286:530-541.
    • (2011) J Biol Chem , vol.286 , pp. 530-541
    • Sumandea, C.A.1    Garcia-Cazarin, M.L.2    Bozio, C.H.3
  • 44
    • 40649095214 scopus 로고    scopus 로고
    • Modulation of cardiac function by A-kinase anchoring proteins
    • Diviani D. Modulation of cardiac function by A-kinase anchoring proteins. Curr Opin Pharmacol. 2008;8:166-173.
    • (2008) Curr Opin Pharmacol , vol.8 , pp. 166-173
    • Diviani, D.1
  • 45
    • 0034640113 scopus 로고    scopus 로고
    • PKA phosphorylation dissociates FKBP12.6 from the calcium release channel (ryanodine receptor): Defective regulation in failing hearts
    • Marx SO, Reiken S, Hisamatsu Y, et al. PKA phosphorylation dissociates FKBP12.6 from the calcium release channel (ryanodine receptor): defective regulation in failing hearts. Cell. 2000;101:365-376.
    • (2000) Cell , vol.101 , pp. 365-376
    • Marx, S.O.1    Reiken, S.2    Hisamatsu, Y.3
  • 48
    • 33845945668 scopus 로고    scopus 로고
    • 1-adrenergic receptor promotes recycling and functional resensitization of the receptor
    • DOI 10.1074/jbc.M601809200
    • Gardner LA, Tavalin SJ, Goehring AS, et al. AKAP79-mediated targeting of the cyclic AMP-dependent protein kinase to the beta1- adrenergic receptor promotes recycling and functional resensitization of the receptor. J Biol Chem. 2006;281:33537-33553. (Pubitemid 46036735)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.44 , pp. 33537-33553
    • Gardner, L.A.1    Tavalin, S.J.2    Goehring, A.S.3    Scott, J.D.4    Bahouth, S.W.5
  • 49
    • 1842866233 scopus 로고    scopus 로고
    • AKAPs (A-kinase anchoring proteins) and molecules that compose their G-protein-coupled receptor signalling complexes
    • DOI 10.1042/BJ20031648
    • Malbon CC, Tao J,Wang HY. AKAPs (A-kinase anchoring proteins) and molecules that compose their G-protein-coupled receptor signalling complexes. Biochem J. 2004;379:1-9. (Pubitemid 38491353)
    • (2004) Biochemical Journal , vol.379 , Issue.1 , pp. 1-9
    • Malbon, C.C.1    Tao, J.2    Wang, H.-Y.3
  • 50
    • 34250340916 scopus 로고    scopus 로고
    • 2-adrenergic receptor resensitization and recycling
    • DOI 10.1074/jbc.M608927200
    • Tao J, Wang HY, Malbon CC. Src docks to A-kinase anchoring protein gravin, regulating beta2-adrenergic receptor resensitization and recycling. J Biol Chem. 2007;282:6597-6608. (Pubitemid 47100888)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.9 , pp. 6597-6608
    • Tao, J.1    Wang, H.-Y.2    Malbon, C.C.3
  • 51
    • 0033554893 scopus 로고    scopus 로고
    • Dynamic complexes of beta2-adrenergic receptors with protein kinases and phosphatases and the role of gravin
    • Shih M, Lin F, Scott JD, et al. Dynamic complexes of beta2-adrenergic receptors with protein kinases and phosphatases and the role of gravin. J Biol Chem. 1999;274:1588-1595.
    • (1999) J Biol Chem , vol.274 , pp. 1588-1595
    • Shih, M.1    Lin, F.2    Scott, J.D.3
  • 52
    • 0035886667 scopus 로고    scopus 로고
    • ATP channels by protein kinase A
    • DOI 10.1111/j.1469-7793.2001.0421c.xd
    • Hayabuchi Y, Dart C, Standen NB. Evidence for involvement of Akinase anchoring protein in activation of rat arterial K(ATP) channels by protein kinase A. J Physiol. 2001;536:421-427. (Pubitemid 32976123)
    • (2001) Journal of Physiology , vol.536 , Issue.2 , pp. 421-427
    • Hayabuchi, Y.1    Dart, C.2    Standen, N.B.3
  • 55
    • 0033345058 scopus 로고    scopus 로고
    • A role for AKAP (A Kinase Anchoring Protein) scaffolding in the loss of a cyclic adenosine 3',5'-monophosphate inhibitory response in late pregnant rat myometrium
    • Dodge KL, Carr DW, Yue C, et al. A role for AKAP (A kinase anchoring protein) scaffolding in the loss of a cyclic adenosine 3′,5′- monophosphate inhibitory response in late pregnant rat myometrium. Mol Endocrinol. 1999;13:1977-1987. (Pubitemid 30637260)
    • (1999) Molecular Endocrinology , vol.13 , Issue.12 , pp. 1977-1987
    • Dodge, K.L.1    Carr, D.W.2    Yue, C.3    Sanborn, B.M.4
  • 56
    • 20444490347 scopus 로고    scopus 로고
    • Role for A kinase-anchoring proteins (AKAPS) in glutamate receptor trafficking and long term synaptic depression
    • DOI 10.1074/jbc.M409693200
    • Snyder EM, Colledge M, Crozier RA, et al. Role for A kinase-anchoring proteins (AKAPS) in glutamate receptor trafficking and long term synaptic depression. J Biol Chem. 2005;280:16962-16968. (Pubitemid 41389157)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.17 , pp. 16962-16968
    • Snyder, E.M.1    Colledge, M.2    Crozier, R.A.3    Chen, W.S.4    Scott, J.D.5    Bear, M.F.6
  • 57
    • 0001559662 scopus 로고
    • Fractionation and characterization of a cyclic adenine ribonucleotide formed by tissue particles
    • Sutherland EW, Rall TW. Fractionation and characterization of a cyclic adenine ribonucleotide formed by tissue particles. J Biol Chem. 1958; 232:1077-1091.
    • (1958) J Biol Chem , vol.232 , pp. 1077-1091
    • Sutherland, E.W.1    Rall, T.W.2
  • 58
    • 33847612208 scopus 로고
    • Adenosine 3′,5′-phosphate in biological materials. I. Purification and properties of cyclic 3′,5′-nucleotide phosphodiesterase and use of this enzyme to characterize adenosine 3′,5′-phosphate in human urine
    • Butcher RW, Sutherland EW. Adenosine 3′,5′-phosphate in biological materials. I. Purification and properties of cyclic 3′,5′-nucleotide phosphodiesterase and use of this enzyme to characterize adenosine 3′,5′-phosphate in human urine. J Biol Chem. 1962;237:1244-1250.
    • (1962) J Biol Chem , vol.237 , pp. 1244-1250
    • Butcher, R.W.1    Sutherland, E.W.2
  • 59
    • 0014938577 scopus 로고
    • Calcium dependent phosphodiesterase activity and its activating factor (PAF) from brain studies on cyclic 3′,5′- nucleotide phosphodiesterase (3)
    • Kakiuchi S, Yamazaki R. Calcium dependent phosphodiesterase activity and its activating factor (PAF) from brain studies on cyclic 3′,5′- nucleotide phosphodiesterase (3). Biochem Biophys Res Commun. 1970; 41:1104-1110.
    • (1970) Biochem Biophys Res Commun , vol.41 , pp. 1104-1110
    • Kakiuchi, S.1    Yamazaki, R.2
  • 60
    • 0015239759 scopus 로고
    • Stimulation of adenosine 3′,5′- monophosphate hydrolysis by guanosine 3′,5′-monophosphate
    • Beavo JA, Hardman JG, Sutherland EW. Stimulation of adenosine 3′,5′- monophosphate hydrolysis by guanosine 3′,5′- monophosphate. J Biol Chem. 1971;246:3841-3846.
    • (1971) J Biol Chem , vol.246 , pp. 3841-3846
    • Beavo, J.A.1    Hardman, J.G.2    Sutherland, E.W.3
  • 61
    • 0015231739 scopus 로고
    • Multiple cyclic nucleotide phosphodiesterase activities from rat brain
    • Thompson WJ, Appleman MM. Multiple cyclic nucleotide phosphodiesterase activities from rat brain. Biochemistry. 1971;10:311-316.
    • (1971) Biochemistry , vol.10 , pp. 311-316
    • Thompson, W.J.1    Appleman, M.M.2
  • 62
    • 0020461444 scopus 로고
    • Identification and properties of cyclic nucleotide phosphodiesterases
    • DOI 10.1016/0303-7207(82)90135-6
    • Beavo JA, Hansen RS, Harrison SA, et al. Identification and properties of cyclic nucleotide phosphodiesterases. Mol Cell Endocrinol. 1982;28: 387-410. (Pubitemid 13253569)
    • (1982) Molecular and Cellular Endocrinology , vol.28 , Issue.3 , pp. 387-410
    • Beavo, J.A.1    Hansen, R.S.2    Harrison, S.A.3
  • 63
    • 0017170010 scopus 로고
    • Mechanism by which psychotropic drugs inhibit adenosine cyclic 3′,5′-monophosphate phosphodiesterase of brain
    • Levin RM, Weiss B. Mechanism by which psychotropic drugs inhibit adenosine cyclic 3′,5′-monophosphate phosphodiesterase of brain. Mol Pharmacol. 1976;12:581-589.
    • (1976) Mol Pharmacol , vol.12 , pp. 581-589
    • Levin, R.M.1    Weiss, B.2
  • 64
    • 0019502743 scopus 로고
    • Inhibition of separated forms of cyclic nucleotide phosphodiesterase from pig coronary arteries by 1,3-disubstituted and 1,3,8-trisubstituted xanthines
    • DOI 10.1021/jm00140a008
    • Wells JN, Garst JE, Kramer GL. Inhibition of separated forms of cyclic nucleotide phosphodiesterase from pig coronary arteries by 1,3- disubstituted and 1,3,8-trisubstituted xanthines. J Med Chem. 1981; 24:954-958. (Pubitemid 11015163)
    • (1981) Journal of Medicinal Chemistry , vol.24 , Issue.8 , pp. 954-958
    • Wells, J.N.1    Garst, J.E.2    Kramer, G.L.3
  • 65
    • 0024616409 scopus 로고
    • Review: Long-term oral therapy of congestive heart failure with phosphodiesterase inhibitors
    • Wood MA, Hess ML. Long-term oral therapy of congestive heart failure with phosphodiesterase inhibitors. Am J Med Sci. 1989;297:105-113. (Pubitemid 19071022)
    • (1989) American Journal of the Medical Sciences , vol.297 , Issue.2 , pp. 105-113
    • Wood, M.A.1    Hess, M.L.2
  • 66
    • 31144433061 scopus 로고    scopus 로고
    • Cyclic nucleotide phosphodiesterase (PDE) superfamily: A new target for the development of specific therapeutic agents
    • DOI 10.1016/j.pharmthera.2005.07.003, PII S0163725805001580
    • Lugnier C. Cyclic nucleotide phosphodiesterase (PDE) superfamily: a new target for the development of specific therapeutic agents. Pharmacol Ther. 2006;109:366-398. (Pubitemid 43132818)
    • (2006) Pharmacology and Therapeutics , vol.109 , Issue.3 , pp. 366-398
    • Lugnier, C.1
  • 67
    • 34447265905 scopus 로고    scopus 로고
    • Biochemistry and physiology of cyclic nucleotide phosphodiesterases: Essential components in cyclic nucleotide signaling
    • Conti M, Beavo J. Biochemistry and physiology of cyclic nucleotide phosphodiesterases: essential components in cyclic nucleotide signaling. Annu Rev Biochem. 2007;76:481-511.
    • (2007) Annu Rev Biochem , vol.76 , pp. 481-511
    • Conti, M.1    Beavo, J.2
  • 69
    • 0037443097 scopus 로고    scopus 로고
    • PDE4 cAMP phosphodiesterases: Modular enzymes that orchestrate signalling cross-talk, desensitization and compartmentalization
    • DOI 10.1042/BJ20021698
    • Houslay MD, Adams DR. PDE4 cAMP phosphodiesterases: modular enzymes that orchestrate signalling cross-talk, desensitization and compartmentalization. Biochem J. 2003;370:1-18. (Pubitemid 36259414)
    • (2003) Biochemical Journal , vol.370 , Issue.1 , pp. 1-18
    • Houslay, M.D.1    Adams, D.R.2
  • 70
    • 49049116205 scopus 로고    scopus 로고
    • PDE4 associates with different scaffolding proteins: Modulating interactions as treatment for certain diseases
    • McCahill AC, Huston E, Li X, et al. PDE4 associates with different scaffolding proteins: modulating interactions as treatment for certain diseases. Handb Exp Pharmacol. 2008:125-166.
    • (2008) Handb Exp Pharmacol , pp. 125-166
    • McCahill, A.C.1    Huston, E.2    Li, X.3
  • 71
    • 0028567796 scopus 로고
    • A novel cyclic GMP stimulated phosphodiesterase from rat brain
    • Yang Q, Paskind M, Bolger G, et al. A novel cyclic GMP stimulated phosphodiesterase from rat brain. Biochem Biophys Res Commun. 1994; 205:1850-1858.
    • (1994) Biochem Biophys Res Commun , vol.205 , pp. 1850-1858
    • Yang, Q.1    Paskind, M.2    Bolger, G.3
  • 72
    • 28244461264 scopus 로고    scopus 로고
    • Isoforms of cyclic nucleotide phosphodiesterase PDE3 and their contribution to cAMP hydrolytic activity in subcellular fractions of human myocardium
    • DOI 10.1074/jbc.M506760200
    • Hambleton R, Krall J, Tikishvili E, et al. Isoforms of cyclic nucleotide phosphodiesterase PDE3 and their contribution to cAMP hydrolytic activity in subcellular fractions of human myocardium. J Biol Chem. 2005;280:39168-39174. (Pubitemid 41713868)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.47 , pp. 39168-39174
    • Hambleton, R.1    Krall, J.2    Tikishvili, E.3    Honeggar, M.4    Ahmad, F.5    Manganiello, V.C.6    Movsesian, M.A.7
  • 73
    • 0030957594 scopus 로고    scopus 로고
    • Structure, localization, and regulation of cGMP-inhibited phosphodiesterase (PDE3)
    • DOI 10.1074/jbc.272.11.6823
    • Degerman E, Belfrage P, Manganiello VC. Structure, localization, and regulation of cGMP-inhibited phosphodiesterase (PDE3). J Biol Chem. 1997;272:6823-6826. (Pubitemid 27166373)
    • (1997) Journal of Biological Chemistry , vol.272 , Issue.11 , pp. 6823-6826
    • Degerman, E.1    Belfrage, P.2    Manganiello, V.C.3
  • 74
    • 33747167330 scopus 로고    scopus 로고
    • CAMP phosphodiesterase-4A1 (PDE4A1) has provided the paradigm for the intracellular targeting of phosphodiesterases, a process that underpins compartmentalized cAMP signalling
    • DOI 10.1042/BST0340504
    • Huston E, Houslay TM, Baillie GS, et al. cAMP phosphodiesterase-4A1 (PDE4A1) has provided the paradigm for the intracellular targeting of phosphodiesterases, a process that underpins compartmentalized cAMP signalling. Biochem Soc Trans. 2006;34:504-509. (Pubitemid 44230748)
    • (2006) Biochemical Society Transactions , vol.34 , Issue.4 , pp. 504-509
    • Huston, E.1    Houslay, T.M.2    Baillie, G.S.3    Houslay, M.D.4
  • 77
    • 79953329375 scopus 로고    scopus 로고
    • PDE4D and PDE4B function in distinct subcellular compartments in mouse embryonic fibroblasts
    • Blackman BE, Horner K, Heidmann J, et al. PDE4D and PDE4B function in distinct subcellular compartments in mouse embryonic fibroblasts. J Biol Chem. 2011;286:530-541.
    • (2011) J Biol Chem , vol.286 , pp. 530-541
    • Blackman, B.E.1    Horner, K.2    Heidmann, J.3
  • 78
    • 0036189968 scopus 로고    scopus 로고
    • In addition to the SH3 binding region, multiple regions within the N-terminal noncatalytic portion of the cAMP-specific phosphodiesterase, PDE4A5, contribute to its intracellular targeting
    • DOI 10.1016/S0898-6568(01)00264-9, PII S0898656801002649
    • Beard MB, Huston E, Campbell L, et al. In addition to the SH3 binding region, multiple regions within the N-terminal noncatalytic portion of the cAMP-specific phosphodiesterase, PDE4A5, contribute to its intracellular targeting. Cell Signal. 2002;14:453-465. (Pubitemid 34214850)
    • (2002) Cellular Signalling , vol.14 , Issue.5 , pp. 453-465
    • Beard, M.B.1    Huston, E.2    Campbell, L.3    Gall, I.4    McPhee, I.5    Yarwood, S.6    Scotland, G.7    Houslay, M.D.8
  • 80
    • 0032882246 scopus 로고    scopus 로고
    • The unique N-terminal domain of the cAMP phosphodiesterase PDE4D4 allows for interaction with specific SH3 domains
    • DOI 10.1016/S0014-5793(99)01335-6, PII S0014579399013356
    • Beard MB, O'Connell JC, Bolger GB, et al. The unique N-terminal domain of the cAMP phosphodiesterase PDE4D4 allows for interaction with specific SH3 domains. FEBS Lett. 1999;460:173-177. (Pubitemid 29479265)
    • (1999) FEBS Letters , vol.460 , Issue.1 , pp. 173-177
    • Beard, M.B.1    O'Connell, J.C.2    Bolger, G.B.3    Houslay, M.D.4
  • 81
    • 0033597139 scopus 로고    scopus 로고
    • Association with the SRC family tyrosyl kinase LYN triggers a conformational change in the catalytic region of human cAMP-specific phosphodiesterase HSPDE4A4B. Consequences for rolipram inhibition
    • McPhee I, Yarwood SJ, Scotland G, et al. Association with the SRC family tyrosyl kinase LYN triggers a conformational change in the catalytic region of human cAMP-specific phosphodiesterase HSPDE4A4B. Consequences for rolipram inhibition. J Biol Chem. 1999;274:11796-11810.
    • (1999) J Biol Chem , vol.274 , pp. 11796-11810
    • McPhee, I.1    Yarwood, S.J.2    Scotland, G.3
  • 85
    • 1542572127 scopus 로고    scopus 로고
    • The unique amino-terminal region of the PDE4D5 cAMP phosphodiesterase isoform confers preferential interaction with beta-arrestins
    • Bolger GB, McCahill A, Huston E, et al. The unique amino-terminal region of the PDE4D5 cAMP phosphodiesterase isoform confers preferential interaction with beta-arrestins. J Biol Chem. 2003;278: 49230-49238.
    • (2003) J Biol Chem , vol.278 , pp. 49230-49238
    • Bolger, G.B.1    McCahill, A.2    Huston, E.3
  • 86
    • 0033591233 scopus 로고    scopus 로고
    • The RACK1 signaling scaffold protein selectively interacts with the cAMP-specific phosphodiesterase PDE4D5 isoform
    • Yarwood SJ, Steele MR, Scotland G, et al. The RACK1 signaling scaffold protein selectively interacts with the cAMP-specific phosphodiesterase PDE4D5 isoform. J Biol Chem. 1999;274:14909-14917.
    • (1999) J Biol Chem , vol.274 , pp. 14909-14917
    • Yarwood, S.J.1    Steele, M.R.2    Scotland, G.3
  • 87
    • 34248333795 scopus 로고    scopus 로고
    • Delineation of RAID1, the RACK1 interaction domain located within the unique N-terminal region of the cAMP-specific phosphodiesterase, PDE4D5
    • Bolger GB, McCahill A, Yarwood SJ, et al. Delineation of RAID1, the RACK1 interaction domain located within the unique N-terminal region of the cAMP-specific phosphodiesterase, PDE4D5. BMC Biochem. 2002;3:24.
    • (2002) BMC Biochem , vol.3 , pp. 24
    • Bolger, G.B.1    McCahill, A.2    Yarwood, S.J.3
  • 88
    • 33646787840 scopus 로고    scopus 로고
    • An anchored PKA and PDE4 complex regulates subplasmalemmal cAMP dynamics
    • Willoughby D, Wong W, Schaack J, et al. An anchored PKA and PDE4 complex regulates subplasmalemmal cAMP dynamics. EMBO J. 2006; 25:2051-2061.
    • (2006) EMBO J , vol.25 , pp. 2051-2061
    • Willoughby, D.1    Wong, W.2    Schaack, J.3
  • 91
    • 34249859626 scopus 로고    scopus 로고
    • Dynamic regulation of cystic fibrosis transmembrane conductance regulator by competitive interactions of molecular adaptors
    • DOI 10.1074/jbc.M610857200
    • Lee JH, Richter W, Namkung W, et al. Dynamic regulation of cystic fibrosis transmembrane conductance regulator by competitive interactions of molecular adaptors. J Biol Chem. 2007;282:10414-10422. (Pubitemid 47093434)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.14 , pp. 10414-10422
    • Ji, H.L.1    Richter, W.2    Namkung, W.3    Kyung, H.K.4    Kim, E.5    Conti, M.6    Min, G.L.7
  • 92
    • 77949472038 scopus 로고    scopus 로고
    • Compartmentalized cyclic adenosine 3′,5′-monophosphate at the plasma membrane clusters PDE3A and cystic fibrosis transmembrane conductance regulator into microdomains
    • Penmatsa H, Zhang W, Yarlagadda S, et al. Compartmentalized cyclic adenosine 3′,5′-monophosphate at the plasma membrane clusters PDE3A and cystic fibrosis transmembrane conductance regulator into microdomains. Mol Biol Cell. 2010;21:1097-1110.
    • (2010) Mol Biol Cell , vol.21 , pp. 1097-1110
    • Penmatsa, H.1    Zhang, W.2    Yarlagadda, S.3
  • 94
    • 65549120682 scopus 로고    scopus 로고
    • Interaction of phosphodiesterase 3A with brefeldin A-inhibited guanine nucleotide-exchange proteins BIG1 and BIG2 and effect on ARF1 activity
    • Puxeddu E, Uhart M, Li CC, et al. Interaction of phosphodiesterase 3A with brefeldin A-inhibited guanine nucleotide-exchange proteins BIG1 and BIG2 and effect on ARF1 activity. Proc Natl Acad Sci U S A. 2009; 106:6158-6163.
    • (2009) Proc Natl Acad Sci U S A , vol.106 , pp. 6158-6163
    • Puxeddu, E.1    Uhart, M.2    Li, C.C.3
  • 98
    • 33644865929 scopus 로고    scopus 로고
    • Compartmentalized phosphodiesterase-2 activity blunts beta-adrenergic cardiac inotropy via an NO/cGMP-dependent pathway
    • Mongillo M, Tocchetti CG, Terrin A, et al. Compartmentalized phosphodiesterase-2 activity blunts beta-adrenergic cardiac inotropy via an NO/cGMP-dependent pathway. Circ Res. 2006;98:226-234.
    • (2006) Circ Res , vol.98 , pp. 226-234
    • Mongillo, M.1    Tocchetti, C.G.2    Terrin, A.3
  • 102
    • 0034789448 scopus 로고    scopus 로고
    • MAKAP and the ryanodine receptor are part of a multi-component signaling complex on the cardiomyocyte nuclear envelope
    • Kapiloff MS, Jackson N, Airhart N. mAKAP and the ryanodine receptor are part of a multi-component signaling complex on the cardiomyocyte nuclear envelope. J Cell Sci. 2001;114:3167-3176. (Pubitemid 32910471)
    • (2001) Journal of Cell Science , vol.114 , Issue.17 , pp. 3167-3176
    • Kapiloff, M.S.1    Jackson, N.2    Airhart, N.3
  • 103
    • 0042090358 scopus 로고    scopus 로고
    • Targeting of Protein Kinase A by Muscle A Kinase-anchoring Protein (mAKAP) Regulates Phosphorylation and Function of the Skeletal Muscle Ryanodine Receptor
    • DOI 10.1074/jbc.M213279200
    • Ruehr ML, Russell MA, Ferguson DG, et al. Targeting of protein kinase A by muscle A kinase-anchoring protein (mAKAP) regulates phosphorylation and function of the skeletal muscle ryanodine receptor. J Biol Chem. 2003;278:24831-24836. (Pubitemid 37548641)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.27 , pp. 24831-24836
    • Ruehr, M.L.1    Russell, M.A.2    Ferguson, D.G.3    Bhat, M.4    Ma, J.5    Damron, D.S.6    Scott, J.D.7    Bond, M.8
  • 104
    • 18544398786 scopus 로고
    • Analysis of a novel A-kinase anchoring protein 100 (AKAP 100)
    • McCartney S, Little BM, Scott JD. Analysis of a novel A-kinase anchoring protein 100 (AKAP 100). Biochem Soc Trans. 1995;23:268S.
    • (1995) Biochem Soc Trans , vol.23
    • McCartney, S.1    Little, B.M.2    Scott, J.D.3
  • 106
    • 12344259872 scopus 로고    scopus 로고
    • Nesprin-1α contributes to the targeting of mAKAP to the cardiac myocyte nuclear envelope
    • DOI 10.1016/j.yexcr.2004.10.009, PII S0014482704005919
    • Pare GC, Easlick JL, Mislow JM, et al. Nesprin-1alpha contributes to the targeting of mAKAP to the cardiac myocyte nuclear envelope. Exp Cell Res. 2005;303:388-399. (Pubitemid 40126271)
    • (2005) Experimental Cell Research , vol.303 , Issue.2 , pp. 388-399
    • Pare, G.C.1    Easlick, J.L.2    Mislow, J.M.3    McNally, E.M.4    Kapiloff, M.S.5
  • 109
    • 0030006920 scopus 로고    scopus 로고
    • Phosphorylation and activation of a cAMP-specific phosphodiesterase by the cAMP-dependent protein kinase. Involvement of serine 54 in the enzyme activation
    • DOI 10.1074/jbc.271.28.16526
    • Sette C, Conti M. Phosphorylation and activation of a cAMP-specific phosphodiesterase by the cAMP-dependent protein kinase. Involvement of serine 54 in the enzyme activation. J Biol Chem. 1996;271:16526-16534. (Pubitemid 26239006)
    • (1996) Journal of Biological Chemistry , vol.271 , Issue.28 , pp. 16526-16534
    • Sette, C.1    Conti, M.2
  • 111
    • 0033558010 scopus 로고    scopus 로고
    • The MAP kinase ERK2 inhibits the cyclic AMP-specific phosphodiesterase HSPDE4D3 by phosphorylating it at ser579
    • DOI 10.1093/emboj/18.4.893
    • Hoffmann R, Baillie GS, MacKenzie SJ, et al. The MAP kinase ERK2 inhibits the cyclic AMP-specific phosphodiesterase HSPDE4D3 by phosphorylating it at Ser579. EMBO J. 1999;18:893-903. (Pubitemid 29082269)
    • (1999) EMBO Journal , vol.18 , Issue.4 , pp. 893-903
    • Hoffmann, R.1    Baillie, G.S.2    MacKenzie, S.J.3    Yarwood, S.J.4    Houslay, M.D.5
  • 113
    • 33646924842 scopus 로고    scopus 로고
    • Cardiac ryanodine receptor phosphorylation: Target sites and functional consequences
    • Bers DM. Cardiac ryanodine receptor phosphorylation: target sites and functional consequences. Biochem J. 2006;396:e1-e3.
    • (2006) Biochem J , vol.396
    • Bers, D.M.1
  • 115
    • 4444382387 scopus 로고    scopus 로고
    • Calcium-calcineurin signaling in the regulation of cardiac hypertrophy
    • DOI 10.1016/j.bbrc.2004.07.121, PII S0006291X04015487
    • Wilkins BJ, Molkentin JD. Calcium-calcineurin signaling in the regulation of cardiac hypertrophy. Biochem Biophys Res Commun. 2004;322:1178-1191. (Pubitemid 39164648)
    • (2004) Biochemical and Biophysical Research Communications , vol.322 , Issue.4 , pp. 1178-1191
    • Wilkins, B.J.1    Molkentin, J.D.2
  • 116
    • 0032520827 scopus 로고    scopus 로고
    • Yotiao, a novel protein of neuromuscular junction and brain that interacts with specific splice variants of NMDA receptor subunit NR1
    • Lin JW, Wyszynski M, Madhavan R, et al. Yotiao, a novel protein of neuromuscular junction and brain that interacts with specific splice variants of NMDA receptor subunit NR1. J Neurosci. 1998;18:2017-2027. (Pubitemid 28141409)
    • (1998) Journal of Neuroscience , vol.18 , Issue.6 , pp. 2017-2027
    • Lin, J.W.1    Wyszynski, M.2    Madhavan, R.3    Sealock, R.4    Kim, J.U.5    Sheng, M.6
  • 118
    • 0345435932 scopus 로고    scopus 로고
    • Cloning and characterization of a cDNA encoding an A-kinase anchoring protein located in the centrosome, AKAP450
    • Witczak O, Skalhegg BS, Keryer G, et al. Cloning and characterization of a cDNA encoding an A-kinase anchoring protein located in the centrosome, AKAP450. EMBO J. 1999;18:1858-1868. (Pubitemid 29158529)
    • (1999) EMBO Journal , vol.18 , Issue.7 , pp. 1858-1868
    • Witczak, O.1    Skalhegg, B.S.2    Keryer, G.3    Bornens, M.4    Tasken, K.5    Jahnsen, T.6    O'Rstavik, S.7
  • 119
    • 0020003884 scopus 로고
    • The ionic basis of concentration-related effects of noradrenaline on the action potential of calf cardiac Purkinje fibres
    • Kass RS, Wiegers SE. The ionic basis of concentration-related effects of noradrenaline on the action potential of calf cardiac purkinje fibres. J Physiol. 1982;322:541-558. (Pubitemid 12177770)
    • (1982) Journal of Physiology , vol.322 , pp. 541-558
    • Kass, R.S.1    Wiegers, S.E.2
  • 120
    • 0024280882 scopus 로고
    • Regulation of a heart potassium channel by protein kinase A and C
    • Walsh KB, Kass RS. Regulation of a heart potassium channel by protein kinase A and C. Science. 1988;242:67-69.
    • (1988) Science , vol.242 , pp. 67-69
    • Walsh, K.B.1    Kass, R.S.2
  • 122
    • 0029952101 scopus 로고    scopus 로고
    • K(V)LQT1 and IsK (minK) proteins associate to form the I(Ks) cardiac potassium current
    • DOI 10.1038/384078a0
    • Barhanin J, Lesage F, Guillemare E, et al. K(V)LQT1 and lsK (minK) proteins associate to form the I(Ks) cardiac potassium current. Nature. 1996;384:78-80. (Pubitemid 26374591)
    • (1996) Nature , vol.384 , Issue.6604 , pp. 78-80
    • Barhanin, J.1    Lesage, F.2    Guillemare, E.3    Fink, M.4    Lazdunski, M.5    Romey, G.6
  • 123
    • 25444529765 scopus 로고    scopus 로고
    • Molecular physiology of cardiac repolarization
    • DOI 10.1152/physrev.00002.2005
    • Nerbonne JM, Kass RS. Molecular physiology of cardiac repolarization. Physiol Rev. 2005;85:1205-1253. (Pubitemid 41362269)
    • (2005) Physiological Reviews , vol.85 , Issue.4 , pp. 1205-1253
    • Nerbonne, J.M.1    Kass, R.S.2
  • 124
    • 0037127028 scopus 로고    scopus 로고
    • Requirement of a macromolecular signaling complex for β adrenergic receptor modulation of the KCNQ1-KCNE1 potassium channel
    • DOI 10.1126/science.1066843
    • Marx SO, Kurokawa J, Reiken S, et al. Requirement of a macromolecular signaling complex for beta adrenergic receptor modulation of the KCNQ1-KCNE1 potassium channel. Science. 2002;295: 496-499. (Pubitemid 34101639)
    • (2002) Science , vol.295 , Issue.5554 , pp. 496-499
    • Marx, S.O.1    Kurokawa, J.2    Reiken, S.3    Motoike, H.4    D'Armiento, J.5    Marks, A.R.6    Kass, R.S.7
  • 125
    • 2442657712 scopus 로고    scopus 로고
    • Four potassium channel mutations account for 73% of the genetic spectrum underlying long-QT syndrome (LQTS) and provide evidence for a strong founder effect in Finland
    • DOI 10.1080/17431380410032689
    • Fodstad H, Swan H, Laitinen P, et al. Four potassium channel mutations account for 73% of the genetic spectrum underlying long-QT syndrome (LQTS) and provide evidence for a strong founder effect in Finland. Ann Med. 2004;36(suppl 1):53-63. (Pubitemid 38669925)
    • (2004) Annals of Medicine , vol.36 , Issue.SUPPL. 1 , pp. 53-63
    • Fodstad, H.1    Swan, H.2    Laitinen, P.3    Piippo, K.4    Paavonen, K.5    Viitasalo, M.6    Toivonen, L.7    Kontula, K.8
  • 126
    • 66149127296 scopus 로고    scopus 로고
    • The cardiac IKs potassium channel macromolecular complex includes the phosphodiesterase PDE4D3
    • Terrenoire C, Houslay MD, Baillie GS, et al. The cardiac IKs potassium channel macromolecular complex includes the phosphodiesterase PDE4D3. J Biol Chem. 2009;284:9140-9146.
    • (2009) J Biol Chem , vol.284 , pp. 9140-9146
    • Terrenoire, C.1    Houslay, M.D.2    Baillie, G.S.3
  • 127
    • 24744442589 scopus 로고    scopus 로고
    • Phosphorylation of the A-kinase-anchoring protein Yotiao contributes to protein kinase A regulation of a heart potassium channel
    • DOI 10.1074/jbc.M505191200
    • Chen L, Kurokawa J, Kass RS. Phosphorylation of the A-kinaseanchoring protein Yotiao contributes to protein kinase A regulation of a heart potassium channel. J Biol Chem. 2005;280:31347-31352. (Pubitemid 41291874)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.36 , pp. 31347-31352
    • Chen, L.1    Kurokawa, J.2    Kass, R.S.3
  • 128
    • 33744998729 scopus 로고    scopus 로고
    • Dual roles of the A kinase-anchoring protein Yotiao in the modulation of a cardiac potassium channel: A passive adaptor versus an active regulator
    • DOI 10.1016/j.ejcb.2006.03.002, PII S0171933506000550
    • Chen L, Kass RS. Dual roles of the A kinase-anchoring protein Yotiao in the modulation of a cardiac potassium channel: a passive adaptor versus an active regulator. Eur J Cell Biol. 2006;85:623-626. (Pubitemid 43863038)
    • (2006) European Journal of Cell Biology , vol.85 , Issue.7 , pp. 623-626
    • Chen, L.1    Kass, R.S.2
  • 130
    • 0035933817 scopus 로고    scopus 로고
    • Phosphodiesterase 4D and protein kinase a type II constitute a signaling unit in the centrosomal area
    • Tasken KA, Collas P, Kemmner WA, et al. Phosphodiesterase 4D and protein kinase a type II constitute a signaling unit in the centrosomal area. J Biol Chem. 2001;276:21999-22002.
    • (2001) J Biol Chem , vol.276 , pp. 21999-22002
    • Tasken, K.A.1    Collas, P.2    Kemmner, W.A.3
  • 131
    • 73249127861 scopus 로고    scopus 로고
    • Differential regulation of adipocyte PDE3B in distinct membrane compartments by insulin and the beta3- adrenergic receptor agonist CL316243: Effects of caveolin-1 knockdown on formation/maintenance of macromolecular signalling complexes
    • Ahmad F, Lindh R, Tang Y, et al. Differential regulation of adipocyte PDE3B in distinct membrane compartments by insulin and the beta3- adrenergic receptor agonist CL316243: effects of caveolin-1 knockdown on formation/maintenance of macromolecular signalling complexes. Biochem J. 2009;424:399-410.
    • (2009) Biochem J , vol.424 , pp. 399-410
    • Ahmad, F.1    Lindh, R.2    Tang, Y.3
  • 134
    • 0034705543 scopus 로고    scopus 로고
    • 2- adrenergic receptor desensitization and resensitization
    • DOI 10.1074/jbc.275.25.19025
    • Lin F, Wang H, Malbon CC. Gravin-mediated formation of signaling complexes in beta 2-adrenergic receptor desensitization and resensitization. J Biol Chem. 2000;275:19025-19034. (Pubitemid 30422869)
    • (2000) Journal of Biological Chemistry , vol.275 , Issue.25 , pp. 19025-19034
    • Lin, F.1    Wang, H.-Y.2    Malbon, C.C.3
  • 135
    • 0035911149 scopus 로고    scopus 로고
    • Of yeast, mice, and men: Rab proteins and organelle transport
    • Deacon SW, Gelfand VI. Of yeast, mice, and men: rab proteins and organelle transport. J Cell Biol. 2001;152:F21-F24.
    • (2001) J Cell Biol , vol.152
    • Deacon, S.W.1    Gelfand, V.I.2
  • 136
    • 0032699082 scopus 로고    scopus 로고
    • Phosphodiesterase 4 (PDE4) inhibitors in asthma and chronic obstructive pulmonary disease (COPD)
    • Barnette MS. Phosphodiesterase 4 (PDE4) inhibitors in asthma and chronic obstructive pulmonary disease (COPD). Prog Drug Res. 1999; 53:193-229. (Pubitemid 29515642)
    • (1999) Progress in Drug Research , vol.53 , pp. 193-229
    • Barnette, M.S.1
  • 137
    • 0033043309 scopus 로고    scopus 로고
    • Emesis induced by inhibitors of type IV cyclic nucleotide phosphodiesterase (PDE IV) in the ferret
    • DOI 10.1016/S0028-3908(98)00190-7, PII S0028390898001907
    • Robichaud A, Tattersall FD, Choudhury I, et al. Emesis induced by inhibitors of type IV cyclic nucleotide phosphodiesterase (PDE IV) in the ferret. Neuropharmacology. 1999;38:289-297. (Pubitemid 29073550)
    • (1999) Neuropharmacology , vol.38 , Issue.2 , pp. 289-297
    • Robichaud, A.1    Tattersall, F.D.2    Choudhury, I.3    Rodger, I.W.4
  • 138
    • 0026072848 scopus 로고
    • Effect of oral milrinone on mortality in severe chronic heart failure
    • The PROMISE Study Research Group
    • Packer M, Carver JR, Rodeheffer RJ, et al. Effect of oral milrinone on mortality in severe chronic heart failure. The PROMISE Study Research Group. N Engl J Med. 1991;325:1468-1475.
    • (1991) N Engl J Med , vol.325 , pp. 1468-1475
    • Packer, M.1    Carver, J.R.2    Rodeheffer, R.J.3


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