메뉴 건너뛰기




Volumn 31, Issue 6, 2006, Pages 316-323

The where's and when's of kinase anchoring

Author keywords

[No Author keywords available]

Indexed keywords

CYCLIC AMP; CYCLIC AMP DEPENDENT PROTEIN KINASE; CYCLIC AMP DEPENDENT PROTEIN KINASE ANCHORING PROTEIN; PHOSPHODIESTERASE;

EID: 33745181698     PISSN: 09680004     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.tibs.2006.04.009     Document Type: Review
Times cited : (124)

References (77)
  • 1
    • 0000187410 scopus 로고
    • Conversion of phosphorylase b to phosphorylase a in muscle extracts
    • Fischer E.H., and Krebs E.G. Conversion of phosphorylase b to phosphorylase a in muscle extracts. J. Biol. Chem. 216 (1955) 121-132
    • (1955) J. Biol. Chem. , vol.216 , pp. 121-132
    • Fischer, E.H.1    Krebs, E.G.2
  • 2
    • 70449285205 scopus 로고
    • Factors affecting the activity of muscle phosphorylase b kinase
    • Krebs E.G., et al. Factors affecting the activity of muscle phosphorylase b kinase. J. Biol. Chem. 234 (1959) 2867-2873
    • (1959) J. Biol. Chem. , vol.234 , pp. 2867-2873
    • Krebs, E.G.1
  • 3
    • 0018580807 scopus 로고
    • An activity phosphorylating tyrosine in polyoma T antigen immunoprecipitates
    • Eckhart W., et al. An activity phosphorylating tyrosine in polyoma T antigen immunoprecipitates. Cell 18 (1979) 925-933
    • (1979) Cell , vol.18 , pp. 925-933
    • Eckhart, W.1
  • 4
    • 0018403188 scopus 로고
    • Detection of the viral sarcoma gene product in cells infected with various strains of avian sarcoma virus and of a related protein in uninfected chicken cells
    • Brugge J.S., et al. Detection of the viral sarcoma gene product in cells infected with various strains of avian sarcoma virus and of a related protein in uninfected chicken cells. J. Virol. 29 (1979) 1196-1203
    • (1979) J. Virol. , vol.29 , pp. 1196-1203
    • Brugge, J.S.1
  • 5
    • 0022977712 scopus 로고
    • A non-catalytic domain conserved among cytoplasmic protein-tyrosine kinases modifies the kinase function and transforming activity of Fujinami sarcoma virus P130gag-fps
    • Sadowski I., et al. A non-catalytic domain conserved among cytoplasmic protein-tyrosine kinases modifies the kinase function and transforming activity of Fujinami sarcoma virus P130gag-fps. Mol. Cell. Biol. 6 (1986) 4396-4408
    • (1986) Mol. Cell. Biol. , vol.6 , pp. 4396-4408
    • Sadowski, I.1
  • 6
    • 0026326821 scopus 로고
    • Structure of a peptide inhibitor bound to the catalytic subunit of cyclic adenosine monophosphate-dependent protein kinase
    • Knighton D.R., et al. Structure of a peptide inhibitor bound to the catalytic subunit of cyclic adenosine monophosphate-dependent protein kinase. Science 253 (1991) 414-420
    • (1991) Science , vol.253 , pp. 414-420
    • Knighton, D.R.1
  • 7
    • 0037032835 scopus 로고    scopus 로고
    • The protein kinase complement of the human genome
    • Manning G., et al. The protein kinase complement of the human genome. Science 298 (2002) 1912-1934
    • (2002) Science , vol.298 , pp. 1912-1934
    • Manning, G.1
  • 8
    • 0021023294 scopus 로고
    • Compartments of cyclic AMP and protein kinase in mammalian cardiomyocytes
    • Buxton I.L.O., and Brunton L.L. Compartments of cyclic AMP and protein kinase in mammalian cardiomyocytes. J. Biol. Chem. 258 (1983) 10233-10239
    • (1983) J. Biol. Chem. , vol.258 , pp. 10233-10239
    • Buxton, I.L.O.1    Brunton, L.L.2
  • 9
    • 0020490408 scopus 로고
    • Molecular characterization of the cAMP-dependent protein kinase bound to microtubule-associated protein 2
    • Theurkauf W.E., and Vallee R.B. Molecular characterization of the cAMP-dependent protein kinase bound to microtubule-associated protein 2. J. Biol. Chem. 257 (1982) 3284-3290
    • (1982) J. Biol. Chem. , vol.257 , pp. 3284-3290
    • Theurkauf, W.E.1    Vallee, R.B.2
  • 10
    • 0344201997 scopus 로고
    • High-affinity binding of the regulatory subunit (RII) of cAMP-dependent protein kinase to microtubule-associated and other cellular proteins
    • Lohmann S.M., et al. High-affinity binding of the regulatory subunit (RII) of cAMP-dependent protein kinase to microtubule-associated and other cellular proteins. Proc. Natl. Acad. Sci. U. S. A. 81 (1984) 6723-6727
    • (1984) Proc. Natl. Acad. Sci. U. S. A. , vol.81 , pp. 6723-6727
    • Lohmann, S.M.1
  • 11
    • 0023018797 scopus 로고
    • Differential binding of the regulatory subunits (RII) of cAMP-dependent protein kinase II from bovine brain and muscle to RII-binding proteins
    • Leiser M., et al. Differential binding of the regulatory subunits (RII) of cAMP-dependent protein kinase II from bovine brain and muscle to RII-binding proteins. J. Biol. Chem. 261 (1986) 1904-1908
    • (1986) J. Biol. Chem. , vol.261 , pp. 1904-1908
    • Leiser, M.1
  • 12
    • 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 D.B., et al. 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. 264 (1989) 4648-4656
    • (1989) J. Biol. Chem. , vol.264 , pp. 4648-4656
    • Bregman, D.B.1
  • 13
    • 0025606328 scopus 로고
    • Type II regulatory subunit dimerization determines the subcellular localization of the cAMP-dependent protein kinase
    • Scott J.D., et al. Type II regulatory subunit dimerization determines the subcellular localization of the cAMP-dependent protein kinase. J. Biol. Chem. 265 (1990) 21561-21566
    • (1990) J. Biol. Chem. , vol.265 , pp. 21561-21566
    • Scott, J.D.1
  • 14
    • 0026348474 scopus 로고
    • Interaction of the regulatory subunit (RII) of cAMP-dependent protein kinase with RII-anchoring proteins occurs through an amphipathic helix binding motif
    • Carr D.W., et al. Interaction of the regulatory subunit (RII) of cAMP-dependent protein kinase with RII-anchoring proteins occurs through an amphipathic helix binding motif. J. Biol. Chem. 266 (1991) 14188-14192
    • (1991) J. Biol. Chem. , vol.266 , pp. 14188-14192
    • Carr, D.W.1
  • 15
    • 0026770492 scopus 로고
    • Blotting and band-shifting: techniques for studying protein-protein interactions
    • Carr D.W., and Scott J.D. Blotting and band-shifting: techniques for studying protein-protein interactions. Trends Biochem. Sci. 17 (1992) 246-249
    • (1992) Trends Biochem. Sci. , vol.17 , pp. 246-249
    • Carr, D.W.1    Scott, J.D.2
  • 16
    • 0026795614 scopus 로고
    • Localization of the cAMP-dependent protein kinase to the postsynaptic densities by A-kinase anchoring proteins: characterization of AKAP79
    • Carr D.W., et al. Localization of the cAMP-dependent protein kinase to the postsynaptic densities by A-kinase anchoring proteins: characterization of AKAP79. J. Biol. Chem. 267 (1992) 16816-16823
    • (1992) J. Biol. Chem. , vol.267 , pp. 16816-16823
    • Carr, D.W.1
  • 17
    • 0026680801 scopus 로고
    • Association of the type II cAMP-dependent protein kinase with a human thyroid RII-anchoring protein. Cloning and characterization of the RII-binding domain
    • Carr D.W., et al. Association of the type II cAMP-dependent protein kinase with a human thyroid RII-anchoring protein. Cloning and characterization of the RII-binding domain. J. Biol. Chem. 267 (1992) 13376-13382
    • (1992) J. Biol. Chem. , vol.267 , pp. 13376-13382
    • Carr, D.W.1
  • 18
    • 0028274544 scopus 로고
    • Anchoring of protein kinase A is required for modulation of AMPA/kainate receptors on hippocampal neurons
    • Rosenmund C., et al. Anchoring of protein kinase A is required for modulation of AMPA/kainate receptors on hippocampal neurons. Nature 368 (1994) 853-856
    • (1994) Nature , vol.368 , pp. 853-856
    • Rosenmund, C.1
  • 19
    • 0028127059 scopus 로고
    • 2+ channels in skeletal muscle cells requires anchored cAMP-dependent protein kinase
    • 2+ channels in skeletal muscle cells requires anchored cAMP-dependent protein kinase. Proc. Natl. Acad. Sci. U. S. A. 91 (1994) 11492-11496
    • (1994) Proc. Natl. Acad. Sci. U. S. A. , vol.91 , pp. 11492-11496
    • Johnson, B.D.1
  • 20
    • 0031040893 scopus 로고    scopus 로고
    • Protein kinase A-anchoring inhibitor peptides arrest mammalian sperm motility
    • Vijayaraghavan S., et al. Protein kinase A-anchoring inhibitor peptides arrest mammalian sperm motility. J. Biol. Chem. 272 (1997) 4747-4752
    • (1997) J. Biol. Chem. , vol.272 , pp. 4747-4752
    • Vijayaraghavan, S.1
  • 21
    • 0037386547 scopus 로고    scopus 로고
    • Designing isoform-specific peptide disruptors of protein kinase A localization
    • Burns-Hamuro L.L., et al. Designing isoform-specific peptide disruptors of protein kinase A localization. Proc. Natl. Acad. Sci. U. S. A. 100 (2003) 4072-4077
    • (2003) Proc. Natl. Acad. Sci. U. S. A. , vol.100 , pp. 4072-4077
    • Burns-Hamuro, L.L.1
  • 22
    • 0037447227 scopus 로고    scopus 로고
    • Bioinformatic design of A-kinase anchoring protein-in silico: a potent and selective peptide antagonist of type II protein kinase A anchoring
    • Alto N.M., et al. Bioinformatic design of A-kinase anchoring protein-in silico: a potent and selective peptide antagonist of type II protein kinase A anchoring. Proc. Natl. Acad. Sci. U. S. A. 100 (2003) 4445-4450
    • (2003) Proc. Natl. Acad. Sci. U. S. A. , vol.100 , pp. 4445-4450
    • Alto, N.M.1
  • 23
    • 0032972739 scopus 로고    scopus 로고
    • The molecular basis for protein kinase A anchoring revealed by solution NMR
    • Newlon M.G., et al. The molecular basis for protein kinase A anchoring revealed by solution NMR. Nat. Struct. Biol. 6 (1999) 222-227
    • (1999) Nat. Struct. Biol. , vol.6 , pp. 222-227
    • Newlon, M.G.1
  • 24
    • 0035794551 scopus 로고    scopus 로고
    • A novel mechanism of PKA anchoring revealed by solution structures of anchoring complexes
    • Newlon M.G., et al. A novel mechanism of PKA anchoring revealed by solution structures of anchoring complexes. EMBO J. 20 (2001) 1651-1662
    • (2001) EMBO J. , vol.20 , pp. 1651-1662
    • Newlon, M.G.1
  • 25
    • 0030903895 scopus 로고    scopus 로고
    • Identification of a novel dual specificity protein kinase A anchoring protein, D-AKAP1
    • Huang L.J., et al. Identification of a novel dual specificity protein kinase A anchoring protein, D-AKAP1. J. Biol. Chem. 272 (1997) 8057-8064
    • (1997) J. Biol. Chem. , vol.272 , pp. 8057-8064
    • Huang, L.J.1
  • 26
    • 0030881687 scopus 로고    scopus 로고
    • D-AKAP2, a novel protein kinase A anchoring protein with a putative RGS domain
    • Huang L.J., et al. D-AKAP2, a novel protein kinase A anchoring protein with a putative RGS domain. Proc. Natl. Acad. Sci. U. S. A. 94 (1997) 11184-11189
    • (1997) Proc. Natl. Acad. Sci. U. S. A. , vol.94 , pp. 11184-11189
    • Huang, L.J.1
  • 27
    • 0347359224 scopus 로고    scopus 로고
    • Localized effects of cAMP mediated by distinct routes of protein kinase A
    • Tasken K., and Aandahl E.M. Localized effects of cAMP mediated by distinct routes of protein kinase A. Physiol. Rev. 84 (2004) 137-167
    • (2004) Physiol. Rev. , vol.84 , pp. 137-167
    • Tasken, K.1    Aandahl, E.M.2
  • 28
    • 0028943777 scopus 로고
    • Association of protein kinase A and protein phosphatase 2B with a common anchoring protein
    • Coghlan V.M., et al. Association of protein kinase A and protein phosphatase 2B with a common anchoring protein. Science 267 (1995) 108-112
    • (1995) Science , vol.267 , pp. 108-112
    • Coghlan, V.M.1
  • 29
    • 0029887701 scopus 로고    scopus 로고
    • Coordination of three signaling enzymes by AKAP79, a mammalian scaffold protein
    • Klauck T.M., et al. Coordination of three signaling enzymes by AKAP79, a mammalian scaffold protein. Science 271 (1996) 1589-1592
    • (1996) Science , vol.271 , pp. 1589-1592
    • Klauck, T.M.1
  • 30
    • 0031018767 scopus 로고    scopus 로고
    • Gravin, an autoantigen recognized by serum from myasthenia gravis patients, is a kinase scaffold protein
    • Nauert J.B., et al. Gravin, an autoantigen recognized by serum from myasthenia gravis patients, is a kinase scaffold protein. Curr. Biol. 7 (1997) 52-62
    • (1997) Curr. Biol. , vol.7 , pp. 52-62
    • Nauert, J.B.1
  • 31
    • 4344642877 scopus 로고    scopus 로고
    • AKAP-Lbc nucleates a protein kinase D activation scaffold
    • Carnegie G.K., et al. AKAP-Lbc nucleates a protein kinase D activation scaffold. Mol. Cell 15 (2004) 889-899
    • (2004) Mol. Cell , vol.15 , pp. 889-899
    • Carnegie, G.K.1
  • 32
    • 0033602449 scopus 로고    scopus 로고
    • Association of the type 1 protein phosphatase PP1 with the A-kinase anchoring protein AKAP220
    • Schillace R.V., and Scott J.D. Association of the type 1 protein phosphatase PP1 with the A-kinase anchoring protein AKAP220. Curr. Biol. 9 (1999) 321-324
    • (1999) Curr. Biol. , vol.9 , pp. 321-324
    • Schillace, R.V.1    Scott, J.D.2
  • 33
    • 0034683658 scopus 로고    scopus 로고
    • Recruitment of protein phosphatase 1 to the nuclear envelope by A-kinase anchoring protein AKAP149 is a prerequisite for nuclear lamina assembly
    • Steen R.L., et al. Recruitment of protein phosphatase 1 to the nuclear envelope by A-kinase anchoring protein AKAP149 is a prerequisite for nuclear lamina assembly. J. Cell Biol. 150 (2000) 1251-1262
    • (2000) J. Cell Biol. , vol.150 , pp. 1251-1262
    • Steen, R.L.1
  • 34
    • 0037443097 scopus 로고    scopus 로고
    • PDE4 cAMP phosphodiesterases: modular enzymes that orchestrate signalling cross-talk, desensitization and compartmentalization
    • Houslay M.D., and Adams D.R. PDE4 cAMP phosphodiesterases: modular enzymes that orchestrate signalling cross-talk, desensitization and compartmentalization. Biochem. J. 370 (2003) 1-18
    • (2003) Biochem. J. , vol.370 , pp. 1-18
    • Houslay, M.D.1    Adams, D.R.2
  • 35
    • 0033591233 scopus 로고    scopus 로고
    • The RACK1 signaling scaffold protein selectively interacts with the cAMP-specific phosphodiesterase PDE4D5 isoform
    • Yarwood S.J., et al. The RACK1 signaling scaffold protein selectively interacts with the cAMP-specific phosphodiesterase PDE4D5 isoform. J. Biol. Chem. 274 (1999) 14909-14917
    • (1999) J. Biol. Chem. , vol.274 , pp. 14909-14917
    • Yarwood, S.J.1
  • 36
    • 0037174646 scopus 로고    scopus 로고
    • Targeting of cyclic AMP degradation to β2-adrenergic receptors by β-arrestins
    • Perry S.J., et al. Targeting of cyclic AMP degradation to β2-adrenergic receptors by β-arrestins. Science 298 (2002) 834-836
    • (2002) Science , vol.298 , pp. 834-836
    • Perry, S.J.1
  • 37
    • 0035815666 scopus 로고    scopus 로고
    • Myomegalin is a novel protein of the Golgi/centrosome that interacts with a cyclic nucleotide phosphodiesterase
    • Verde I., et al. Myomegalin is a novel protein of the Golgi/centrosome that interacts with a cyclic nucleotide phosphodiesterase. J. Biol. Chem. 276 (2001) 11189-11198
    • (2001) J. Biol. Chem. , vol.276 , pp. 11189-11198
    • Verde, I.1
  • 38
    • 0035901502 scopus 로고    scopus 로고
    • mAKAP assembles a protein kinase A/PDE4 phosphodiesterase cAMP signaling module
    • Dodge K.L., et al. mAKAP assembles a protein kinase A/PDE4 phosphodiesterase cAMP signaling module. EMBO J. 20 (2001) 1921-1930
    • (2001) EMBO J. , vol.20 , pp. 1921-1930
    • Dodge, K.L.1
  • 39
    • 20444412702 scopus 로고    scopus 로고
    • Compartmentalisation of phosphodiesterases and protein kinase A: opposites attract
    • Baillie G.S., et al. Compartmentalisation of phosphodiesterases and protein kinase A: opposites attract. FEBS Lett. 579 (2005) 3264-3270
    • (2005) FEBS Lett. , vol.579 , pp. 3264-3270
    • Baillie, G.S.1
  • 40
    • 4344594414 scopus 로고    scopus 로고
    • PKA phosphorylation of PDE4D3 facilitates recruitment of the mAKAP signaling complex
    • Carlisle Michel J.J., et al. PKA phosphorylation of PDE4D3 facilitates recruitment of the mAKAP signaling complex. Biochem. J. 381 (2004) 587-592
    • (2004) Biochem. J. , vol.381 , pp. 587-592
    • Carlisle Michel, J.J.1
  • 41
    • 0030006920 scopus 로고    scopus 로고
    • Phosphorylation and activation of a cAMP-specific phosphodiesterase by the cAMP-dependent protein kinase
    • Sette C., and Conti M. Phosphorylation and activation of a cAMP-specific phosphodiesterase by the cAMP-dependent protein kinase. J. Biol. Chem. 271 (1996) 16526-16534
    • (1996) J. Biol. Chem. , vol.271 , pp. 16526-16534
    • Sette, C.1    Conti, M.2
  • 42
    • 0033558010 scopus 로고    scopus 로고
    • The MAP kinase ERK2 inhibits the cyclic AMP-specific phosphodiesterase HSPDE4D3 by phosphorylating it at Ser579
    • Hoffmann R., et al. The MAP kinase ERK2 inhibits the cyclic AMP-specific phosphodiesterase HSPDE4D3 by phosphorylating it at Ser579. EMBO J. 18 (1999) 893-903
    • (1999) EMBO J. , vol.18 , pp. 893-903
    • Hoffmann, R.1
  • 43
    • 25644452031 scopus 로고    scopus 로고
    • The protein kinase A anchoring protein mAKAP coordinates two integrated cAMP effector pathways
    • Dodge-Kafka K.L., et al. The protein kinase A anchoring protein mAKAP coordinates two integrated cAMP effector pathways. Nature 437 (2005) 574-578
    • (2005) Nature , vol.437 , pp. 574-578
    • Dodge-Kafka, K.L.1
  • 44
    • 28444443387 scopus 로고    scopus 로고
    • Spatial restriction of PDK1 activation cascades by anchoring to mAKAPα
    • Michel J.J., et al. Spatial restriction of PDK1 activation cascades by anchoring to mAKAPα. Mol. Cell 20 (2005) 661-672
    • (2005) Mol. Cell , vol.20 , pp. 661-672
    • Michel, J.J.1
  • 45
    • 0035933817 scopus 로고    scopus 로고
    • Phosphodiesterase 4D and protein kinase a type II constitute a signaling unit in the centrosomal area
    • Tasken K.A., et al. Phosphodiesterase 4D and protein kinase a type II constitute a signaling unit in the centrosomal area. J. Biol. Chem. 276 (2001) 21999-22002
    • (2001) J. Biol. Chem. , vol.276 , pp. 21999-22002
    • Tasken, K.A.1
  • 46
    • 6344221448 scopus 로고    scopus 로고
    • A-kinase anchoring proteins interact with phosphodiesterases in T lymphocyte cell lines
    • Asirvatham A.L., et al. A-kinase anchoring proteins interact with phosphodiesterases in T lymphocyte cell lines. J. Immunol. 173 (2004) 4806-4814
    • (2004) J. Immunol. , vol.173 , pp. 4806-4814
    • Asirvatham, A.L.1
  • 47
    • 30344469932 scopus 로고    scopus 로고
    • AKAP3 selectively binds PDE4A isoforms in bovine spermatozoa
    • Bajpai M., et al. AKAP3 selectively binds PDE4A isoforms in bovine spermatozoa. Biol. Reprod. 74 (2006) 109-118
    • (2006) Biol. Reprod. , vol.74 , pp. 109-118
    • Bajpai, M.1
  • 48
    • 0027730774 scopus 로고
    • A-kinase anchoring proteins: a key to selective activation of cAMP-responsive events?
    • Coghlan V.M., et al. A-kinase anchoring proteins: a key to selective activation of cAMP-responsive events?. Mol. Cell. Biochem. 127 (1993) 309-319
    • (1993) Mol. Cell. Biochem. , vol.127 , pp. 309-319
    • Coghlan, V.M.1
  • 49
    • 0033516701 scopus 로고    scopus 로고
    • Regulation of NMDA receptors by an associated phosphatase-kinase signaling complex
    • Westphal R.S., et al. Regulation of NMDA receptors by an associated phosphatase-kinase signaling complex. Science 285 (1999) 93-96
    • (1999) Science , vol.285 , pp. 93-96
    • Westphal, R.S.1
  • 50
    • 85047689493 scopus 로고    scopus 로고
    • Long QT syndrome: novel insights into the mechanisms of cardiac arrhythmias
    • Kass R.S., and Moss A.J. Long QT syndrome: novel insights into the mechanisms of cardiac arrhythmias. J. Clin. Invest. 112 (2003) 810-815
    • (2003) J. Clin. Invest. , vol.112 , pp. 810-815
    • Kass, R.S.1    Moss, A.J.2
  • 51
    • 0037127028 scopus 로고    scopus 로고
    • Requirement of a macromolecular signaling complex for β adrenergic receptor modulation of the KCNQ1-KCNE1 potassium channel
    • Marx S.O., et al. Requirement of a macromolecular signaling complex for β adrenergic receptor modulation of the KCNQ1-KCNE1 potassium channel. Science 295 (2002) 496-499
    • (2002) Science , vol.295 , pp. 496-499
    • Marx, S.O.1
  • 52
    • 24744442589 scopus 로고    scopus 로고
    • Phosphorylation of the A-kinase-anchoring protein Yotiao contributes to protein kinase A regulation of a heart potassium channel
    • Chen L., et al. Phosphorylation of the A-kinase-anchoring protein Yotiao contributes to protein kinase A regulation of a heart potassium channel. J. Biol. Chem. 280 (2005) 31347-31352
    • (2005) J. Biol. Chem. , vol.280 , pp. 31347-31352
    • Chen, L.1
  • 53
    • 0033554893 scopus 로고    scopus 로고
    • Dynamic complexes of β2-adrenergic receptors with protein kinases and phosphatases and the role of gravin
    • Shih M., et al. Dynamic complexes of β2-adrenergic receptors with protein kinases and phosphatases and the role of gravin. J. Biol. Chem. 274 (1999) 1588-1595
    • (1999) J. Biol. Chem. , vol.274 , pp. 1588-1595
    • Shih, M.1
  • 54
    • 0346993722 scopus 로고    scopus 로고
    • Protein kinase A regulates AKAP250 (gravin) scaffold binding to the β2-adrenergic receptor
    • Tao J., et al. Protein kinase A regulates AKAP250 (gravin) scaffold binding to the β2-adrenergic receptor. EMBO J. 22 (2003) 6419-6429
    • (2003) EMBO J. , vol.22 , pp. 6419-6429
    • Tao, J.1
  • 55
    • 0035941212 scopus 로고    scopus 로고
    • AKAP-Lbc anchors protein kinase A and nucleates Gα12-selective Rho-mediated stress fiber formation
    • Diviani D., et al. AKAP-Lbc anchors protein kinase A and nucleates Gα12-selective Rho-mediated stress fiber formation. J. Biol. Chem. 276 (2001) 44247-44257
    • (2001) J. Biol. Chem. , vol.276 , pp. 44247-44257
    • Diviani, D.1
  • 56
    • 0035798219 scopus 로고    scopus 로고
    • Ht31: the first protein kinase A anchoring protein to integrate protein kinase A and Rho signaling
    • Klussmann E., et al. Ht31: the first protein kinase A anchoring protein to integrate protein kinase A and Rho signaling. FEBS Lett. 507 (2001) 264-268
    • (2001) FEBS Lett. , vol.507 , pp. 264-268
    • Klussmann, E.1
  • 57
    • 3543020962 scopus 로고    scopus 로고
    • Anchoring of both PKA and 14-3-3 inhibits the Rho-GEF activity of the AKAP-Lbc signaling complex
    • Diviani D., et al. Anchoring of both PKA and 14-3-3 inhibits the Rho-GEF activity of the AKAP-Lbc signaling complex. EMBO J. 23 (2004) 2811-2820
    • (2004) EMBO J. , vol.23 , pp. 2811-2820
    • Diviani, D.1
  • 58
    • 4344598183 scopus 로고    scopus 로고
    • Proteomic, functional, and domain-based analysis of in vivo 14-3-3 binding proteins involved in cytoskeletal regulation and cellular organization
    • Jin J., et al. Proteomic, functional, and domain-based analysis of in vivo 14-3-3 binding proteins involved in cytoskeletal regulation and cellular organization. Curr. Biol. 14 (2004) 1436-1450
    • (2004) Curr. Biol. , vol.14 , pp. 1436-1450
    • Jin, J.1
  • 59
    • 33644827808 scopus 로고    scopus 로고
    • Distinct enzyme combinations in AKAP signalling complexes permit functional diversity
    • Hoshi N., et al. Distinct enzyme combinations in AKAP signalling complexes permit functional diversity. Nat. Cell Biol. 7 (2005) 1066-1073
    • (2005) Nat. Cell Biol. , vol.7 , pp. 1066-1073
    • Hoshi, N.1
  • 60
    • 0034001787 scopus 로고    scopus 로고
    • Control of GluR1 AMPA receptor function by cAMP-dependent protein kinase
    • Banke T.G., et al. Control of GluR1 AMPA receptor function by cAMP-dependent protein kinase. J. Neurosci. 20 (2000) 89-102
    • (2000) J. Neurosci. , vol.20 , pp. 89-102
    • Banke, T.G.1
  • 61
    • 0037092436 scopus 로고    scopus 로고
    • Regulation of GluR1 by the A-kinase anchoring protein 79 (AKAP79) signaling complex shares properties with long-term depression
    • Tavalin S.J., et al. Regulation of GluR1 by the A-kinase anchoring protein 79 (AKAP79) signaling complex shares properties with long-term depression. J. Neurosci. 22 (2002) 3044-3051
    • (2002) J. Neurosci. , vol.22 , pp. 3044-3051
    • Tavalin, S.J.1
  • 62
    • 0034611757 scopus 로고    scopus 로고
    • 2-adrenergic receptor complex facilitates receptor phosphorylation and signaling
    • 2-adrenergic receptor complex facilitates receptor phosphorylation and signaling. Curr. Biol. 10 (2000) 409-412
    • (2000) Curr. Biol. , vol.10 , pp. 409-412
    • Fraser, I.D.1
  • 63
    • 0035805528 scopus 로고    scopus 로고
    • Regulation of membrane targeting of the G protein-coupled receptor kinase 2 by protein kinase A and its anchoring protein AKAP79
    • Cong M., et al. Regulation of membrane targeting of the G protein-coupled receptor kinase 2 by protein kinase A and its anchoring protein AKAP79. J. Biol. Chem. 276 (2001) 15192-15199
    • (2001) J. Biol. Chem. , vol.276 , pp. 15192-15199
    • Cong, M.1
  • 64
    • 23944494162 scopus 로고    scopus 로고
    • RNA silencing identifies PDE4D5 as the functionally relevant cAMP phosphodiesterase interacting with β arrestin to control the protein kinase A/AKAP79-mediated switching of the β2-adrenergic receptor to activation of ERK in HEK293B2 cells
    • Lynch M.J., et al. RNA silencing identifies PDE4D5 as the functionally relevant cAMP phosphodiesterase interacting with β arrestin to control the protein kinase A/AKAP79-mediated switching of the β2-adrenergic receptor to activation of ERK in HEK293B2 cells. J. Biol. Chem. 280 (2005) 33178-33189
    • (2005) J. Biol. Chem. , vol.280 , pp. 33178-33189
    • Lynch, M.J.1
  • 65
    • 33644818937 scopus 로고    scopus 로고
    • A-kinase anchoring proteins: different partners, different dance
    • Chen L., and Kass R.S. A-kinase anchoring proteins: different partners, different dance. Nat. Cell Biol. 7 (2005) 1050-1051
    • (2005) Nat. Cell Biol. , vol.7 , pp. 1050-1051
    • Chen, L.1    Kass, R.S.2
  • 66
    • 0035858868 scopus 로고    scopus 로고
    • Phosphorylation-dependent regulation of ryanodine receptors: a novel role for leucine/isoleucine zippers
    • Marx S.O., et al. Phosphorylation-dependent regulation of ryanodine receptors: a novel role for leucine/isoleucine zippers. J. Cell Biol. 153 (2001) 699-708
    • (2001) J. Cell Biol. , vol.153 , pp. 699-708
    • Marx, S.O.1
  • 67
    • 26244467287 scopus 로고    scopus 로고
    • Phosphodiesterase 4D deficiency in the ryanodine-receptor complex promotes heart failure and arrhythmias
    • Lehnart S.E., et al. Phosphodiesterase 4D deficiency in the ryanodine-receptor complex promotes heart failure and arrhythmias. Cell 123 (2005) 25-35
    • (2005) Cell , vol.123 , pp. 25-35
    • Lehnart, S.E.1
  • 68
    • 0026029895 scopus 로고
    • Fluorescence ratio imaging of cyclic AMP in single cells
    • Adams S.R., et al. Fluorescence ratio imaging of cyclic AMP in single cells. Nature 349 (1991) 694-697
    • (1991) Nature , vol.349 , pp. 694-697
    • Adams, S.R.1
  • 69
    • 0036500494 scopus 로고    scopus 로고
    • Discrete microdomains with high concentration of cAMP in stimulated rat neonatal cardiac myocytes
    • Zaccolo M., and Pozzan T. Discrete microdomains with high concentration of cAMP in stimulated rat neonatal cardiac myocytes. Science 295 (2002) 1711-1715
    • (2002) Science , vol.295 , pp. 1711-1715
    • Zaccolo, M.1    Pozzan, T.2
  • 70
    • 3142723295 scopus 로고    scopus 로고
    • Fluorescence resonance energy transfer-based analysis of cAMP dynamics in live neonatal rat cardiac myocytes reveals distinct functions of compartmentalized phosphodiesterases
    • Mongillo M., et al. Fluorescence resonance energy transfer-based analysis of cAMP dynamics in live neonatal rat cardiac myocytes reveals distinct functions of compartmentalized phosphodiesterases. Circ. Res. 95 (2004) 67-75
    • (2004) Circ. Res. , vol.95 , pp. 67-75
    • Mongillo, M.1
  • 71
    • 0033617447 scopus 로고    scopus 로고
    • 2+-inhibitable adenylyl cyclase in C6-2B glioma cells
    • 2+-inhibitable adenylyl cyclase in C6-2B glioma cells. J. Biol. Chem. 274 (1999) 12445-12453
    • (1999) J. Biol. Chem. , vol.274 , pp. 12445-12453
    • Fagan, K.A.1
  • 72
    • 0033895842 scopus 로고    scopus 로고
    • Cyclic nucleotide-gated channels colocalize with adenylyl cyclase in regions of restricted cAMP diffusion
    • Rich T.C., et al. Cyclic nucleotide-gated channels colocalize with adenylyl cyclase in regions of restricted cAMP diffusion. J. Gen. Physiol. 116 (2000) 147-161
    • (2000) J. Gen. Physiol. , vol.116 , pp. 147-161
    • Rich, T.C.1
  • 73
    • 0034942107 scopus 로고    scopus 로고
    • In vivo assessment of local phosphodiesterase activity using tailored cyclic nucleotide-gated channels as cAMP sensors
    • Rich T.C., et al. In vivo assessment of local phosphodiesterase activity using tailored cyclic nucleotide-gated channels as cAMP sensors. J. Gen. Physiol. 118 (2001) 63-78
    • (2001) J. Gen. Physiol. , vol.118 , pp. 63-78
    • Rich, T.C.1
  • 74
    • 4444377903 scopus 로고    scopus 로고
    • Novel single chain cAMP sensors for receptor-induced signal propagation
    • Nikolaev V.O., et al. Novel single chain cAMP sensors for receptor-induced signal propagation. J. Biol. Chem. 279 (2004) 37215-37218
    • (2004) J. Biol. Chem. , vol.279 , pp. 37215-37218
    • Nikolaev, V.O.1
  • 75
    • 9344220483 scopus 로고    scopus 로고
    • Fluorescent indicators of cAMP and Epac activation reveal differential dynamics of cAMP signaling within discrete subcellular compartments
    • DiPilato L.M., et al. Fluorescent indicators of cAMP and Epac activation reveal differential dynamics of cAMP signaling within discrete subcellular compartments. Proc. Natl Acad. Sci. U. S. A. 101 (2004) 16513-16518
    • (2004) Proc. Natl Acad. Sci. U. S. A. , vol.101 , pp. 16513-16518
    • DiPilato, L.M.1
  • 76
    • 25644446102 scopus 로고    scopus 로고
    • Insulin disrupts β-adrenergic signalling to protein kinase A in adipocytes
    • Zhang J., et al. Insulin disrupts β-adrenergic signalling to protein kinase A in adipocytes. Nature 437 (2005) 569-573
    • (2005) Nature , vol.437 , pp. 569-573
    • Zhang, J.1
  • 77
    • 0035910074 scopus 로고    scopus 로고
    • Genetically encoded reporters of protein kinase A activity reveal impact of substrate tethering
    • Zhang J., et al. Genetically encoded reporters of protein kinase A activity reveal impact of substrate tethering. Proc. Natl Acad. Sci. U. S. A. 98 (2001) 14997-15002
    • (2001) Proc. Natl Acad. Sci. U. S. A. , vol.98 , pp. 14997-15002
    • Zhang, J.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.