메뉴 건너뛰기




Volumn 5, Issue 12, 2004, Pages 959-970

AKAP signalling complexes: Focal points in space and time

Author keywords

[No Author keywords available]

Indexed keywords

CYCLIC AMP DEPENDENT PROTEIN KINASE ANCHORING PROTEIN; HORMONE; NEUROTRANSMITTER; PHOSPHATASE; PROTEIN KINASE;

EID: 10044253425     PISSN: 14710072     EISSN: None     Source Type: Journal    
DOI: 10.1038/nrm1527     Document Type: Review
Times cited : (895)

References (130)
  • 1
    • 0001559662 scopus 로고
    • Fractionation and characterization of a cyclic adenine ribonucleotide formed by tissue particles
    • Sutherland, E. W. & Rall, T. W. Fractionation and characterization of a cyclic adenine ribonucleotide formed by tissue particles. J. Biol. Chem. 232, 1077-1091 (1958).
    • (1958) J. Biol. Chem. , vol.232 , pp. 1077-1091
    • Sutherland, E.W.1    Rall, T.W.2
  • 2
    • 0014524874 scopus 로고
    • Adenyl cyclase and hormone action. I. Effects of adrenocorticotropic hormone, glucagon, and epinephrine on the plasma membrane of rat fat cells
    • Bar, H. P. & Hechter, O. Adenyl cyclase and hormone action. I. Effects of adrenocorticotropic hormone, glucagon, and epinephrine on the plasma membrane of rat fat cells. Proc. Natl Acad. Sci. USA 63, 350-356 (1969).
    • (1969) Proc. Natl. Acad. Sci. USA , vol.63 , pp. 350-356
    • Bar, H.P.1    Hechter, O.2
  • 4
    • 0023769896 scopus 로고
    • From epinephrine to cyclic AMP
    • Levitzki, A. From epinephrine to cyclic AMP. Science 241, 800-806 (1988).
    • (1988) Science , vol.241 , pp. 800-806
    • Levitzki, A.1
  • 5
    • 0028218758 scopus 로고
    • 3 and cAMP as long-range and associative messengers
    • 3 and cAMP as long-range and associative messengers. Trends Neurosci. 17, 95-101 (1994).
    • (1994) Trends Neurosci. , vol.17 , pp. 95-101
    • Kasai, H.1    Petersen, O.H.2
  • 6
    • 0025181717 scopus 로고
    • Immunocytology on microwave-fixed cells reveals rapid and agonist-specific changes in subcellular accumulation patterns for cAMP or cGMP
    • Barsony, J. & Marks, S. J. Immunocytology on microwave-fixed cells reveals rapid and agonist-specific changes in subcellular accumulation patterns for cAMP or cGMP. Proc. Natl Acad. Sci. USA 87, 1188-1192 (1990).
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 1188-1192
    • Barsony, J.1    Marks, S.J.2
  • 7
    • 0027246341 scopus 로고
    • Spatially resolved dynamics of cAMP and protein kinase A subunits in Aplysia sensory neurons
    • Bacskai, B. J. et al. Spatially resolved dynamics of cAMP and protein kinase A subunits in Aplysia sensory neurons. Science 260, 222-226 (1993).
    • (1993) Science , vol.260 , pp. 222-226
    • Bacskai, B.J.1
  • 8
    • 0036500494 scopus 로고    scopus 로고
    • Discrete microdomains with high concentration of cAMP in stimulated rat neonatal cardiac myocytes
    • Zaccolo, M. & Pozzan, T. Discrete microdomains with high concentration of cAMP in stimulated rat neonatal cardiac myocytes. Science 295, 1711-1715 (2002). An elegant study to visualize cAMP dynamics in primary mammalian cells using physiologically relevant stimuli in real time.
    • (2002) Science , vol.295 , pp. 1711-1715
    • Zaccolo, M.1    Pozzan, T.2
  • 9
    • 0036301043 scopus 로고    scopus 로고
    • Cyclic nucleotide-gated ion channels
    • Kaupp, U. B. & Seifert, R. Cyclic nucleotide-gated ion channels. Physiol. Rev. 82, 769-824 (2002).
    • (2002) Physiol. Rev. , vol.82 , pp. 769-824
    • Kaupp, U.B.1    Seifert, R.2
  • 10
    • 0037443097 scopus 로고    scopus 로고
    • PDE4 cAMP phosphodiesterases: Modular enzymes that orchestrate signalling cross-talk, desensitization and compartmentalization
    • Houslay, M. D. & Adams, D. R. PDE4 cAMP phosphodiesterases: modular enzymes that orchestrate signalling cross-talk, desensitization and compartmentalization. Biochem. J. 370, 1-18 (2003).
    • (2003) Biochem. J. , vol.370 , pp. 1-18
    • Houslay, M.D.1    Adams, D.R.2
  • 11
    • 0041836339 scopus 로고    scopus 로고
    • Epac: A new cAMP target and new avenues in cAMP research
    • Bos, J. L. Epac: a new cAMP target and new avenues in cAMP research. Nature Rev. Mol. Cell Biol. 4, 733-738 (2003).
    • (2003) Nature Rev. Mol. Cell Biol. , vol.4 , pp. 733-738
    • Bos, J.L.1
  • 12
    • 0014409394 scopus 로고
    • An adenosine 3′,5′-monophosphate-dependent protein kinase from rabbit skeletal muscle
    • Walsh, D. A., Perkins, J. P. & Krebs, E. G. An adenosine 3′,5′-monophosphate-dependent protein kinase from rabbit skeletal muscle. J. Biol. Chem. 243, 3763-3765 (1968).
    • (1968) J. Biol. Chem. , vol.243 , pp. 3763-3765
    • Walsh, D.A.1    Perkins, J.P.2    Krebs, E.G.3
  • 13
    • 0015919341 scopus 로고
    • Regulation of adenosine 3′,5′-monophosphate-dependent protein kinase
    • Corbin, J. D., Soderling, T. R. & Park, C. R. Regulation of adenosine 3′,5′-monophosphate-dependent protein kinase. J. Biol. Chem. 248, 1813-1821 (1973).
    • (1973) J. Biol. Chem. , vol.248 , pp. 1813-1821
    • Corbin, J.D.1    Soderling, T.R.2    Park, C.R.3
  • 14
    • 0017369531 scopus 로고
    • Characterization and regulation of heart adenosine 3′:5′- monophosphate-dependent protein kinase isozymes
    • Corbin, J. D. & Keely, S. L. Characterization and regulation of heart adenosine 3′:5′-monophosphate-dependent protein kinase isozymes. J. Biol. Chem. 252, 910-918 (1977).
    • (1977) J. Biol. Chem. , vol.252 , pp. 910-918
    • Corbin, J.D.1    Keely, S.L.2
  • 15
    • 0018786508 scopus 로고
    • Relationships between structural domains and function in the regulatory subunit of cAMP-dependent protein kinases I and II from porcine skeletal muscle
    • Potter, R. L. & Taylor, S. S. Relationships between structural domains and function in the regulatory subunit of cAMP-dependent protein kinases I and II from porcine skeletal muscle. J. Biol. Chem. 254, 2413-2418 (1979).
    • (1979) J. Biol. Chem. , vol.254 , pp. 2413-2418
    • Potter, R.L.1    Taylor, S.S.2
  • 16
    • 0020770086 scopus 로고
    • Isolation of cDNA clone for the type I regulatory subunit of bovine cAMP-dependent protein kinase
    • Lee, D. C., Carmichael, D. F., Krebs, E. G. & McKnight, G. S. Isolation of cDNA clone for the type I regulatory subunit of bovine cAMP-dependent protein kinase. Proc. Natl Acad. Sci. USA 80, 3608-3612 (1983).
    • (1983) Proc. Natl. Acad. Sci. USA , vol.80 , pp. 3608-3612
    • Lee, D.C.1    Carmichael, D.F.2    Krebs, E.G.3    McKnight, G.S.4
  • 17
    • 0023388024 scopus 로고
    • The molecular cloning of a type II regulatory subunit of the cAMP-dependent protein kinase from rat skeletal muscle and mouse brain
    • Scott, J. D. et al. The molecular cloning of a type II regulatory subunit of the cAMP-dependent protein kinase from rat skeletal muscle and mouse brain. Proc. Natl Acad. Sci. USA 84, 5192-5196 (1987).
    • (1987) Proc. Natl. Acad. Sci. USA , vol.84 , pp. 5192-5196
    • Scott, J.D.1
  • 18
    • 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. 285, 21561-21566 (1990).
    • (1990) J. Biol. Chem. , vol.285 , pp. 21561-21566
    • Scott, J.D.1
  • 19
    • 0038001261 scopus 로고    scopus 로고
    • A-kinase anchoring proteins and neuronal signaling mechanisms
    • Carnegie, G. K. & Scott, J. D. A-kinase anchoring proteins and neuronal signaling mechanisms. Genes Dev. 17, 1557-1568 (2003).
    • (2003) Genes Dev. , vol.17 , pp. 1557-1568
    • Carnegie, G.K.1    Scott, J.D.2
  • 20
    • 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., De Camilli, P., Einig, I. & Walter, U. High-affinity binding of the regulatory subunit (RII) of cAMP-dependent protein kinase to microtubule-associated and other cellular proteins. Proc. Natl Acad. Sci. USA 81, 6723-6727 (1984). Introduction of the RII overlay procedure, a widely used in vitro assay used to discover novel AKAPs.
    • (1984) Proc. Natl. Acad. Sci. USA , vol.81 , pp. 6723-6727
    • Lohmann, S.M.1    De Camilli, P.2    Einig, I.3    Walter, U.4
  • 21
    • 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
    • Can, 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, 14188-14192 (1991). Identified an amphipathic helical structure as the key determinant for RII binding.
    • (1991) J. Biol. Chem. , vol.266 , pp. 14188-14192
    • Can, D.W.1
  • 22
    • 0030861621 scopus 로고    scopus 로고
    • The A-kinase anchoring domain of type IIα cAMP-dependent protein kinase is highly helical
    • Newton, M. G., Roy, M., Hausken, Z. E., Scott, J. D. & Jennings, P. A. The A-kinase anchoring domain of type IIα cAMP-dependent protein kinase is highly helical. J. Biol. Chem. 272, 23637-23644 (1997).
    • (1997) J. Biol. Chem. , vol.272 , pp. 23637-23644
    • Newton, M.G.1    Roy, M.2    Hausken, Z.E.3    Scott, J.D.4    Jennings, P.A.5
  • 23
    • 0035794551 scopus 로고    scopus 로고
    • A novel mechanism of PKA anchoring revealed by solution structures of anchoring complexes
    • Newton, M. G. et al. A novel mechanism of PKA anchoring revealed by solution structures of anchoring complexes. EMBO J. 20, 1651-1662 (2001).
    • (2001) EMBO J. , vol.20 , pp. 1651-1662
    • Newton, M.G.1
  • 24
    • 0032972739 scopus 로고    scopus 로고
    • The molecular basis for protein kinase A anchoring revealed by solution NMR
    • Newton, M. G. et al. The molecular basis for protein kinase A anchoring revealed by solution NMR. Nature Struct. Biol. 6, 222-227 (1999).
    • (1999) Nature Struct. Biol. , vol.6 , pp. 222-227
    • Newton, M.G.1
  • 25
    • 0032486376 scopus 로고    scopus 로고
    • CE) of type I protein kinase A from Caenorhabditis elegans
    • CE) of type I protein kinase A from Caenorhabditis elegans. J. Biol. Chem. 273, 14633-14643 (1998).
    • (1998) J. Biol. Chem. , vol.273 , pp. 14633-14643
    • Angelo, R.1    Rubin, C.S.2
  • 26
    • 0030903895 scopus 로고    scopus 로고
    • Identification of a novel dual specificity protein kinase A anchoring protein, D-AKAP1
    • Huang, L. J., Durick, K., Weiner, J. A., Chun, J. & Taylor, S. S. Identification of a novel dual specificity protein kinase A anchoring protein, D-AKAP1. J. Biol. Chem. 272, 8057-8064 (1997).
    • (1997) J. Biol. Chem. , vol.272 , pp. 8057-8064
    • Huang, L.J.1    Durick, K.2    Weiner, J.A.3    Chun, J.4    Taylor, S.S.5
  • 27
    • 0035853041 scopus 로고    scopus 로고
    • Cloning and mitochondrial localization of full-length D-AKAP2, a protein kinase A anchoring protein
    • Wang, L. et al. Cloning and mitochondrial localization of full-length D-AKAP2, a protein kinase A anchoring protein. Proc. Natl Acad. Sci. USA 98, 3220-3225 (2001).
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 3220-3225
    • Wang, L.1
  • 28
    • 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., Hausken, Z. E., Fraser, I. D., Stofko-Hahn, R. E. & Scott, J. D. 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, 13376-13382 (1992).
    • (1992) J. Biol. Chem. , vol.267 , pp. 13376-13382
    • Carr, D.W.1    Hausken, Z.E.2    Fraser, I.D.3    Stofko-Hahn, R.E.4    Scott, J.D.5
  • 29
    • 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. USA 100, 4445-4450 (2003).
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 4445-4450
    • Alto, N.M.1
  • 30
    • 0037386547 scopus 로고    scopus 로고
    • Designing isoform-specific peptide disruptors of proten kinase A localization
    • Burns-Hamuro, L. L. et al. Designing isoform-specific peptide disruptors of proten kinase A localization. Proc. Natl Acad. Sci. USA 100, 4072-4077 (2003). References 29 and 30 show that it is possible to design peptides that selectively disrupt R-subunit-AKAP interactions.
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 4072-4077
    • Burns-Hamuro, L.L.1
  • 31
    • 0032522719 scopus 로고    scopus 로고
    • Membrane-targeting sequences on AKAP79 bind phosphatidylinositol-4,5- bisphosphate
    • Dell'Acqua, M. L., Faux, M. C., Thorburn, J., Thorburn, A. & Scott, J. D. Membrane-targeting sequences on AKAP79 bind phosphatidylinositol-4,5- bisphosphate. EMBO J. 17, 2246-2260 (1998).
    • (1998) EMBO J. , vol.17 , pp. 2246-2260
    • Dell'Acqua, M.L.1    Faux, M.C.2    Thorburn, J.3    Thorburn, A.4    Scott, J.D.5
  • 32
    • 1842866233 scopus 로고    scopus 로고
    • AKAPs (A-kinase anchoring proteins) and molecules that compose their G-protein-coupled receptor signaling complexes
    • Malbon, C. C., Tao, J. & Wang, H. Y. AKAPs (A-kinase anchoring proteins) and molecules that compose their G-protein-coupled receptor signaling complexes. Biochem. J. 379, 1-9 (2004).
    • (2004) Biochem. J. , vol.379 , pp. 1-9
    • Malbon, C.C.1    Tao, J.2    Wang, H.Y.3
  • 33
    • 0033611168 scopus 로고    scopus 로고
    • Alternative splicing regulates the subcellular localization of A-kinase anchoring protein 18 isoforms
    • Trotter, K. W. et al. Alternative splicing regulates the subcellular localization of A-kinase anchoring protein 18 isoforms. J. Cell Biol. 147, 1481-1492 (1999).
    • (1999) J. Cell Biol. , vol.147 , pp. 1481-1492
    • Trotter, K.W.1
  • 34
    • 0033620489 scopus 로고    scopus 로고
    • 2-terminal targeting motifs direct dual specificity A-kinase-anchoring protein 1 (D-AKAP1) to either mitochondria or endoplasmic reticulum
    • 2-terminal targeting motifs direct dual specificity A-kinase-anchoring protein 1 (D-AKAP1) to either mitochondria or endoplasmic reticulum. J. Cell Biol. 145, 951-959 (1999).
    • (1999) J. Cell Biol. , vol.145 , pp. 951-959
    • Huang, L.J.1
  • 35
    • 0037135975 scopus 로고    scopus 로고
    • Rab32 is an A-kinase anchoring protein and participates in mitochondrial dynamics
    • Alto, N. M., Soderling, J. & Scott, J. D. Rab32 is an A-kinase anchoring protein and participates in mitochondrial dynamics. J. Cell Biol. 158, 659-668 (2002).
    • (2002) J. Cell Biol. , vol.158 , pp. 659-668
    • Alto, N.M.1    Soderling, J.2    Scott, J.D.3
  • 36
    • 0041357164 scopus 로고    scopus 로고
    • BAD and glucokinase reside in a mitochondrial complex that integrates glycolysis and apoptosis
    • Danial, N. N. et al. BAD and glucokinase reside in a mitochondrial complex that integrates glycolysis and apoptosis. Nature 424, 952-956 (2003).
    • (2003) Nature , vol.424 , pp. 952-956
    • Danial, N.N.1
  • 37
    • 0034611693 scopus 로고    scopus 로고
    • Pericentrin anchors protein kinase A at the centrosome through a newly identified RII-binding domain
    • Diviani, D., Langeberg, L. K., Doxsey, S. J. & Scott, J. D. Pericentrin anchors protein kinase A at the centrosome through a newly identified RII-binding domain. Curr. Biol. 10, 417-420 (2000).
    • (2000) Curr. Biol. , vol.10 , pp. 417-420
    • Diviani, D.1    Langeberg, L.K.2    Doxsey, S.J.3    Scott, J.D.4
  • 38
    • 0034574615 scopus 로고    scopus 로고
    • The PACT domain, a conserved centrosomal targeting motif in the coiled-coil proteins AKAP450 and pericentrin
    • Gillingham, A. K. & Munro, S. The PACT domain, a conserved centrosomal targeting motif in the coiled-coil proteins AKAP450 and pericentrin. EMBO Rep. 1, 524-529 (2000).
    • (2000) EMBO Rep. , vol.1 , pp. 524-529
    • Gillingham, A.K.1    Munro, S.2
  • 39
    • 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, 93-96 (1999).
    • (1999) Science , vol.285 , pp. 93-96
    • Westphal, R.S.1
  • 40
    • 0033613941 scopus 로고    scopus 로고
    • AKAP350: A multiply spliced A-kinase anchoring protein associated wih centrosomes
    • Schmidt, R. H. et al. AKAP350: a multiply spliced A-kinase anchoring protein associated wih centrosomes. J. Biol. Chem. 274, 3055-3066 (1999).
    • (1999) J. Biol. Chem. , vol.274 , pp. 3055-3066
    • Schmidt, R.H.1
  • 41
    • 0345435932 scopus 로고    scopus 로고
    • Cloning and characterization of a cDNA encoding an A-kinase anchoring protein located in the centrosome, AKAP450
    • Witczak, O. et al. Cloning and characterization of a cDNA encoding an A-kinase anchoring protein located in the centrosome, AKAP450. EMBO J. 18, 1858-1868 (1999).
    • (1999) EMBO J. , vol.18 , pp. 1858-1868
    • Witczak, O.1
  • 42
    • 2642705036 scopus 로고    scopus 로고
    • A novel lipid-anchored A-kinase anchoring protein facilitates cAMP-responsive membrane events
    • Fraser, I. D. et al. A novel lipid-anchored A-kinase anchoring protein facilitates cAMP-responsive membrane events. EMBO J. 17, 2261-2272 (1998).
    • (1998) EMBO J. , vol.17 , pp. 2261-2272
    • Fraser, I.D.1
  • 43
    • 0025912302 scopus 로고
    • Molecular characterization of bovine brain P75, a high affinity binding protein for the regulatory subunit of cAMP-dependent protein kinase IIβ
    • Bregman, D. B., Hirsch, A. H. & Rubin, C. S. Molecular characterization of bovine brain P75, a high affinity binding protein for the regulatory subunit of cAMP-dependent protein kinase IIβ. J. Biol. Chem. 266, 7207-7213 (1991).
    • (1991) J. Biol. Chem. , vol.266 , pp. 7207-7213
    • Bregman, D.B.1    Hirsch, A.H.2    Rubin, C.S.3
  • 44
    • 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., Stofko-Hahn, R. E., Fraser, I. D. C., Cone, R. D. & Scott, J. D. Localization of the cAMP-dependent protein kinase to the postsynaptic densities by A-kinase anchoring proteins: characterization of AKAP79. J. Biol. Chem. 24, 16816-16823 (1992).
    • (1992) J. Biol. Chem. , vol.24 , pp. 16816-16823
    • Carr, D.W.1    Stofko-Hahn, R.E.2    Fraser, I.D.C.3    Cone, R.D.4    Scott, J.D.5
  • 45
    • 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, 108-112 (1995).
    • (1995) Science , vol.267 , pp. 108-112
    • Coghlan, V.M.1
  • 46
    • 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, 1589-1592 (1996). The first demonstration of a multivalent AKAP complex - in particular, one that contains a signalling molecule from a distinct pathway (PKC) and a signal-termination enzyme.
    • (1996) Science , vol.271 , pp. 1589-1592
    • Klauck, T.M.1
  • 47
    • 0002830450 scopus 로고    scopus 로고
    • Molecular glue: Kinase anchoring and scaffold proteins
    • Faux, M. C. & Scott, J. D. Molecular glue: kinase anchoring and scaffold proteins. Cell 70, 8-12 (1996).
    • (1996) Cell , vol.70 , pp. 8-12
    • Faux, M.C.1    Scott, J.D.2
  • 48
    • 0033569659 scopus 로고    scopus 로고
    • Mechanism of A-kinase-anchoring protein 79 (AKAP79) and protein kinase C interaction
    • Faux, M. C. et al. Mechanism of A-kinase-anchoring protein 79 (AKAP79) and protein kinase C interaction. Biochem. J. 343, 443-452 (1999).
    • (1999) Biochem. J. , vol.343 , pp. 443-452
    • Faux, M.C.1
  • 49
    • 0033166454 scopus 로고    scopus 로고
    • Modulation of ion channels: A 'current' view of AKAPs
    • Fraser, I. D. & Scott, J. D. Modulation of ion channels: a 'current' view of AKAPs. Neuron 23, 423-426 (1999).
    • (1999) Neuron , vol.23 , pp. 423-426
    • Fraser, I.D.1    Scott, J.D.2
  • 50
    • 0030760304 scopus 로고    scopus 로고
    • 2+ channels requires membrane targeting of PKA and phosphorylation of channel subunits
    • 2+ channels requires membrane targeting of PKA and phosphorylation of channel subunits. Neuron 19, 185-196 (1997).
    • (1997) Neuron , vol.19 , pp. 185-196
    • Gao, T.1
  • 51
    • 0035203604 scopus 로고    scopus 로고
    • AQP2 is a substrate for endogenous PP2B activity within an inner medullary AKAP-signalling complex
    • Jo, I., et al. AQP2 is a substrate for endogenous PP2B activity within an inner medullary AKAP-signalling complex. Am. J. Physiol. Renal Physiol. 281, F958-F965 (2001).
    • (2001) Am. J. Physiol. Renal Physiol. , vol.281
    • Jo, I.1
  • 53
    • 0031018767 scopus 로고    scopus 로고
    • Gravin, an autoantigen recognized by serum from myasthenia gravis patients, is a kinase scaffold protein
    • Nauert, J. B., Klauck, T. M., Langeberg, L. K. & Scott, J. D. Gravin, an autoantigen recognized by serum from myasthenia gravis patients, is a kinase scaffold protein. Curr. Biol. 7, 52-62 (1997).
    • (1997) Curr. Biol. , vol.7 , pp. 52-62
    • Nauert, J.B.1    Klauck, T.M.2    Langeberg, L.K.3    Scott, J.D.4
  • 54
    • 0033546152 scopus 로고    scopus 로고
    • Characterization of a novel giant scaffolding protein, CG-NAP, that anchors multiple signaling enzymes to centrosome and the Golgi apparatus
    • Takahashi, M. et al. Characterization of a novel giant scaffolding protein, CG-NAP, that anchors multiple signaling enzymes to centrosome and the Golgi apparatus. J. Biol. Chem. 274, 17267-17274 (1999).
    • (1999) J. Biol. Chem. , vol.274 , pp. 17267-17274
    • Takahashi, M.1
  • 55
    • 0034602398 scopus 로고    scopus 로고
    • Association of immature hypo-phosphorylated protein kinase Cε with an anchoring protein CG-NAP
    • Takahashi, M., Mukai, H., Oishi, K., Isagawa, T. & Ono, Y. Association of immature hypo-phosphorylated protein kinase Cε with an anchoring protein CG-NAP. J. Biol. Chem. 275, 34592-34596 (2000).
    • (2000) J. Biol. Chem. , vol.275 , pp. 34592-34596
    • Takahashi, M.1    Mukai, H.2    Oishi, K.3    Isagawa, T.4    Ono, Y.5
  • 56
    • 0036387280 scopus 로고    scopus 로고
    • Centrosomal anchoring of the protein kinase CK1δ mediated by attachment to the large, coiled-coil scaffolding protein CG-NAP/AKAP450
    • Sillibourne, J. E., Milne, D. M., Takahashi, M., Ono, Y. & Meek, D. W. Centrosomal anchoring of the protein kinase CK1δ mediated by attachment to the large, coiled-coil scaffolding protein CG-NAP/AKAP450. J. Mol. Biol. 322, 785-797 (2002).
    • (2002) J. Mol. Biol. , vol.322 , pp. 785-797
    • Sillibourne, J.E.1    Milne, D.M.2    Takahashi, M.3    Ono, Y.4    Meek, D.W.5
  • 57
    • 0033602449 scopus 로고    scopus 로고
    • Association of the type 1 protein phosphatase PP1 with the A-kinase anchoring protein AKAP220
    • Schillace, R. V. & Scott, J. D. Association of the type 1 protein phosphatase PP1 with the A-kinase anchoring protein AKAP220. Curr. Biol. 9, 321-324 (1999).
    • (1999) Curr. Biol. , vol.9 , pp. 321-324
    • Schillace, R.V.1    Scott, J.D.2
  • 58
    • 0037020072 scopus 로고    scopus 로고
    • A-kinase anchoring protein AKAP220 binds to glycogen synthase kinase-3β (GSK-3β) and mediates protein kinase A-dependent inhibition of GSK-3β
    • Tanji, C. et al. A-kinase anchoring protein AKAP220 binds to glycogen synthase kinase-3β (GSK-3β) and mediates protein kinase A-dependent inhibition of GSK-3β. J. Biol. Chem. 277, 36955-36961 (2002).
    • (2002) J. Biol. Chem. , vol.277 , pp. 36955-36961
    • Tanji, C.1
  • 59
    • 0032403083 scopus 로고    scopus 로고
    • WAVE a novel WASP-family protein involved in actin reorganization induced by Rac
    • Miki, H., Suetsugu, S. & Takenawa, T. WAVE, a novel WASP-family protein involved in actin reorganization induced by Rac. EMBO J. 17, 6932-6941 (1998).
    • (1998) EMBO J. , vol.17 , pp. 6932-6941
    • Miki, H.1    Suetsugu, S.2    Takenawa, T.3
  • 60
    • 0034282711 scopus 로고    scopus 로고
    • Scar/WAVE-1, a Wiskott-Aldrich syndrome protein, assembles an actin-associated multi-kinase scaffold
    • Westphal, R. S., Soderling, S. H., Alto, N. M., Langeberg, L. K. & Scott, J. D. Scar/WAVE-1, a Wiskott-Aldrich syndrome protein, assembles an actin-associated multi-kinase scaffold. EMBO J. 19, 4589-4600 (2000).
    • (2000) EMBO J. , vol.19 , pp. 4589-4600
    • Westphal, R.S.1    Soderling, S.H.2    Alto, N.M.3    Langeberg, L.K.4    Scott, J.D.5
  • 61
    • 0036903024 scopus 로고    scopus 로고
    • The WRP component of the WAVE-1 complex attenuates Rac-mediated signalling
    • Soderling, S. H. et al. The WRP component of the WAVE-1 complex attenuates Rac-mediated signalling. Nature Cell Biol. 4, 970-975 (2002).
    • (2002) Nature Cell Biol. , vol.4 , pp. 970-975
    • Soderling, S.H.1
  • 62
    • 0032585538 scopus 로고    scopus 로고
    • Scar1 and the related Wiskott-Aldrich syndrome protein, WASP, regulate the actin cytoskeleton through the Arp2/3 complex
    • Machesky, L. M. & Insall, R. H. Scar1 and the related Wiskott-Aldrich syndrome protein, WASP, regulate the actin cytoskeleton through the Arp2/3 complex. Curr. Biol. 8, 1347-1356 (1998).
    • (1998) Curr. Biol. , vol.8 , pp. 1347-1356
    • Machesky, L.M.1    Insall, R.H.2
  • 64
    • 0033554893 scopus 로고    scopus 로고
    • Dynamic complexes of β2-adrenergic receptors with protein kinases and phosphatases and the role of gravin
    • Shih, M., Lin, F., Scott, J. D., Wang, H. Y. & Malbon, C. C. Dynamic complexes of β2-adrenergic receptors with protein kinases and phosphatases and the role of gravin. J. Biol. Chem. 274, 1588-1595 (1999).
    • (1999) J. Biol. Chem. , vol.274 , pp. 1588-1595
    • Shih, M.1    Lin, F.2    Scott, J.D.3    Wang, H.Y.4    Malbon, C.C.5
  • 65
    • 0346993722 scopus 로고    scopus 로고
    • Protein kinase A regulates AKAP250 (gravin) scaffold binding to the β2-adrenergic receptor
    • Tao, J., Wang, H. Y. & Malbon, C. C. Protein kinase A regulates AKAP250 (gravin) scaffold binding to the β2-adrenergic receptor. EMBO J. 22, 6419-6429 (2003).
    • (2003) EMBO J. , vol.22 , pp. 6419-6429
    • Tao, J.1    Wang, H.Y.2    Malbon, C.C.3
  • 66
    • 0037102301 scopus 로고    scopus 로고
    • Mechanism of regulation of WAVE1-induced actin nucleation by Rac1 and Nck
    • Eden, S., Rohatgi, R., Podtelejnikov, A. V., Mann, M. & Kirschner, M. W. Mechanism of regulation of WAVE1-induced actin nucleation by Rac1 and Nck. Nature 418, 790-793 (2002).
    • (2002) Nature , vol.418 , pp. 790-793
    • Eden, S.1    Rohatgi, R.2    Podtelejnikov, A.V.3    Mann, M.4    Kirschner, M.W.5
  • 67
    • 2342483041 scopus 로고    scopus 로고
    • Abl1 is essential for the formation and activation of a WAVE2 signalling complex
    • Innocenti, M. et al. Abl1 is essential for the formation and activation of a WAVE2 signalling complex. Nature Cell Biol. 6, 319-327 (2004).
    • (2004) Nature Cell Biol. , vol.6 , pp. 319-327
    • Innocenti, M.1
  • 68
    • 0037452615 scopus 로고    scopus 로고
    • Loss of WAVE-1 causes sensorimotor retardation and reduced learning and memory in mice
    • Soderling, S. H. et al. Loss of WAVE-1 causes sensorimotor retardation and reduced learning and memory in mice. Proc. Natl Acad. Sci. USA 100, 1723-1728 (2003). One of the first published reports on an AKAP-null mouse model, the phenotype of which implies that the WAVE1 scaffold is crucial for the development and function of the central nervous system.
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 1723-1728
    • Soderling, S.H.1
  • 69
    • 0033120591 scopus 로고    scopus 로고
    • Phosphorylation and inactivation of BAD by mitochondria-anchored protein kinase A
    • Harada, H. et al. Phosphorylation and inactivation of BAD by mitochondria-anchored protein kinase A. Mol. Cell 3, 413-422 (1999).
    • (1999) Mol. Cell , vol.3 , pp. 413-422
    • Harada, H.1
  • 70
    • 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, 496-499 (2002).
    • (2002) Science , vol.295 , pp. 496-499
    • Marx, S.O.1
  • 71
    • 2442531859 scopus 로고    scopus 로고
    • Association of type 1 inositol 1,4,5-trisphosphate receptor with AKAP9 (Yotiao) and protein kinase A
    • Tu, H., Tang, T. S., Wang, Z. & Bezprozvanny, I. Association of type 1 inositol 1,4,5-trisphosphate receptor with AKAP9 (Yotiao) and protein kinase A. J. Biol. Chem. 279, 19375-19382 (2004).
    • (2004) J. Biol. Chem. , vol.279 , pp. 19375-19382
    • Tu, H.1    Tang, T.S.2    Wang, Z.3    Bezprozvanny, I.4
  • 72
    • 0037174869 scopus 로고    scopus 로고
    • AKAP350 at the Golgi apparatus. I. Identification of a distinct Golgi apparatus targeting motif in AKAP350
    • Shanks, R. A., Steadman, B. T., Schmidt, P. H. & Goldenring, J. R. AKAP350 at the Golgi apparatus. I. Identification of a distinct Golgi apparatus targeting motif in AKAP350. J. Biol. Chem. 277, 40967-40972 (2002).
    • (2002) J. Biol. Chem. , vol.277 , pp. 40967-40972
    • Shanks, R.A.1    Steadman, B.T.2    Schmidt, P.H.3    Goldenring, J.R.4
  • 73
    • 0037174956 scopus 로고    scopus 로고
    • AKAP350 at the Golgi apparatus. II. Association of AKAP350 with a novel chloride intracellular channel (CLIC) family member
    • Shanks, R. A. et al. AKAP350 at the Golgi apparatus. II. Association of AKAP350 with a novel chloride intracellular channel (CLIC) family member. J. Biol. Chem. 277, 40973-40980 (2002).
    • (2002) J. Biol. Chem. , vol.277 , pp. 40973-40980
    • Shanks, R.A.1
  • 74
    • 0036736094 scopus 로고    scopus 로고
    • Centrosomal proteins CG-NAP and kendrin provide microtubule nucleation sites by anchoring γ-tubulin ring complex
    • Takahashi, M., Yamagiwa, A., Nishimura, T., Mukai, H. & Ono, Y. Centrosomal proteins CG-NAP and kendrin provide microtubule nucleation sites by anchoring γ-tubulin ring complex. Mol. Biol. Cell 13, 3235-3245 (2002).
    • (2002) Mol. Biol. Cell , vol.13 , pp. 3235-3245
    • Takahashi, M.1    Yamagiwa, A.2    Nishimura, T.3    Mukai, H.4    Ono, Y.5
  • 75
    • 0026418306 scopus 로고
    • Enhancement of glutamate response by cAMP-dependent protein kinase in hippocampal neurons
    • Greengard, P., Jen, J., Nairn, A. C. & Stevens, C. F. Enhancement of glutamate response by cAMP-dependent protein kinase in hippocampal neurons. Science 253, 1135-1138 (1991).
    • (1991) Science , vol.253 , pp. 1135-1138
    • Greengard, P.1    Jen, J.2    Nairn, A.C.3    Stevens, C.F.4
  • 76
    • 0026873542 scopus 로고
    • Synaptic excitation mediated by glutamate-gated ion channels
    • Jahr, C. E. & Lester, R. A. J. Synaptic excitation mediated by glutamate-gated ion channels. Curr. Opin. Neurobiol. 2, 395-400 (1992).
    • (1992) Curr. Opin. Neurobiol. , vol.2 , pp. 395-400
    • Jahr, C.E.1    Lester, R.A.J.2
  • 77
    • 0033671742 scopus 로고    scopus 로고
    • Targeting of PKA to glutamate receptors through a MAGUK-AKAP complex
    • Colledge, M. et al. Targeting of PKA to glutamate receptors through a MAGUK-AKAP complex. Neuron 27, 107-119 (2000). Describes the molecular mechanism by which AKAP79/150-anchored PKA can modulate NMDA and AMPA receptors.
    • (2000) Neuron , vol.27 , pp. 107-119
    • Colledge, M.1
  • 78
    • 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, 3044-3051 (2002).
    • (2002) J. Neurosci. , vol.22 , pp. 3044-3051
    • Tavalin, S.J.1
  • 79
    • 0032215153 scopus 로고    scopus 로고
    • Involvement of a postsynaptic protein kinase A substrate in the expression of homosynaptic long-term depression
    • Kameyama, K., Lee, H. K., Bear, M. F. & Huganir, R. L. Involvement of a postsynaptic protein kinase A substrate in the expression of homosynaptic long-term depression. Neuron 21, 1163-1175 (1998).
    • (1998) Neuron , vol.21 , pp. 1163-1175
    • Kameyama, K.1    Lee, H.K.2    Bear, M.F.3    Huganir, R.L.4
  • 80
    • 0034702259 scopus 로고    scopus 로고
    • Regulation of distinct AMPA receptor phosphorylation sites during bidirectional synaptic plasticity
    • Lee, H. K., Barbarosie, M., Kameyama, K., Bear, M. F. & Huganir, R. L. Regulation of distinct AMPA receptor phosphorylation sites during bidirectional synaptic plasticity. Nature 405, 955-959 (2000).
    • (2000) Nature , vol.405 , pp. 955-959
    • Lee, H.K.1    Barbarosie, M.2    Kameyama, K.3    Bear, M.F.4    Huganir, R.L.5
  • 81
    • 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, 89-102 (2000).
    • (2000) J. Neurosci. , vol.20 , pp. 89-102
    • Banke, T.G.1
  • 82
    • 0028116665 scopus 로고
    • Cyclic AMP synaptic activity-dependent phosphorylation of AMPA-preferring glutamate receptors
    • Blackstone, C., Murphy, T. H., Moss, S. J., Baraban, J. M. & Huganir, R. L. Cyclic AMP and synaptic activity-dependent phosphorylation of AMPA-preferring glutamate receptors. J. Neurosci. 14, 7585-7593 (1994).
    • (1994) J. Neurosci. , vol.14 , pp. 7585-7593
    • Blackstone, C.1    Murphy, T.H.2    Moss, S.J.3    Baraban, J.M.4    Huganir, R.L.5
  • 84
    • 0037312605 scopus 로고    scopus 로고
    • PKA phosphorylation of AMPA receptor subunits controls synaptic trafficking underlying plasticity
    • Esteban, J. A. et al. PKA phosphorylation of AMPA receptor subunits controls synaptic trafficking underlying plasticity. Nature Neurosci. 6, 136-143 (2003).
    • (2003) Nature Neurosci. , vol.6 , pp. 136-143
    • Esteban, J.A.1
  • 85
    • 0345119031 scopus 로고    scopus 로고
    • Ubiquitination regulates PSD-95 degradation and AMPA receptor surface expression
    • Colledge, M. et al. Ubiquitination regulates PSD-95 degradation and AMPA receptor surface expression. Neuron 40, 595-607 (2003).
    • (2003) Neuron , vol.40 , pp. 595-607
    • Colledge, M.1
  • 86
    • 0028817705 scopus 로고
    • α/11
    • α/11. Neuron 14, 399-405 (1995).
    • (1995) Neuron , vol.14 , pp. 399-405
    • Jones, S.1
  • 87
    • 0029068866 scopus 로고
    • Potassium currents in rat prevertebral and paravertebral sympathetic neurones: Control of firing properties
    • Wang, H. S. & McKinnon, D. Potassium currents in rat prevertebral and paravertebral sympathetic neurones: control of firing properties. J. Physiol. 485, 319-335 (1995).
    • (1995) J. Physiol. , vol.485 , pp. 319-335
    • Wang, H.S.1    McKinnon, D.2
  • 88
    • 0036683972 scopus 로고    scopus 로고
    • Recovery from muscarinic modulation of M current channels requires phosphatidylinositol 4,5-bisphosphate synthesis
    • Suh, B. C. & Hille, B. Recovery from muscarinic modulation of M current channels requires phosphatidylinositol 4,5-bisphosphate synthesis. Neuron 35, 507-520 (2002).
    • (2002) Neuron , vol.35 , pp. 507-520
    • Suh, B.C.1    Hille, B.2
  • 89
    • 0037468826 scopus 로고    scopus 로고
    • 2 activates KCNQ channels, and its hydrolysis underlies receptor-mediated inhibition of M currents
    • 2 activates KCNQ channels, and its hydrolysis underlies receptor-mediated inhibition of M currents. Neuron 37, 963-975 (2003).
    • (2003) Neuron , vol.37 , pp. 963-975
    • Zhang, H.1
  • 90
    • 0032104245 scopus 로고    scopus 로고
    • The extended protein kinase C super-family
    • Mellor, H. & Parker, P. J. The extended protein kinase C super-family. Biochem. J. 332, 281-292 (1998).
    • (1998) Biochem. J. , vol.332 , pp. 281-292
    • Mellor, H.1    Parker, P.J.2
  • 91
    • 0038407962 scopus 로고
    • Protein kinase C is not necessary for peptide-induced suppression of M current or for desensitization of the peptide receptors
    • Bosma, M. M. & Hille, B. Protein kinase C is not necessary for peptide-induced suppression of M current or for desensitization of the peptide receptors. Proc. Natl Acad. Sci. USA 86, 2943-2947 (1989).
    • (1989) Proc. Natl. Acad. Sci. USA , vol.86 , pp. 2943-2947
    • Bosma, M.M.1    Hille, B.2
  • 93
    • 0018843137 scopus 로고
    • +-current in bullfrog sympathetic neurones
    • +-current in bullfrog sympathetic neurones. Br. J. Pharmacol. 68, 353-355 (1980).
    • (1980) Br. J. Pharmacol. , vol.68 , pp. 353-355
    • Adams, P.R.1    Brown, D.A.2
  • 94
    • 0037512350 scopus 로고    scopus 로고
    • AKAP150 signaling complex promotes suppression of the M-current by muscarinic agonists
    • Hoshi, N. et al. AKAP150 signaling complex promotes suppression of the M-current by muscarinic agonists. Nature Neurosci. 6, 584-571 (2003). Shows that AKAPs can organize signalling complexes that contain a subset of all the possible binding partners.
    • (2003) Nature Neurosci. , vol.6 , pp. 584-571
    • Hoshi, N.1
  • 96
    • 0032476061 scopus 로고    scopus 로고
    • AKAP15 anchors cAMP-dependent protein kinase to brain sodium channels
    • Tibbs, V. C., Gray, P. C., Catterall, W. A. & Murphy, B. J. AKAP15 anchors cAMP-dependent protein kinase to brain sodium channels. J. Biol. Chem. 273, 25783-25788 (1998).
    • (1998) J. Biol. Chem. , vol.273 , pp. 25783-25788
    • Tibbs, V.C.1    Gray, P.C.2    Catterall, W.A.3    Murphy, B.J.4
  • 97
    • 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, 1921-1930 (2001). Describes a negative-feedback loop between PKA and a phosphodiesterase anchored to an AKAP.
    • (2001) EMBO J. , vol.20 , pp. 1921-1930
    • Dodge, K.L.1
  • 98
    • 0033761535 scopus 로고    scopus 로고
    • Phosphodiesterases and cyclic nucleotide signaling in endocrine cells
    • Conti, M. Phosphodiesterases and cyclic nucleotide signaling in endocrine cells. Mol. Endocrinol. 14, 1317-1327 (2000).
    • (2000) Mol. Endocrinol. , vol.14 , pp. 1317-1327
    • Conti, M.1
  • 99
    • 0037458648 scopus 로고    scopus 로고
    • Cyclic AMP-specifc PDE4 Phosphodiesterases as critical components of cyclic AMP signaling
    • Conti, M. et al. Cyclic AMP-specifc PDE4 Phosphodiesterases as critical components of cyclic AMP signaling. J. Biol. Chem. 278, 5493-5496 (2003).
    • (2003) J. Biol. Chem. , vol.278 , pp. 5493-5496
    • Conti, M.1
  • 100
    • 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, 264-268 (2001).
    • (2001) FEBS Lett. , vol.507 , pp. 264-268
    • Klussmann, E.1
  • 101
    • 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., Abuin, L., Cotecchia, S. & Pansier, L. Anchoring of both PKA and 14-3-3 inhibits the Rho-GEF activity of the AKAP-Lbc signaling complex. EMBO J. 23, 2811-2820 (2004).
    • (2004) EMBO J. , vol.23 , pp. 2811-2820
    • Diviani, D.1    Abuin, L.2    Cotecchia, S.3    Pansier, L.4
  • 102
    • 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, 1436-1450 (2004). References 101 and 102 identify an inhibitory mechanism that downregulates the Rho-GEF activity of AKAP-Lbc, and provide the first example of an interaction between an AKAP and 14-3-3, a classic phosphoserine/threonine binding protein.
    • (2004) Curr. Biol. , vol.14 , pp. 1436-1450
    • Jin, J.1
  • 103
    • 3242788127 scopus 로고    scopus 로고
    • Dynamic interactions between 14-3-3 proteins and phosphoproteins regulate diverse cellular processes
    • Mackintosh, C. Dynamic interactions between 14-3-3 proteins and phosphoproteins regulate diverse cellular processes. Biochem. J. 381, 320-342 (2004).
    • (2004) Biochem. J. , vol.381 , pp. 320-342
    • Mackintosh, C.1
  • 104
    • 0030006920 scopus 로고    scopus 로고
    • Phosphorylation and activation of a cAMP-specific phosphodiesterase by the cAMP-dependent protein kinase
    • Sette, C. & Conti, M. Phosphorylation and activation of a cAMP-specific phosphodiesterase by the cAMP-dependent protein kinase. J. Biol. Chem. 271, 16526-16534 (1996).
    • (1996) J. Biol. Chem. , vol.271 , pp. 16526-16534
    • Sette, C.1    Conti, M.2
  • 105
    • 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, 587-592 (2004).
    • (2004) Biochem. J. , vol.381 , pp. 587-592
    • Carlisle Michel, J.J.1
  • 106
    • 0034789448 scopus 로고    scopus 로고
    • mAKAP and the ryanodine receptor are part of a multi-component signaling complex on the cardiomyocyte nuclear envelope
    • Kapiloff, M. S., 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. 114, 3167-3176 (2001).
    • (2001) J. Cell Sci. , vol.114 , pp. 3167-3176
    • Kapiloff, M.S.1    Jackson, N.2    Airhart, N.3
  • 107
    • 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, 21999-22002 (2001).
    • (2001) J. Biol. Chem. , vol.276 , pp. 21999-22002
    • Tasken, K.A.1
  • 109
    • 0029964752 scopus 로고    scopus 로고
    • Protein kinase D (PKD) activation in intact cells through a protein kinase C-dependent signal transduction pathway
    • Zugaza, J. L., Sinnett-Smith, J., Van Lint, J. & Rozengurt, E. Protein kinase D (PKD) activation in intact cells through a protein kinase C-dependent signal transduction pathway. EMBO J. 15, 6220-6230 (1996).
    • (1996) EMBO J. , vol.15 , pp. 6220-6230
    • Zugaza, J.L.1    Sinnett-Smith, J.2    Van Lint, J.3    Rozengurt, E.4
  • 110
    • 8944263302 scopus 로고    scopus 로고
    • A role for Rho in receptor- and G protein-stimulated phospholipase C. Reduction in phosphatidylinositol 4,5-bisphosphate by Clostridium difficile toxin B
    • Schmidt, M. et al. A role for Rho in receptor- and G protein-stimulated phospholipase C. Reduction in phosphatidylinositol 4,5-bisphosphate by Clostridium difficile toxin B. Naunyn Schmiedebergs Arch. Pharmacol. 354, 87-94 (1996).
    • (1996) Naunyn Schmiedebergs Arch. Pharmacol. , vol.354 , pp. 87-94
    • Schmidt, M.1
  • 111
    • 0033779101 scopus 로고    scopus 로고
    • Structure, function, and control of phosphoinositide-specific phospholipase C
    • Rebecchi, M. J. & Pentyala, S. N. Structure, function, and control of phosphoinositide-specific phospholipase C. Physiol. Rev. 80, 1291-1335 (2000).
    • (2000) Physiol. Rev. , vol.80 , pp. 1291-1335
    • Rebecchi, M.J.1    Pentyala, S.N.2
  • 112
    • 0037389225 scopus 로고    scopus 로고
    • Mechanism of persistent protein kinase D1 translocation and activation
    • Oancea, E., Bezzerides, V. J., Greka, A. & Clapham, D. E. Mechanism of persistent protein kinase D1 translocation and activation. Dev. Cell 4, 561-574 (2003).
    • (2003) Dev. Cell , vol.4 , pp. 561-574
    • Oancea, E.1    Bezzerides, V.J.2    Greka, A.3    Clapham, D.E.4
  • 113
    • 0142250491 scopus 로고    scopus 로고
    • Intracellular location and cell context-dependent function of protein kinase D
    • Marklund, U., Lightfoot, K. & Cantrell, D. Intracellular location and cell context-dependent function of protein kinase D. Immunity 19, 491-501 (2003).
    • (2003) Immunity , vol.19 , pp. 491-501
    • Marklund, U.1    Lightfoot, K.2    Cantrell, D.3
  • 114
    • 0034659737 scopus 로고    scopus 로고
    • Spatial and temporal regulation of protein kinase D (PKD)
    • Matthews, S. A., Iglesias, T., Rozengurt, E. & Cantrell, D. Spatial and temporal regulation of protein kinase D (PKD). EMBO J. 19, 2935-2945 (2000).
    • (2000) EMBO J. , vol.19 , pp. 2935-2945
    • Matthews, S.A.1    Iglesias, T.2    Rozengurt, E.3    Cantrell, D.4
  • 115
    • 0035980125 scopus 로고    scopus 로고
    • Activation loop Ser744 and Ser748 in protein kinase D are transphosphorylated in vivo
    • Waldron, R. T. et al. Activation loop Ser744 and Ser748 in protein kinase D are transphosphorylated in vivo. J. Biol. Chem. 276, 32606-32615 (2001).
    • (2001) J. Biol. Chem. , vol.276 , pp. 32606-32615
    • Waldron, R.T.1
  • 116
    • 0036536426 scopus 로고    scopus 로고
    • Protein kinase D: An intracellular traffic regulator on the move
    • Van Lint, J. et al. Protein kinase D: an intracellular traffic regulator on the move. Trends Cell Biol. 12, 193-200 (2002).
    • (2002) Trends Cell Biol. , vol.12 , pp. 193-200
    • Van Lint, J.1
  • 117
    • 0034705543 scopus 로고    scopus 로고
    • Gravin-mediated formation of signaling complexes in β2-adrenergic receptor desensitization and resensitization
    • Lin, F., Wang, H. & Malbon, C. C. Gravin-mediated formation of signaling complexes in β2-adrenergic receptor desensitization and resensitization. J. Biol. Chem. 275, 19025-19034 (2000).
    • (2000) J. Biol. Chem. , vol.275 , pp. 19025-19034
    • Lin, F.1    Wang, H.2    Malbon, C.C.3
  • 118
    • 0035968196 scopus 로고    scopus 로고
    • The scaffold protein gravin (cAMP-dependent protein kinase-anchoring protein 250) binds the β2-adrenergic receptor via the receptor cytoplasmic Arg-329 to Leu-413 domain and provides a mobile scaffold during desensitization
    • Fan, G., Shumay, E., Wang, H. & Malbon, C. C. The scaffold protein gravin (cAMP-dependent protein kinase-anchoring protein 250) binds the β2-adrenergic receptor via the receptor cytoplasmic Arg-329 to Leu-413 domain and provides a mobile scaffold during desensitization. J. Biol. Chem. 276, 24005-24014 (2001).
    • (2001) J. Biol. Chem. , vol.276 , pp. 24005-24014
    • Fan, G.1    Shumay, E.2    Wang, H.3    Malbon, C.C.4
  • 119
    • 0035834428 scopus 로고    scopus 로고
    • Regulation of receptor fate by ubiquitination of activated β2-adrenergic receptor and β-arrestin
    • Shenoy, S. K., McDonald, P. H., Kohout, T. A. & Lefkowitz, R. J. Regulation of receptor fate by ubiquitination of activated β2-adrenergic receptor and β-arrestin. Science 294, 1307-1313 (2001).
    • (2001) Science , vol.294 , pp. 1307-1313
    • Shenoy, S.K.1    McDonald, P.H.2    Kohout, T.A.3    Lefkowitz, R.J.4
  • 120
    • 0035089841 scopus 로고    scopus 로고
    • Targeted protein kinase A and PP-2B regulate insulin secretion through reversible phosphorylation
    • Lester, L. B., Faux, M. C., Nauert, J. B. & Scott, J. D. Targeted protein kinase A and PP-2B regulate insulin secretion through reversible phosphorylation. Endocrinology 142, 1218-1227 (2001).
    • (2001) Endocrinology , vol.142 , pp. 1218-1227
    • Lester, L.B.1    Faux, M.C.2    Nauert, J.B.3    Scott, J.D.4
  • 121
    • 0037083640 scopus 로고    scopus 로고
    • Identification and characterization of myeloid translocation gene 16b as a novel A kinase anchoring protein in T lymphocytes
    • Schillace, R. V., Andrews, S. F., Liberty, G. A., Davey, M. P. & Carr, D. W. Identification and characterization of myeloid translocation gene 16b as a novel A kinase anchoring protein in T lymphocytes. J. Immunol. 168, 1590-1599 (2002).
    • (2002) J. Immunol. , vol.168 , pp. 1590-1599
    • Schillace, R.V.1    Andrews, S.F.2    Liberty, G.A.3    Davey, M.P.4    Carr, D.W.5
  • 122
    • 0037421222 scopus 로고    scopus 로고
    • Imaging kinase-AKAP79-phosphatase scaffold complexes at the plasma membrane in living cells using FRET microscopy
    • Oliveria, S. F., Gomez, L. L. & Dell'Acqua, M. L. Imaging kinase-AKAP79-phosphatase scaffold complexes at the plasma membrane in living cells using FRET microscopy. J. Cell Biol. 160, 101-112 (2003).
    • (2003) J. Cell Biol. , vol.160 , pp. 101-112
    • Oliveria, S.F.1    Gomez, L.L.2    Dell'Acqua, M.L.3
  • 123
    • 0036469182 scopus 로고    scopus 로고
    • Luminescent quantum dots for multiplexed biological detection and imaging
    • Chan, W. C. et al. Luminescent quantum dots for multiplexed biological detection and imaging. Curr. Opin. Biotechnol. 13, 40-46 (2002).
    • (2002) Curr. Opin. Biotechnol. , vol.13 , pp. 40-46
    • Chan, W.C.1
  • 124
    • 1542336956 scopus 로고    scopus 로고
    • The molecular properties and applications of Anthozoa fluorescent proteins and chromoproteins
    • Verkhusha, V. V. & Lukyanov, K. A. The molecular properties and applications of Anthozoa fluorescent proteins and chromoproteins. Nature Biotechnol. 22, 289-296 (2004).
    • (2004) Nature Biotechnol. , vol.22 , pp. 289-296
    • Verkhusha, V.V.1    Lukyanov, K.A.2
  • 125
    • 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., Martins, S. B., Tasken, K. & Colas, P. 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, 1251-1262 (2000).
    • (2000) J. Cell Biol. , vol.150 , pp. 1251-1262
    • Steen, R.L.1    Martins, S.B.2    Tasken, K.3    Colas, P.4
  • 126
    • 1042266629 scopus 로고    scopus 로고
    • Centrosomal anchoring of protein kinase C βII by pericentrin controls microtubule organization, spindle function, and cytokinesis
    • Chen, D., Purohit, A., Halilovic, E., Doxsey, S. J. & Newton, A. C. Centrosomal anchoring of protein kinase C βII by pericentrin controls microtubule organization, spindle function, and cytokinesis. J. Biol. Chem. 279, 4829-4839 (2004).
    • (2004) J. Biol. Chem. , vol.279 , pp. 4829-4839
    • Chen, D.1    Purohit, A.2    Halilovic, E.3    Doxsey, S.J.4    Newton, A.C.5
  • 127
    • 0034700490 scopus 로고    scopus 로고
    • Stargazin regulates synaptic targeting of AMPA receptors by two distinct mechanisms
    • Chen, L. et al. Stargazin regulates synaptic targeting of AMPA receptors by two distinct mechanisms. Nature 408, 936-943 (2000).
    • (2000) Nature , vol.408 , pp. 936-943
    • Chen, L.1
  • 128
    • 0032842848 scopus 로고    scopus 로고
    • mAKAP: An A-kinase anchoring protein targeted to the nuclear membrane of differentiated myocytes
    • Kapiloff, M. S., Schillace, R. V., Westphal, A. M. & Scott, J. D. mAKAP: an A-kinase anchoring protein targeted to the nuclear membrane of differentiated myocytes. J. Cell Sci. 112, 2725-2736 (1999).
    • (1999) J. Cell Sci. , vol.112 , pp. 2725-2736
    • Kapiloff, M.S.1    Schillace, R.V.2    Westphal, A.M.3    Scott, J.D.4
  • 129
    • 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., Bhattacharyya, N. & Rubin, C. S. 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, 4648-4656 (1989).
    • (1989) J. Biol. Chem. , vol.264 , pp. 4648-4656
    • Bregman, D.B.1    Bhattacharyya, N.2    Rubin, C.S.3
  • 130
    • 0018248691 scopus 로고
    • Fractionation of brain microtubule-associated proteins. Isolation of two different proteins which stimulate tubulin polymerization in vitro
    • Herzog, W. & Weber, K. Fractionation of brain microtubule-associated proteins. Isolation of two different proteins which stimulate tubulin polymerization in vitro. Eur. J. Biochem. 92, 1-8 (1978).
    • (1978) Eur. J. Biochem. , vol.92 , pp. 1-8
    • Herzog, W.1    Weber, K.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.