Cyclic nucleotide-dependent protein kinases: Intracellular receptors for cAMP and cGMP action

Critical Reviews in Clinical Laboratory Sciences

Volumn 36, Issue 4, 1999, Pages 275-328

  Francis, Sharron H ^a   Corbin, Jackie D ^a  

^a VANDERBILT UNIVERSITY SCHOOL OF MEDICINE   (United States)

Author keywords

cAMP; cGMP; Intracellular receptors; Phosphorylation; Protein kinases; Second messenger; Signal transduction

Indexed keywords

ADENOSINE TRIPHOSPHATE MAGNESIUM; CALCIUM ION; CYCLIC AMP; CYCLIC GMP; CYCLIC NUCLEOTIDE DEPENDENT PROTEIN KINASE; NUCLEOTIDE; PROTEIN KINASE INHIBITOR; RECEPTOR;

ALTERNATIVE RNA SPLICING; BINDING SITE; BONE TURNOVER; CALCIUM CELL LEVEL; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME LOCALIZATION; ENZYME STRUCTURE; ENZYME SUBUNIT; FEEDBACK SYSTEM; GENOME; KIDNEY FUNCTION; MELANOGENESIS; PRIORITY JOURNAL; PROTEIN PHOSPHORYLATION; PROTEIN PROTEIN INTERACTION; REVIEW; SECOND MESSENGER; SIGNAL TRANSDUCTION; SMOOTH MUSCLE; THROMBOCYTE AGGREGATION;

ANIMALS; BINDING SITES; CYCLIC AMP; CYCLIC AMP-DEPENDENT PROTEIN KINASES; CYCLIC GMP; CYCLIC GMP-DEPENDENT PROTEIN KINASES; HUMANS;

EID: 0032848914     PISSN: 10408363     EISSN: None     Source Type: Journal    
DOI: 10.1080/10408369991239213     Document Type: Review

References (269)

1. Friedman DL, Larner J. Studies on UDPG-α-glucan transglucosylase III. Interconversion of two forms of muscle UDPG-α-glucan transglucosylase by a phosphorylation-dephosphorylation reaction sequence. Biochemistry 1963; 4: 669-75.
2. Rosell-Perez M, Larner J. Studies on UDPG-α-glucan transglucosylase V. Two forms of the enzyme in dog skeletal muscle and their interconversion. Biochemistry 1964; 3: 81-88.
3. Walsh DA, Perkins JP Krebs EG. An adenosine 3′,5′-monophosphate-dependent protein kinase form rabbit skeletal muscle. J Biol Chem 1968; 243: 3763-65.
4. Beebe SJ, Corbin JD. Cyclic nucleotide-dependent protein kinases. In: Boyer P, Krebs E, eds. The enzymes, 17A. Pp. 43-111. Orlando: Academic Press, 1986.
5. Edelman AM, Blumenthal DK Krebs EG. Protein serine/threonine kinases. Annu Rev Biochem 1987; 56: 567-613.
6. Gettys TW, Corbin JD. The protein kinase family of enzymes. In: Moudgil VK, ed. Receptor phosphorylation. Pp. 40-88. Boca Raton: CRC Press, 1989.
7. Krebs EG. The enzymology of control by phosphorylation. In: Boyer PD, Krebs EG, eds. The enzymes, 58. Pp. 3-20. New York: Academic Press, 1986.
8. Scott JD. Cyclic nucleotide-dependent protein kinases. Pharmacol Ther 1991; 50: 123-45.
9. Taylor SS, Buechler JA Yonemoto Y. cAMP-dependent protein kinase: framework for diverse family of regulatory enzymes, Annu Rev Biochem 1990; 9; 971-1005.
10. Woodford TA, Taylor SJ Corbin JD. The biological functions of protein phosphorylation-dephosphorylation. In: Bittar EE, ed. Fundamentals of medical cell biology, 3B. Pp. 453-507. London: JAI Press, 1992.
11. Kuo JF, Greengard P. Isolation and partial purification of a protein kinase activated by cGMP. J Biol Chem 1970; 245: 2493-98.
12. Corbin JD, Lincoln TM. Comparison of cAMP- and cGMP-dependent protein kinases. Adv Cyclic Nucleotide Res 1978; 9: 159-70.
13. Gill GN, Holdy KE, Walton GM, et al. Purification and characterization of cGMP-dependent protein kinase, Proc Natl Acad Sci USA 1976; 73: 3918-22.
14. Hanks SK, Quinn AM Hunter T. The protein kinase family: conserved features and deduced phylogeny of the catalytic domains. Science 1988; 241: 42-52.
15. Hofmann F, Dostmann W, Keilbach A, et al. Structure and physiological role of cGMP-dependent protein kinase. Biochim Biophys Acta 1992; 1135: 51-60.
16. Lincoln TM, Corbin JD. Characterization and biological role of the cGMP-dependent protein kinase. Adv Cyclic Nucleotide Res 1983; 15: 139-92.
17. Takio K, Wade RD, Smith SB, et al. Guanosine cyclic 3′,5′-phosphate dependent protein kinase, a chimeric protein homologous with two separate protein families. Biochemistry 1984; 23: 4207-18.
18. Butt E, Geiger J, Jarchau T, et al. The cGMP-dependent protein kinase-gene, protein and function. Neurochem Res 1993; 18: 27-42.
19. Francis SH, Corbin JD. Progress in understanding the mechanism and function of cGMP-dependent protein kinase. In: Advances in pharmacology. Vol. 26, Pp. 115-70. Orlando: Academic Press, 1993.
20. Lincoln TM. Cyclic GMP and mechanisms of vasodilation. Pharmacol Ther 1989; 41: 479-502.
21. Lincoln TM, Cornwell, TL. Intracellular cGMP receptor proteins. FASEB J 1993; 7: 328-38.
22. Murad F. Cyclic guanosine monophosphate as a mediator of vasodilation. J Clin Invest 1986; 78: 1-5.
23. Walter U. Physiological role of cGMP and cGMP-dependent protein kinase in the cardiovascular system. Rev Physiol Biochem Pharmacol 1989; 113: 42-88.
24. Lohmann SM, Vaandrager AB, Smolenski A, et al. Distinct and specific functions of cGMP-dependent protein kinases. Trends Biochem Sci 1997; 22: 307-12.
25. Shabb JB, Corbin JD. Cyclic nucleotide-binding domains in proteins having diverse functions. J Biol Chem 1992; 267: 5723-26.
26. Shoji S, Ericsson LH, Walsh KA, et al. Amino acid sequence of the catalytic subunit of bovine type II adenosine cyclic 3′,5′- phosphate dependent protein kinase. Biochemistry 1983; 22: 3702-9.
27. Takio K, Smith SB, Krebs EG, et al. Amino acid sequence of the regulatory subunit of bovine type II adenosine 3′,5′-monophosphate dependent protein kinase. Biochemistry 1984; 23: 4200-6.
28. Titani K, Sasagawa T, Ericsson LH, et al. Amino acid sequence of the type I regulatory subunit of bovine type I adenosine cyclic 3′,5′-phosphate-dependent protein kinase. Biochemistry 1984; 23: 4193-99.
29. Rannels SR, Cobb CE, Landiss LR, et al. The regulatory subunit monomer of cAMP-dependent protein kinase retains the salient kinetic properties of the native dimeric subunit. J Biol Chem 1985; 260: 3423-30.
30. Reimann EM. Conversion of bovine cardiac adenosine cyclic 3′,5′-phosphate dependent protein kinase to a heterodimer by removal of 45 residues at the N-terminus of the regulatory subunit. Biochemistry 1986; 25: 119-25.
31. Doskeland SO, Maronde E Gjertsen BT. The genetic subtypes of cAMP-dependent protein kinase-functionally different or redundant? Biochim Biophys Acta 1993; 1178: 249-58.
32. Corbin JD, Sugden PH, West L, et al. Studies on properties and mode of action of the purified regulatory subunit of bovine heart cAMP-dependent protein kinase. J Biol Chem 1978; 253: 3997-4033.
33. Robinson-Steiner AM, Corbin JD. Probable involvement of both intrachain cAMP binding sites in activation of protein kinase. J Biol Chem 1983; 258: 1032-40.
34. Reimann, EM, Brostrom, CD, Corbin, JD, et al. Separation of regulatory and catalytic subunits of the cyclic 3′,5′-adenosine monophosphate-dependent protein kinase(s) of rabbit skeletal muscle. Biochem Biophys Res Commun 1971; 42: 187-94.
35. Houge G, Steinberg RA, Ogreid D, et al. The rate of recombination of the subunits (RJ and C) of cAMP-dependent protein kinase depends on whether one or two cAMP molecules are bound per RI monomer. J Biol Chem 1990; 265: 19507-16.
36. Johnson DA, Leathers VL, Martinez AM, et al. Fluorescence resonance energy transfer within a heterochromatic cAMP-dependent protein kinase holoenzyme under equilibrium conditions: new insights into the conformational changes that result in cAMP-dependent activation. Biochemistry 1993; 32: 6402-10.
37. Jahnsen T, Hedin L, Kidd VJ, et al. Molecular cloning, cDNA structure, and regulation of the regulatory subunit of type II cAMP-dependent protein kinase from rat ovarian granulosa cells. J Biol Chem 1986; 261: 12352-61.
38. Flockhart DA, Corbin JD. Regulatory mechanisms in the control of protein kinases. Crit Rev Biochem 1982; 12: 133-86.
39. Beebe SJ, Holloway R, Rannels SR, et al. Two classes of cAMP analogs which are selective for the two different cAMP-binding sites of Type 11 protein kinase demonstrate synergism when added together to intact adipocytes. J Biol Chem 1984; 259: 3539-47.
40. Skalhegg BS, Landmark B, Doskeland SO, et al. Cyclic AMP-dependent protein kinase type I mediates the inhibitory effects of 3′,5′-cyclic adenosine monophosphate on cell replication in T lymphocytes. J Biol Chem 1992; 267: 15707-14.
41. Van Sande J, Lefort A, Beebe S, et al. Pairs of cAMP analogs, that are specifically synergistic for type I and type II cAMP-dependent protein kinases, mimic thyrotropin effects on function, differentiation expression and mitogenesis of dog thyroid cells. Eur J Biochem 1989; 183: 699-708.
42. Tasken K, Skalhegg BS, Tasken KA, et al. Structure, function, and regulation of human cAMP-dependent protein kinases. Adv Second Mess Phosphoprotein Res 1997; 31: 191-204.
43. Corbin JD, Sugden PH, Lincoln TM, et al. Compartmentalization of adenosine 3′:5′-monophosphate-dependent protein kinase in heart tissue. J Biol Chem 1997; 252: 3854-61.
44. Feliciello A, Li Y, Avvedimento EV, et al. A-kinase anchor protein 75 increases the rate and magnitude of cAMP signaling of the nucleus. Curr Biol 1997; 7: 1011-14.
45. Pawson T, Scott JD. Signaling through scaffold, anchoring, and adaptor proteins. Science 1997; 278: 2075-80.
46. Tasken K, Skalhegg BS, Solberg R, et al. Novel isozymes of cAMP-dependent protein kinase exist in human cells due to formation of RIα-RIβ heterodimeric complexes. J Biol Chem 1993; 268: 21276-83.
47. Li V, Rubin CS. Mutagenesis of the regulatory subunit RIIβ of cAMP-dependent protein kinase IIβ reveals hydrophobic amino acids that are essential for RIIβ dimerization and/or anchoring RIIβ to the cytoskeleton. J Biol Chem 1995; 270: 1935-44.
48. Leon DA, Herberg FW, Banky P, et al. A stable α-helical domain at the N terminus of the RIα subunits of cAMP-dependent protein kinase is a novel dimerization/docking motif. J Biol Chem 1997; 272: 28431-7.
49. Beebe SJ. The cAMP-dependent protein kinases and cAMP signal transduction. Sem Cancer Biol 1994; 5: 285-94.
50. Chrivia JC, Uhler MD McKnight GS. Characterization of genomic clones coding for the Cα and Cβ subunits of mouse cAMP-dependent protein kinase. J Biol Chem 1988; 263: 5739-44.
51. Gamm DM, Baude EJ Uhler MD. The major catalytic subunit isoforms of cAMP-dependent protein kinase have distinct biochemical properties in vitro and in vivo. J Biol Chem 1996; 271: 15736-42.
52. Cummings DE, Edelhoff S, Disteche CM, et al. Cloning of a mouse protein kinase A catalytic subunit pseudogene and chromosomal mapping of C subunit isoforms. Mamm Genome 1994; 5: 701-6.
53. Tasken K, Solberg R, Zhao Y, et al. The gene encoding the catalytic subunit Cα of cAMP-dependent protein kinase (locus PRKACA) localizes to human chromosome region 19p13.1. Genomics 1996, 36: 535-8.
54. Guthric CR, Skalhegg BS McKnight GS. Two novel brain-specific splice variants of the murine Cβ gene of cAMP-dependent protein kinase, J Biol Chem 1997; 272: 29560-5.
55. Foss K, Simard J, Berube D, et al. Localization of the catalytic subunit Cg of the cAMP-dependent protein kinase gene (PRKACG) to human chromosome region 9ql3. Cytogenet Cell Genet 1992; 60: 22-5.
56. Toda T, Cameron S, Sass P, et al. Three different genes in S. cerevisiae encode the catalytic subunits of the cAMP-dependent protein kinase. Cell 1987; 50: 277-87.
57. Cadd GG, Uhler MD McKnight GS. Holoenzymes of cAMP-dependent protein kinase containing the neural form of type I regulatory subunit have an increased sensitivity to cyclic nucleotides. J Biol Chem 1990; 265; 19502-6.
58. Glass DB, Krebs EG. Comparison of the substrate specificity of cAMP- and cGMP-dependent protein kinases. J Biol Chem 1979; 254: 9728-38.
59. Kemp BE, Graves DJ, Benjamini E, et al. Role of multiple basic residues in determining the substrate specificity of cAMP-dependent protein kinase J Biol Chem 1977; 252: 4888-94.
60. Kemp BE, Pearson RB. Protein kinase recognition sequence motifs. Trends Biochem Sci 1990; 15: 342-46.
61. Kennelly PJ, Krebs EG. Consensus sequences as substrate specificity determinants for protein kinases and protein phosphatases. J Biol Chem 1991; 266: 15555-58.
62. Yeaman SJ, Cohen P, Watson DC, et al. The substrate specificity of adenosine 3′,5′-cyclic monophosphate-dependent protein kinase. Biochem J 1977; 152: 411-21.
63. Zetterqvist O, Ragnarsson U Engstrom L. Substrate specificity of cyclic AMP-dependent protein kinase. In: Kemp BE, ed. Peptides and protein phosphorylation. Pp. 171-188. Boca Raton: CRC Press, 1990.
64. Rannels SR, Corbin JD. Two different intrachain cAMP binding sites of cAMP-dependent protein kinases. J Biol Chem 1980; 255: 7985-8.
65. Cobb CE, Beth AH Corbin JD. Purification and characterization of an inactive form of cAMP-dependent protein kinase containing bound cAMP. J Biol Chem 1987; 262: 16566-74.
66. Luo A, Shafit-Zagardo B Erlichman J. Identification of the MAP2 and P75-binding domain in the regulatory subunit (RIIβ) of type II cAMP-dependent protein kinase. J Biol Chem 1990; 265: 21804-10.
67. Scott JD, Stofko RE, McDonald JR, et al. Type II regulatory subunit dimerization determines the subcellular localization of the cAMP-dependent protein kinase. J Biol Chem 1990; 265: 21561-66.
68. Weber IT, Steitz TA, Bubis J, et al. Predicted structures of cAMP binding domains of type I and II regulatory subunits of cAMP-dependent protein kinases. Biochemistry 1987; 26: 343-51.
69. Doskeland SO, Ogreid D. Characterization of the interchain and intrachain interactions between the binding sites of the free regulatory moiety of protein kinase I. J Biol Chem 1984; 259: 2921-301.
70. Miller JP, Uno H, Christensen LJ, et al. Effect of modification of the 1-, 2-, and 6-positions of 9-β-D-ribofuranosyl-purine cyclic 3′,5′-phosphate and guanosine cyclic 3′,5′- phosphate dependent protein kinases. Biochem Pharmacol 1981; 30: 509-15.
71. Ogreid D, Doskeland SO. The kinetics of association of cyclic AMP to the two types of binding sites associated with protein kinase II from bovine myocardium. FEBS Lett 1981; 129: 287-92.
72. Ogreid D, Doskeland SO Miller JP. Evidence that cyclic nucleotides activating rabbit muscle protein kinase T interact with both types of cAMP binding sites associated with the enzyme. J Biol Chem 1983; 258: 1041-49.
73. Ogreid D, Ekanger RH, Suva JP, et al. Activation of protein kinase isozymes by cyclic nucleotide analogs used singly or in combination. Eur J Biochem 1985; 150: 219-27.
74. McKnight GS, Cadd GG, Clegg C. et al. Expression of wild-type and mutant subunits of the cAMP-dependent protein kinase. Cold Spring Harbor Symp Quant Biol 1988; 53: 111-19.
75. Solberg R, Sandberg M, Natarajan V, et al. The human gene for the regulatory subunit of RIα of cyclic adenosine 3′,5′-monophosphate-dependent protein kinase: two distinct promoters provide differential regulation of alternatively spliced messenger ribonucleic acids. Endocrinology 1997; 138: 169-81.
76. Clegg CH, Koeiman MR, Jenkins NA, et al. Structural features of the murine gene encoding the RIβ subunit of cAMP-dependent protein kinase. Mol Cell Neurosci 1994; 5: 153-64
77. Shoji S, Titani K, Demaille JG, et al. Sequence of two phosphorylated sites in the catalytic subunit of bovine cardiac muscle adenosine 3′,5′-monophosphate-dependent protein kinase. J Biol Chem 1979; 254: 6211-14.
78. Cauthron RD, Carter KB, Liauw S, et al. Physiological phosphorylation of protein kinase A at Thr-197 is by a protein kinase A kinase. Mol Cell Biol 1998; 18: 1416-23.
79. Cheng X, Ma Y, Moore M, et al. Phosphorylation and activation of cAMP-dependent protein kinase by phosphoinositide-dependent protein kinase. Proc Natl Acad Sci USA 1998; 95: 9849-54.
80. Knighton DR, Zheng J, Ten Eyck LF, et al. Crystal structure of the catalytic subunit of cAMP-dependent protein kinase. Science 1991; 253: 407-13.
81. Knighton DR, Zheng J, Ten Eyck LF, et al. Structure of a peptide inhibitor bound to the catalytic subunit of cAMP-dependent protein kinase. Science 1991; 253: 414-20.
82. Gibson RM, Taylor SS. Dissecting the cooperative reassociation of the regulatory and catalytic subunits of cAMP-dependent protein kinase. Role of Trp-196 in the catalytic subunit. J Biol Chem 1997; 272: 31998-2005.
83. Levin LR, Kuret J, Johnson KE, et al. 1988. A mutation in the catalytic subunit of cAMP-dependent protein kinase that disrupts regulation. Science 240: 68-70.
84. Rangel-Aldao R, Kupiec JW Rosen OM. Resolution of the phosphorylated and dephosphorylated cAMP-binding proteins of bovine cardiac muscle by affinity labeling and two dimensional electrophoresis. J Biol Chem 1979; 254: 2499-508.
85. Flockhart DA, Waterson DM Corbin JD. Studies on functional domain of the regulatory subunit of bovine heart cAMP-dependent protein kinase. J Biol Chem 1980; 25: 4435-40.
86. Saraswat LD, Ringheim GE, Bubis J, et al. Deletion mutants as probes for localizing regions of subunit interaction in cAMP-dependent protein kinase. J Biol Chem 1988; 263: 18241-46.
87. Poteet-Smith CE, Shabb JB, Francis SH, et al. Identification of critical determinants for autoinhibition in the pseudosubstrate region of type Iα cAMP-dependent protein kinase. J Biol Chem 1997; 272: 379-88.
88. Wang Y, Scott JD, McKnight GS, et al. A constitutively active holoenzyme form of the cAMP-dependent protein kinase. Proc Natl Acad Sci USA 1991; 88: 2446-50.
89. Smith CP, Corbin JD Francis SH. Autoinhibition of cAMP- and cGMP-dependent protein kinases involves multiple structural components as determined by synthetic peptide analysis. In: Corbin J, Francis S, eds. Advances in second messengers and phosphoproteins: signal transduction in health and disease, Vol 31. Pp. 219-35, Lippincott-Raven Publishers, Philadelphia, 1997.
90. Woodford TA, Correll LA, McKnight GS, et al. Expression and characterization of mutant forms of the type I regulatory subunit of cAMP-dependent protein kinase. J Biol Chem 1989; 264: 13321-8.
91. Bregman DB, Hirsch AH Rubin CS. Molecular characterization of bovine brain P75, a high affinity binding protein for the regulatory subunit of cAMP-dependent protein kinase IIβ. J Biol Chem 1991; 266: 7207-13.
92. Bregman DB, Bhattacharyya N Rubin CS. High affinity binding protein for the regulatory subunit of cAMP-dependent protein kinase II-B. J Biol Chem 1989; 264: 4648-56.
93. Keely SL, Corbin JD Park CR. Regulation of adenosine 3′,5′-monophosphate-dependent protein kinase. Regulation of the heart enzyme by epinephrine, glucagon, insulin and 1-methyl-3-isobutylxanthine. J Biol Chem 1975; 250: 4832-40.
94. Lohmann SM, DeCamilli P, Einig I, 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 USA 1984; 81: 6723-27.
95. Carr DW, Stofko-Hahn RE, Fraser IDC, et al. Localization of the cAMP-dependent protein kinase to the postsynaptic densities by A kinase anchoring proteins. J Biol Chem 1992; 267: 16816-23.
96. Rubin CS, Rangel-Aldao R, Sarkar D, et al. Characterization and comparison of membrane-associated and cytosolic cAMP-dependent protein kinases. J Biol Chem 1979; 254: 3797-3805.
97. Lohmann SM, Walter U DeCamilli P. Interaction of the regulatory subunit (RII) of cAMP-dependent protein kinase with tissue-specific binding proteins including microtubule associated proteins. Ann NY Acad Sci 1986; 466: 449-52.
98. Rubin GS. A kinase anchor proteins and the intracellular targeting of signals carried by cAMP. Biochim Biophys Acta 1994; 1224: 467-479.
99. Rubino HM, Dammerman M, Shafit-Zagardo B, et al. Localization and characterization of the binding site for the regulatory subunit of type II cAMP-dependent protein kinase on MAP2. Neuron 1989; 3: 631-38.
100. Terasaki WL, Brooker G. Cardiac adenosine 3′,5′-monophosphate. Free and bound forms in the isolated rat atrium. J Biol Chem 1977; 252: 1041-50.
101. Rubin CS, Erlichman J Rosen OM. Cyclic adenosine 3′,5′-monophosphate-dependent protein kinase of erythrocyte membranes. J Biol Chem 1972; 247: 6135-139.
102. Glantz SB, Amat JA Rubin CS. cAMP signaling in neurons: patterns of neuronal expression and intracellular localization for a novel protein, AKAP 150 that anchors the regulatory subunit of cAMP-dependent protein kinase II beta. Mol Biol Cell 1992; 3: 1215-28.
103. 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.
104. 2+-channel activity by cAMP-dependent protein kinase. Proc Natl Acad Sci USA 1997; 94: 11067-72.
105. Carr DW, Stofko-Hahn RE, Fraser IDC, 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 1991; 266: 14188-89.
106. Leiser M, Rubin CS, Erlichman J. 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 1986; 261: 1904-8.
107. Ndubuka C, Li Y Rubin CS. Expression of A kinase anchor protein 75 depletes type II cAMP-dependent protein kinases from the cytoplasm and sequesters the kinases in a particulate pool. J Biol Chem 1993; 268: 7621-24.
108. Yonemoto W, McGlone MD Taylor SS. N-myristylation of the catalytic subunit of cAMP-dependent protein kinase conveys structural stability. J Biol Chem 1993; 268: 2348-52.
109. Cox S, Radzio-Andzelm E Taylor SS. Domain movement in protein kinases. Curr Opin Struc Biol 1994; 4: 893-901.
110. Herberg FW, Zimmerman B, McGlone M, et al. Importance of the A-helix of the catalytic subunit of cAMP-dependent protein kinase for stability and for orienting subdomains at the cleft interface. Protein Sci 1997; 6: 569-79.
111. Shaltiel S, Cox S Taylor SS. Conserved water molecules contribute to the extensive network of interactions at the active site of protein kinase A. Proc Natl Acad Sci USA 1998; 95: 484-91.
112. Taylor SS, Knighton DR, Zheng J, et al. A template for the protein kinase family. Trends Biochem Sci 1993; 18: 84-9.
113. Zheng JH, Knighton DR, Xuong NH, et al. Crystal structure of the myristylated catalytic subunit of cAMP-dependent protein kinase reveals open and closed conformations. Protein Sci 1993; 2: 1559-73.
114. Zheng JH, Knighton DR, Ten Eyck LF, et al. Crystal structure of the catalytic subunit of cAMP-dependent protein kinase complexed with MgATP and peptide inhibitor. Biochemistry 1993; 32: 2154-61.
115. Madhusudan, Trafney EA, Xuong NH, et al. cAMP-Dependent protein kinase: crystallographic insights into substrate recognition and phosphotransfer. Protein Sci 1994; 3: 176-87.
116. Grant BD, Hemmer W, Tsigelny I, et al. Kinetic and analysis of mutations in the glycine-rich loop of cAMP-dependent protein kinase. Biochemistry 1998; 37: 7708-15.
117. Tomoda T, Murata T, Arai K, et al. Mutations on 170Glu, a substrate recognition residue in mouse cAMP-dependent protein kinase, generate enzymes with altered substrate affinity and biological functions. Biochim Biophys Acta 1993; 1175: 333-42.
118. Orellana SA, Amieux PS, Zhao X, et al. Mutations in the catalytic subunit of the cAMP-dependent protein kinase interfere with holoenzyme formation without disrupting inhibition by protein kinase inhibitor. J Biol Chem 1993; 268: 6843-46.
119. Chestukhin A, Litovchick L, Schourov D, et al. Functional malleability of the carboxylterminal tail in protein kinase A. J Biol Chem 1996; 271: 10175-82.
120. Adams JA, McGlone ML, Gibson R, et al. Phosphorylation modulates catalytic function and regulation in the cAMP-dependent protein kinase. Biochemistry 1995; 34: 2447-54.
121. Colbran JL, Francis SH, Leach AB, et al. A phenylalanine in peptide substrates provides for selectivity between cGMP- and cAMP-dependent protein kinases. J Biol Chem 1992; 267: 9589-94.
122. Cook PF, Neville ME Jr, Brana KE, et al. Adenosine cyclic 3′,5′-monophosphate-dependent protein kinase: kinetic mechanism for the bovine skeletal muscle catalytic subunit. Biochemistry 1982; 21: 5794-99.
123. Granot J, Mildvan AS Kaiser ET. Studies of the mechanism of action and regulation of cAMP-dependent protein kinase. Arch Biochem Biophy 1980; 205: 1-17.
124. Whitehouse S, Feramisco JR, Casnellie JE, et al. Studies on the kinetic mechanism of the catalytic subunit of the cAMP-dependent protein kinase. J Biol Chem 1983; 258: 3693-701.
125. Yoon M-Y, Cook PF. Chemical mechanism of the adenosine cyclic 3′,5′-monophosphate dependent protein kinase from pH studies. Biochemistry 1987; 26: 4118-25.
126. Bramson HN, Thomas NE, Miller WT, et al. Conformation of Leu-Arg-Arg-Ser-Leu-Gly bound in the active site of adenosine cyclic 3′,5′-phosphate-dependent protein kinase. Biochemistry 1987; 26: 4466-70.
127. Granot J, Mildvan AS, Bramson HN, et al. Nuclear magnetic resonance studies of the conformation and kinetics of the peptide-substrate at the active site of bovine heart protein kinase. Biochemistry 1981; 20: 602-10.
128. Olah GA, Mitchell RD, Sosnick TR, et al. Solution structure of the cAMP-dependent protein kinase catalytic subunit and its contraction upon binding the protein kinase inhibitor peptide. Biochemistry 3993; 32: 3649-57.
129. Ho M-f, Bramson HN, Hansen DE, et al. Stereochemical course of the phospho group transfer catalyzed by cAMP-dependent protein kinase. J Am Chem Soc 1988; 110: 2680-81
130. Walsh DA, Ashby CD, Gonzalez C, et al. Purification and characterization of a protein inhibitor of adenosine 3′,5′-monophosphate-dependent protein kinases. J Biol Chem 1971; 246: 1977-85.
131. Scott JD, Glaccum. MB, Fischer EH, et al. Primary-structure requirements for inhibition by the heat stable inhibitor of the cAMP-dependent protein kinase. Proc Natl Acad Sci USA 1986; 83: 1613-16.
132. Walsh DA, Angelos KL, Van Patten SM, et al. The inhibitor protein of the cAMP-dependent protein kinase. In: Kemp BE, ed. Peptides and protein phosphorylation. Pp. 43-84. Boca Raton: CRC Press, 1990.
133. Cheng HC, Kemp BE, Pearson RB, et al. A potent synthetic peptide inhibitor of the cAMP-dependent protein kinase. J Biol Chem 1986; 271: 989-92.
134. Zoller MJ, Kuret J, Cameron S, et al. Purification and characterization of C1, the catalytic subunit of Saccharomyces cerevisiae cAMP-dependent protein kinase encoded by TPK 1. J Biol Chem 1988; 263: 9142-8.
135. Glass DB, Feller MJ, Levin LR, et al. Structural basis for the low affinities of yeast cAMP-dependent protein kinases for protein kinase inhibitor peptides. Biochemistry 1992; 31: 1728-34.
136. Glass DB, Krebs EG. Phosphorylation by cGMP-dependent protein kinase of synthetic peptide analogs of a site phosphorylated in histone H2B. J Biol Chem 1982; 257: 1196-200.
137. Glass DB. Substrate specificity of the cGMP-dependent protein kinase. In: Kemp BE, ed. Peptides and protein phosphorylation. Pp. 210-38. Boca Raton: CRC Press, 1990.
138. Fantozzi DA, Harootunian AT, Wen W, et al. Thermostable inhibitor of cAMP-dependent protein kinase enhances the rate of export of the kinase catalytic subunit from the nucleus. J Biol Chem 1994; 269: 2676-86.
139. Bacskai BJ, Hochner B, Mahaut-Smith M, et al. Spatially resolved dynamics of cAMP and protein kinase A subunits in Aplysia sensory neurons. Science 1993; 260: 22-26.
140. Hayes JS, Brunton LL. Functional compartments in cyclic nucleotide action. J Cyclic Nucleotide Res 1982; 8: 1-16.
141. Jungmann RA, Hiestand PC Schweppe JS. Mechanism of action of gonadotropin. Cyclic adenosine monophosphate-dependent translocation of ovarian cytoplasmic cyclic adenosine monophosphate-binding protein and protein kinase to nuclear acceptor sites. Endocrinology 1974; 94: 168-83.
142. Nigg EA, Hilz H, Eppenberger HM, et al. Rapid and reversible translocation of the catalytic subunit of cAMP-dependent protein kinase type II from the Golgi complex to the nucleus, EMBO J 1985; 4: 2801-6.
143. Srivastava RK, Lee YN, Noguchi K, et al. The RIIβ regulatory subunit of protein kinase A binds to cAMP response element; an alternative cAMP signaling pathway. Proc Natl Acad Sci USA 1998; 95: 6687-92.
144. Mellon PL, Clegg CH, Correll LA, et al. Regulation of transcription by cyclic AMP-dependent protein kinase. Proc Natl Acad Sci USA 1989; 86: 4887-91.
145. Harootunian AT, Adams SR, Wen W, et al. Movement of the free catalytic subunit of cAMP-dependent protein kinase into and out of the nucleus can be explained by diffusion. Mol Biol Cell 1993; 4: 993-1002.
146. Gonzalez GA, Montminy MR. Cyclic AMP stimulates somatostatin gene transcription by phosphorylation of CREB at serine 133. Cell 1989; 59: 675-80.
147. Wen W, Harootunian AT, Adams SR, et al. Heat stable inhibitors of cAMP-dependent protein kinase carry a nuclear export signal. J Biol Chem 1994; 269: 32214-20.
148. Herberg FW, Taylor SS, Dostmann WR. Active site mutations define the pathway for the cooperative activation of the cAMP-dependent protein kinase. Biochemistry 1996; 35: 2934-2942.
149. Shabb JB, Poteet CE, Kapphahn MA, et al. Characterization of the isolated cAMP-binding B domain of cAMP-dependent protein kinase. Protein Sci 1995; 4: 2100-06.
150. Su Y, Dostmann WR, Herberg F, et al. Regulatory subunit of protein kinase A: structure of a deletion mutant with cAMP binding domains. Science 1995; 269: 807-13.
151. Zorn M, Fladmark KE, Ogreid D, et al. Ala 335 is essential for high affinity cAMP-binding of both sites A and B of cAMP-dependent protein kinase type L FEES Lett 1995; 362: 291-4.
152. Correll LA, Woodford TA, Corbin JD, et al. Functional characterization of cAMP-binding mutations in type I protein kinase. J Biol Chem 1989; 264: 16672-78.
153. Ogreid D, Doskeland SO, Gorman KG, et al. Mutations that prevent cyclic nucleotide binding to binding sites A or B of type I cAMP-dependent protein kinase. J Biol Chem 1988; 263: 17397-404.
154. Shabb JB, Buzzeo BD, Ng L, et al. Mutating protein kinase cAMP-binding sites into cGMP-binding sites. J Biol Chem 1991; 266: 24320-26.
155. Zom M, Fladmark KE, Ogreid D, et al. Ala 335 is essential for high-affinity cAMP-binding of both sites A and B of cAMP-dependent protein kinase type I. FEBS Lett 1995; 362: 291-294
156. Dostmann WR, Taylor SS. Identifying the molecular switches that determine whether (Rp)-cAMPS functions as an antagonist or an agonist in the activation of cAMP-dependent. protein kinase I. Biochemistry 1991; 30: 8710-16.
157. Gjertsen BT, Mellgren G, Otten A, et al. Novel (Rp)-cAMPS analogs as tools for inhibition of cAMP kinase in cell culture. Basal cAMP-kinase activity modulates interleukin-1 beta action. J Biol Chem 1995; 270: 20599-607.
158. de Rooij J, Zwartkruis FJ, Verheijen MH, et al. Epac is a Rapl guanine-nucleotide-exchange factor directly activated by cyclic AMP. Nature 1998; 396: 474-77.
159. Kawasaki H, Springett CM, Mochizuki N, et al. A family of cAMP-binding proteins that directly activate Rapl. Science 1998; 282: 2275-79.
160. Jiang H, Colbran JL, Francis SH, et al. Direct evidence for cross-activation of cGMP-dependent protein kinase by cAMP in pig coronary arteries. J Biol Chem 1992; 267: 1015-19.
161. 2+ in vertebrate photoreceptor excitation and adaptation. Annu Rev Physiol 1992; 54: 153-75.
162. Ludwig J, Margalit T, Eismann E, et al. Primary structure of cAMP-gated channel from bovine olfactory epithelium. FEBS Lett 1990; 270: 24-29.
163. Hardman JG. Cyclic nucleotides and regulation of vascular smooth muscle. J Cardiovasc Pharmacol 1984; 6: 5639-45.
164. Ignarro LJ, Kadowitz PJ. The pharmacological and physiological role of cGMP in vascular smooth muscle relaxation. Annu Rev Pharmacol Toxicol 1985; 25: 171-91.
165. Smith JA, Francis SH, Walsh KA, et al. Autophosphorylation of type Iβ cGMP-dependent protein kinase increases basal catalytic activity and enhances allosteric activation by cGMP or cAMP. J Biol Chem 1996; 271: 20756-62.
166. Francis SH, Noblett BD, Todd BW, et al. Relaxation of vascular and tracheal smooth muscle by cyclic nucleotide analogs that preferentially activate purified cGMP-dependent protein kinase. Mol Pharmacol 1988; 34: 506-17.
167. Reed BB, Sandberg M, Jahnsen T, et al. Fast and slow cyclic nucleotide-dissociation sites in cAMP-dependent protein kinase are transposed in type Iβ cGMP-dependent protein kinase. J Biol Chem 1996; 271: 17570-75.
168. Reed RB, Sandberg M, Jahnsen T, et al. Structural order of the slow and fast intrasubunit cGMP-binding sites of type Iα cGMP-dependent protein kinase. Adv Second Mess Phosphoproteins 1997; 31: 205-17.
169. Eckly-Michel A, Martin V Lugnier C-Involvement of cyclic nucleotide-dependent protein kinases in cyclic AMP-mediated vasorelaxation. Br J Pharm 1997; 122: 158-64.
170. Forte LR, Thorne PK, Eber SL, et al. Stimulation of intestinal CF transport by heat-stable enterotoxin: activation of cAMP-dependem protein kinase by cGMP. Am J Physiol 1992; 263: C607-15.
171. DeJonge HR, Lohmann SM. Mechanisms by which cyclic nucleotides and other intracellular mediators regulate secretion. Ciba Foundation Symposium 1985; 112: 116-38.
172. - channels co-expressed with cGMP-dependent protein kinase type II but not type Iβ. J Biol Chem 1997; 272: 4195-200.
173. Schumacher H, Muller D Mukhopadhyay AK. Stimulation of testosterone production by atrial natriuretic peptide in isolated mouse leydig cells results from a promiscuous activation of cyclic AMP-dependent protein kinase by cyclic GMP. Mol Cell Endocrinol 1992; 90: 47-52
174. Adams MR, Brandon EP Chartoff EH, et al. Loss of haloperidol induced gene expression and catalespy in protein kinase A-deficient mice. Proc Natl Acad Sci USA 1997; 94: 12157-61.
175. Brandon EP, Logue SF, Adams MR, et al. Defective motor behavior and neural gene expression in RIIβ-protein kinase A mutant mice. J Neurosci 1998; 18: 3639-49.
176. Cummings DE, Brandon EP, Planas JV, et al. Genetically lean mice result from targeted disruption of the RIIβ subunit of protein kinase A. Nature 1996; 382: 622-6.
177. Hensch TK, Gordon JA, Brandon EP, et al. Comparison of plasticity in vivo and in vitro in the developing visual cortex of normal and protein kinase A RIβ-deficient mice. J Neurosci 1998; 18: 2108-17.
178. Conti M, Nemoz G, Sette C, et al. Recent progress in understanding the hormonal regulation of PDEs. Endocrinol Rev 1995; 16: 370-389
179. Corbin JD, Beebe SJ Blackmore PF. cAMP-dependent protein kinase activation lowers hepatocyte cAMP. J Biol Chem 1985; 260: 8731-35.
180. Gettys TW, Blackmore PF, Redmon JB, et al. Short-term feedback regulation of cAMP by accelerated degradation in rat tissues. J Biol Chem 1987; 262: 333-39.
181. Loten EG, Sneyd JG. An effect of insulin on adipose tissue adenosine 3′,5′-monophosphate phosphodiesterase, Biochem J 1970; 120: 187-93.
182. Degerman E, Belfrage P Manganiello VC, Structure, localization, and regulation of cG-inhibited PDE (PDE3). J Biol Chem 1997; 272: 6823-6.
183. Sette C, Conti M. Phosphorylation and activation of a cAMP-specific PDE by the cAMP-dependent protein kinase. Involvement of Ser-54 in the enzyme activation. J Biol Chem 1996; 271: 16526-16530.
184. Joyce NC, DeCamilli P, Lohmann SM, et al. cGMP-dependent protein kinase is present in high concentrations in contractile cells of the kidney vasculature. J Cyclic Nucleotide Protein Phosphoryl Res 1986; 11: 191-98.
185. Lohmann SM, Walter U, Miller PE, et al. Immunohistochemical localization of cGMP-dependent protein kinase in mammalian brain. Proc Natl Acad Sci USA 1981; 78: 653-57.
186. Walter U. Distribution of cGMP-dependent protein kinase in various rat tissues and cell lines determined by a sensitive and specific radioimmunoassay. Eur J Biochem 1981; 118: 339-46.
187. DeJonge HR. Cyclic GMP-dependent protein kinase in intestinal brush borders. Adv Cyclic Nucleotide Res 1981; 14: 315-33.
188. Cornwall TL, Pryzwansky KB, Wyatt TA, et al. Regulation of sarcoplasmic reticulum protein phosphorylation by localized cGMP-dependent protein kinase in vascular smooth muscles. Mol Pharmacol 1991; 40: 923-31.
189. Pryzwansky KB, Wyatt TA, Nichols H, et al. Compartmentalization of cGMP-dependent protein kinase in formyl-peptide stimulated neutrophils. Blood 1990; 76: 612-18.
190. Wyatt TA, Lincoln TM Pryzwansky KB. Vimentin is transiently co-localized with and phosphorylated by cGMP-dependent protein kinase in formyl-peptide-stimulated neutrophils. J Biol Chem 1991; 266: 21274-80.
191. Doskeland SO, Vintermyr PK, Corbin JD, et al. Studies on the interactions between the cyclic nucleotide-binding sites of cGMP-dependent protein kinase. J Biol Chem 1987; 262: 3534-40.
192. Lincoln TM, Thompson M Cornwell TL. Purification and characterization of two forms of cGMP-dependent protein kinase from bovine aorta. J Biol Chem 1988; 263: 17632-37.
193. Wolfe L, Corbin JD Francis SH. Characterization of a novel isozyme of cGMP-dependent protein kinase from bovine aorta. J Biol Chem 1989; 264: 7734-41.
194. Wolfe L, Francis SH Corbin JD, Properties of a cGMP-dependent monomeric protein kinase from bovine aorta. J Biol Chem 1989; 264: 4157-62.
195. Francis, SH, Woodford TA, Wolfe L, et al. Types Iα and Iβ isozymes of cGMP dependent protein kinase: alternative mRNA splicing may produce different inhibitory domains. Second Mess Phosphoproteins 1988-89; 12: 301-10.
196. Sandberg M, Natarajan V, Ronander I, et al. Molecular cloning and predicted full-length amino acid sequence of the type Iβ isozyme of cGMP-dependent protein kinase from human placenta. FEBS Lett 1989; 255: 321-29.
197. Wernet W, Flockerzi V Hofmann F. The cDNA of the two isoforms of bovine cGMP-dependent protein kinase. FEBS Lett 1989; 251: 191-6.
198. Uhler MD. Cloning and expression of a novel cyclic GMP-dependent protein kinase from mouse brain. J Biol Chem 1993; 268: 13586-91.
199. Gamm DM, Francis SH, Angelotti TP, et al. The type II isoform of cGMP-dependent protein kinase is dimeric and possesses regulatory and catalytic properties distinct from the type I isoforms. J Biol Chem 1995; 270: 27380-8.
200. Jarchau T, Hausler C, Markert T, et al. Cloning, expression, and in situ localization of rat intestinal cGMP-dependent protein kinase II. Proc Natl Acad Sci USA 1994; 91: 9426-30.
201. Witczak O, Orstavik S, Natarajan V, et al. Characterization of the gene encoding the human type II cGMP-dependent protein kinase. Biochem Biophys Res Commun 1998; 245: 113-9.
202. Vaandrager AB, Ehlert EME, Jarchau T, et al. N-Terminal myristoylation is required for membrane localization of cGMP-dependent protein kinase type II. J Biol Chem 1996; 271: 7025-29.
203. Corbin JD, Ogreid D, Miller JP, et al. Studies of cGMP analog specificity and function of the two intrasubunit binding sites of cGMP-dependent protein kinase. J Biol Chem 1986; 261: 1208-14.
204. Aitken A, Hemmings B Hofmann F, Identification of residues on cGMP-dependent protein kinase that are autophosphorylated in the presence of cAMP and cGMP. Biochim Biophys Acta 1984; 790: 219-25.
205. Francis SH, Smith JA, Colbran JL, et al. Arginine-75 in the pseudosubstrate sequence of type Iβ cGMP-dependent protein kinase provides for potent autoinhibition, although autophosphorylated Serine-63 is outside this sequence. J Biol Chem 1996; 271: 20748-55.
206. Landgraf W, Hullin R, Gobel C, et al. Phosphorylation of cGMP-dependent protein kinase increases the affinity for cAMP. Eur J Biochem 1986; 154: 113-17.
207. Ruth P, Landgraf W, Keilbach A, et al. The activation of expressed cGMP-dependent protein kinase isozymes Iα and Iβ is determined by the different aminotermini. Eur J Biochem 1991; 202: 1339-44.
208. Ruth P, Pfeifer A, Kamm S, et al. Identification of the amino acid sequences responsible for high affinity activation of cGMP kinase Iα. J Biol Chem 1997; 272: 10522-28.
209. Pfeifer A, Aszodi A, Seidler U, et al. Intestinal secretory defects and dwarfism in mice lacking cGMP-dependent protein kinase II, Science 1996; 274: 2082-6.
210. Sandberg M, Natarajan V, Orstavik S. et al. The human type I cGMP-dependent protein kinase gene. NATO ASI Ser Biol Signal Transduction 1991; H-52: 301-8.
211. Orstavik S, Solberg R Tasken K. Molecular cloning, cDNA structure, and chromosomal localization of the human type II cGMP-dependent protein kinase. Biochem Biophys Res Commun 1996; 220: 759-65
212. Kalderon D, Rubin GM. cGMP-dependent protein kinase genes in Drosophila. J Biol Chem 1989; 264: 10738-48.
213. Landgraf W, Hofmann F, Pelton JT, et al. Effects of cGMP on the secondary structure of cGMP-dependent protein kinase and analysis of the enzyme's amino-terminal domain by far-ultraviolet circular dichroism. Biochemistry 1990; 29: 90921-28.
214. 1H-NMR and circular dichroism studies of the N-terminal domain of cGMP-dependent protein kinase: a leucine/isoleucine zipper. Biochemistry 1991; 30: 9387-95.
215. Monken CE, Gill GN. Structural analysis of cGMP-dependent protein kinase using limited proteolysis. J Biol Chem 1980; 255: 7067-70.
216. Heil WG, Landgraf W Hofmann F. A catalytically active fragment of cGMP-dependent protein kinase: occupation of its cGMP-binding sites does not affect its phosphotransferase activity. Eur J Biochem 1987; 168: 117-21
217. Dostmann WR, Koep N Endres R. The catalytic domain of the cGMP-dependent protein kinase Iα modulates the cGMP-binding characteristics of its regulatory domain. FEBS Lett 1996; 398: 206-10.
218. Bubis J, Vedvick TS Taylor SS. Anti-parallel alignment of the two promoters of the regulatory subunit dimer of cAMP-dependent protein kinase I. J Biol Chem 1987; 262: 14961-66.
219. Hofmann F, Gensheimer H Gobel C. cGMP-dependent protein kinase: autophosphorylation changes the characteristics of binding site 1. Eur J Biochem 1985; 147: 361-65.
220. Smith JA, Francis SH Corbin JD. Autophosphorylation: a salient feature of protein kinases. In: Khandelwal RL, Wang JH, ed. Molecular and cellular biochemistry, reversible protein phosphorylation in cell regulation Vol. 127/128. Pp. 51-70, Dordrecht: Kluwer Academic Publishers, 1993.
221. Chu D-M, Corbin JD, Grimes KA, et al. Activation by cyclic GMP binding causes an apparent conformational change in cGMP-dependent protein kinase. J Biol Chem 1997; 272: 31922-28.
222. Chu D-M, Francis SH, Thomas JW, et al. Activation by autophosphorylation or cGMP binding produces a similar apparent conformational change in cGMP-dependent protein kinase. J Biol Chem 1998; 273; 14649-56.
223. Zhao J, Trewhella J, Corbin J, et al. Progressive cyclic nucleotide-induced conformational changes in the cGMP-dependent protein kinase studied by small-angle X-ray scattering in solution. J Biol Chem 1997; 272: 31929-36.
224. Monod J, Wyman J Changeaux J-P. On the nature of allosteric transitions - a plausible model. J Mol Biol 1965; 12: 88-118.
225. Sekhar KR, Hatchett RJ, Shabb JB, et al. Relaxation of pig coronary arteries by new and potent cGMP analogs that selectively activate type Iα, compared with type Iβ, cGMP-dependent protein kinase. Mol Pharmacol 1992; 42: 103-8.
226. McCune RW, Gill GN. Positive cooperativity in guanosine 3′,5′-monophosphate binding to guanosine 3′,5′- monophosphate-dependent protein kinase. J Biol Chem 1979; 265: 5083-91.
227. Wolfe L, Francis SH Landiss LR, et al. Interconvertible cGMP-free and cGMP-bound forms of cGMP-dependent protein kinase in mammalian tissues. J Biol Chem 1987; 262: 16906-13.
228. Weber FT, Shabb JB Corbin JD. Predicted structure of the cGMP binding domains of the cGMP-dependent protein kinase: a key alanine/threonine difference in evolutionary divergence of cAMP and cGMP binding sites. Biochemistry 1989; 28: 6122-7.
229. Feil R, Kellermann J Hofmann F. Functional cGMP-dependent protein kinase is phosphorylated in its catalytic domain at threonine-516. Biochemistry 1995; 34: 13152-58
230. Thomas MK, Francis SH Corbin JD. Substrate- and kinase-directed regulation of phosphorylation of a cGMP-binding phosphodiesterase by cGMP. J Biol Chem 1990; 265: 14971-78.
231. Wyatt TA, Naftilan AJ, Francis SH, et al. ANF elicits phosphorylation of the cGMP phosphodiesterase (PDE5) in vascular smooth muscle cells. Am J Physiol 1997; 273: H448-55.
232. Waldmann R, Nieberding M Walter U. Vasodilator-stimulated protein phosphorylation in platelets is mediated by cAMP- and cGMP-dependent protein kinases. Eur J Biochem 1987; 167: 441-8.
233. Geahlen RL, Krebs EG. Regulatory subunit of the type I cAMP-dependent protein kinase as an inhibitor and substrate of the cGMP-dependent protein kinase. J Biol Chem 1980; 255: 1164-69.
234. Aswad DW, Greengard P. A specific substrate from rabbit cerebellum for guanosine 3′,5′-monophosphate-dependent protein kinase: purification and characterization. J Biol Chem 1981; 256: 3487-93.
235. Schlichter DJ, Casnellie JE Greengard P. An endogenous substrate for cGMP-dependent protein kinase in mammalian cerebellum. Nature 1978; 273: 61-62.
236. Tegge W, Frank R, Hofmann F, et al. Determination of cyclic nucleotide-dependent protein kinase substrate specificity by the use of peptide libraries on cellulose paper. Biochemistry 1995; 34: 10569-77.
237. Yan X, Corbin JD, Francis SH, et al. Precision targeting of protein kinases. An affinity label that inactivates the cGMP- but not the cAMP-dependent protein kinase. J Biol Chem 1996; 271: 1845-8.
238. Yan X, Lawrence DS, Corbin JD, et al. Distinguishing between closely related protein kinases: a variation on the bisubstrate inhibition theme. J Am Chem Soc 1996; 118: 6321-2.
239. Wood JS, Yan X, Mendelow M, et al. Precision substrate targeting of protein kinases. The cGMP- and cAMP-dependent protein kinases. J Biol Chem 1996; 271: 174-9.
240. Pfeifer A, Klatt P, Massberg S, et al. Defective smooth muscle regulation in cGMP kinase I-deficient mice. EMBO J 1998; 17: 3045-51.
241. Fiscus RP, Rapoport RM Murad F. Atriopeptin II elevates cGMP, activates cGMP-dependent protein kinase and causes relaxation in rat thorax aorta. Biochem Biophys Acta 1984; 846: 179-84.
242. Rapoport RM, Dragnin MB Murad F. Endothelium-dependent protein phosphorylation. Nature 1983; 306: 174-76.
243. Ballard SA, Gingell CJ, Tang K, et al. Effects of sildenafil on the relaxation of human corpus cavernosuum tissue in vitro and on the activities of cyclic nucleotide phosphodiesterase isozymes. J Urol 1998; 159: 2164-71.
244. Baltensperger K, Chiesi M Carafoli E. Substrates of cGMP kinase in vascular smooth muscle and their role in the relaxation process. Biochemistry 1990; 29: 9753-60.
245. Patel AI, Diamond J. Activation of guanosine 3′,5′-cyclic monophosphate (cGMP)-dependent protein kinase in rabbit aorta by nitroglycerin and sodium nitroprusside. J Pharmacol Exp Ther 1997; 283: 885-93.
246. Deliconstantinos G, Villotiou V, Stavrides JC. Inhibition of ultraviolet B-induced skin erythema by N-nitro-L-arginine and N-monomethyl-L-arginine. J Dermatological Sci 1997; 15: 23-35.
247. 2+ by cAMP in vascular smooth muscle cells. Am J Physiol 1990; 258: C399-497.
248. Dey NB, Boerth NJ, Murphy-Ullrich JE, et al. Cyclic GMP-dependent protein kinase inhibits osteopontin and thrombospondin production in rat aortic smooth muscle cells. Circ Res 1998; 82: 139-46.
249. Nolte C, Eigenthaler M, Schanzenbacher P, et al. Endothelial cell-dependent phosphorylation of a platelet protein mediated by cAMP- and cGMP-elevating factors. J Biol Chem 1991; 266: 14808-12.
250. Geiger J, Nolte C, Butt E, et al. Role of cGMP and cGMP-dependent protein kinase in nitrovasodilator inhibition of agonist-evoked calcium elevation in human platelets. Proc Natl Acad Sci USA 1992; 89: 1031-35.
251. Halbrugge M, Freidrich C, Eigenthaler M, et al. Stoichiometric and reversible phosphorylation of a 46-kDa protein in human platelets in response to cGMP- and cAMP-elevating vasodilators. J Biol Chem 1990; 265: 3088-93.
252. 2+ levels in cultured vascular smooth muscle cells. J Biol Chem 1989; 264: 1146-55.
253. Raeymaekers L, Hofmann F Casteels R. Cyclic GMP-dependent protein kinase phosphorylates phospholamban in isolated sarcoplasmic reticulum from cardiac and smooth muscle. Biochem J 1988; 252: 269-73.
254. Hirata M, Kohse KP, Chang C, et al. Mechanism of cGMP inhibition of inositol phosphate formation in rat aorta segments and cultured bovine aortic smooth muscle cells. J Biol Chem 1990; 265: 1268-73.
255. Johansson JS, Haynes DH, Cyclic GMP increases the rate of the calcium extrusion pump in intact human platelets but has no direct effect on the dense tubular calcium accumulation system. Biochim Biophys Acta 1992; 1105: 40-50.
256. Lohmann SM, Fischmeister R Walter U. Signal transduction by cGMP in heart. Basic Res Cardiol 1991; 86: 503-14.
257. Ives HE, Casnellie JE, Greengard P, et al. Subcellular localization of cGMP-dependent protein kinase and its substrates in vascular smooth muscle. J Biol Chem 1980; 255: 3777-85.
258. Huggins, JP, Cook EA, Piggott JR, et al. Phospholamban is a good substrate for cGMP-dependent protein kinase in vitro, but not in intact cardiac or smooth muscle. Biochem J 1989; 260: 829-35
259. 2+ ATPase by cGMP-dependent protein kinase. Proc Natl Acad Sci USA 1987; 84: 5685-89.
260. 2+ pump ATPase of vascular smooth muscle via phosphorylation of a 240-kDa protein. J Biol Chem 1991; 266: 19819-25.
261. 2+ current is regulated by cGMP-dependent protein kinase in mammalian cardiac myocytes. Proc Natl Acad Sci USA 1991; 88: 1197-201.
262. Light DB, Corbin JD Stanton BA. Dual ion-channel regulation by cGMP and cGMP-dependent protein kinase. Nature 1990; 344: 336-39.
263. White RE, Lee AB, Shcherbatko AD, et al. Potassium channel stimulation by natriuretic peptides through cGMP-dependent dephosphorylation. Nature 1993; 361: 263-5.
264. Van Epps-Fung C, Williams JP, Cornwell TL, et al. Regulation of osteoclastic acid secretion by cGMP-dependent protein kinase. Biochem Biophys Res Commun 1994; 204: 565-71.
265. Roczniak A, Burns KD. Nitric oxide stimulates guanylyl cyclase and regulates sodium transport in rabbit proximal tubule. Am J Physiol 1996; 270: F106-15.
266. + channels in the basolateral membranes of rat cortical collecting duct are regulated by a cGMP-dependent protein kinase. Pflugers Arch-Eur J Physiol 1995; 429: 338-44.
267. Gambaryan S, Hausler C, Markert T, et al. Expression of type II cGMP-dependent protein kinase in rat kidney is regulated by dehydration and correlated with renin gene expression. J Clin Invest 1996; 98: 662-70.
268. Romero-Graillet C, Aberdam E, Biagoli N, et al. Ultraviolet B radiation acts through the nitric oxide and cGMP signal transduction pathway to stimulate melanogenesis in human melanocytes. J Biol Chem 1996; 271: 28052-56.
269. Beavo JA. Multiple isoenzymes of cyclic nucleotide phosphodiesterase. Adv Second Mess Phosphoprotein Res 1988; 11: 1-38.