Phosphorylation and Dephosphorylation of Glycogen Phosphorylase: A Prototype for Reversible Covalent Enzyme Modification

Current Topics in Cellular Regulation

Volumn 18, Issue C, 1981, Pages 401-419

  Krebs, Edwin G ^a  

^a UNIVERSITY OF WASHINGTON SCHOOL OF MEDICINE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CALCIUM; CYCLIC AMP; PHOSPHOPROTEIN PHOSPHATASE; PHOSPHORYLASE; PHOSPHORYLASE KINASE; PHOSPHORYLASE PHOSPHATASE; PROTEIN KINASE;

AMINO ACID SEQUENCE; ANIMAL; ARTICLE; ENZYME SPECIFICITY; KINETICS; METABOLISM; PHOSPHORYLATION;

AMINO ACID SEQUENCE; ANIMALS; CALCIUM; CYCLIC AMP; KINETICS; PHOSPHOPROTEIN PHOSPHATASE; PHOSPHORYLASE KINASE; PHOSPHORYLASE PHOSPHATASE; PHOSPHORYLASES; PHOSPHORYLATION; PROTEIN KINASES; SUBSTRATE SPECIFICITY;

EID: 0019376924     PISSN: 00702137     EISSN: None     Source Type: Book Series    
DOI: 10.1016/B978-0-12-152818-8.50030-X     Document Type: Chapter

References (105)

1. Cori, G.T., Green, A.A., J. Biol. Chem. 151 (1943), 31–38.
2. Cori, G.T., Cori, C.B., J. Biol. Chem. 158 (1945), 321–332.
3. Cori, G.T., J. Biol. Chem. 158 (1945), 333–339.
4. Sutherland, E.W. Jr., Wosilait, W.D., Nature (London) 175 (1955), 169–171.
5. Rall, T.W., Sutherland, E.W., Wosilait, W.D., J. Biol. Chem. 218 (1956), 483–495.
6. Fischer, E.H., Krebs, E.G., J. Biol. Chem. 216 (1955), 121–132.
7. Krebs, E.G., Kent, A.B., Fischer, E.H., J. Biol. Chem. 231 (1958), 73–83.
8. Harris, D.L., J. Biol. Chem. 165 (1946), 541–550.
9. Feinstein, R.N., Volk, M.E., J. Biol. Chem. 177 (1949), 339–346.
10. Burnett, B., Kennedy, E.P., J. Biol. Chem. 211 (1954), 969–980.
11. Krebs, E.G., Graves, D.J., Fischer, E.H., J. Biol. Chem. 234 (1959), 2867–2873.
12. Friedman, D.L., Larner, J., Biochemistry 2 (1963), 669–675.
13. Rizack, M.A., J. Biol. Chem. 239 (1964), 392–395.
14. Corbin, J.C., Reimann, E.M., Walsh, D.A., Krebs, E.G., J. Biol. Chem. 245 (1970), 4849–4851.
15. Huttunen, J.K., Steinberg, D., Mayer, S.E., Proc. Natl. Acad. Sci. U.S.A. 67 (1970), 290–295.
16. Mendicino, J., Beaudreau, C., Bhattacharyya, R.N., Arch. Biochem. Biophys. 116 (1966), 436–445.
17. Riou, J.P., Claus, T.H., Flockhart, D.A., Corbin, J.D., Pilkis, S.J., Proc. Natl. Acad. Sci. U.S.A. 74 (1977), 4615–4619.
18. Linn, T.C., Pettit, F.H., Reed, L.J., Proc. Natl. Acad. Sci. U.S.A. 62 (1969), 234–241.
19. Beg, Z.H., Allmann, D.W., Gibson, D.M., Biochem. Biophys. Res. Commun. 54 (1973), 1362–1369.
20. 19a Ingebritsen, T.S., Lee, H.-S., Parker, R.A., Gibson, D.M., Biochem. Biophys. Res. Commun. 81 (1978), 1268–1277.
21. Perrie, W.T., Smillie, L.B., Perry, S.V., Biochem. J. 135 (1973), 151–164.
22. Carlson, C.A., Kim, K.H., J. Biol. Chem. 248 (1973), 378–380.
23. Martelo, O.J., Huijing, F., Lee, E.Y.C., (eds.) “Protein Phosphorylation in Control Mechanisms, Miami Winter Symposium”, 1973, Academic Press, New York, 199–216.
24. Ljungström, O., Hjelmquist, G., Engström, L., Biochim. Biophys. Acta 358 (1974), 289–298.
25. Trzeciak, W.H., Boyd, G.S., Eur. J. Biochem. 46 (1974), 201–207.
26. Erlichman, J., Rosenfeld, R., Rosen, O.M., J. Biol. Chem. 249 (1974), 5000–5003.
27. Brand, I.A., Söling, H.D., FEBS Lett. 57 (1975), 163–168.
28. Morgenroth, V.H. III, Hegstrand, L.R., Roth, R.H., Greengard, P., J. Biol. Chem. 250 (1975), 1946–1948.
29. Milstien, S., Abita, J.P., Chang, N., Kaufman, S., Proc. Natl. Acad. Sci. U.S.A. 73 (1976), 1591–1593.
30. Farrell, P.J., Balkow, K., Hunt, T., Jackson, J.J., Trachsel, H., Cell 11 (1977), 187–200.
31. Bechtel, P.J., Beavo, J.A., Krebs, E.G., J. Biol. Chem. 252 (1977), 2691–2697.
32. de Jonge, H.R., Rosen, O.M., J. Biol. Chem. 252 (1977), 2780–2783.
33. Hamon, M., Bourgoin, S., Artaud, F., Héry, F., J. Neurochem. 28 (1977), 811–818.
34. Steinberg, R.A., O'Farrell, P.H., Friedrich, U., Coffino, P., Cell 10 (1977), 381–391.
35. Geahlen, R.L., Krebs, E.G., J. Biol. Chem. 255 (1980), 1164–1169.
36. Hemmings, B.A., J. Biol. Chem. 253 (1978), 5255–5258.
37. Nimmo, H.G., Houston, B., Biochem. J. 176 (1978), 607–610.
38. Adelstein, R.S., Conti, M.A., Hathaway, D.R., Klee, C.B., J. Biol. Chem. 253 (1978), 8347–8350.
39. Van Eldick, L.J., Watterson, D.M., Fed. Proc., Fed. Am. Soc. Exp. Biol., 38, 1979, 789.
40. Linn, T.C., Srere, P.A., J. Biol. Chem. 254 (1979), 1691–1698.
41. Guy, P.S., Cohen, P., Hardie, D.G., FEBS Lett. 109 (1980), 205–208.
42. Rose, K.M., Jacob, S.T., J. Biol. Chem. 254 (1979), 10256–10261.
43. Garnak, M., Reeves, H.C., Science 203 (1979), 1111–1112.
44. Titani, K., Koide, A., Hermann, J., Ericsson, L.H., Kumar, S., Wade, R.D., Walsh, K.A., Neurath, H., Fischer, E.H., Proc. Natl. Acad. Sci. U.S.A. 74 (1977), 4762–4766.
45. Graves, D.J., Wang, J.H., The Enzymes 7 (1972), 435–482.
46. Johnson, L.N., Weber, I.T., Wild, D.L., Wilson, K.S., Yeates, D., Esmann, V., (eds.) “Regulatory Mechanisms of Carbohydrate Metabolism”, 1978, Pergamon Press, Oxford, 185–194.
47. Fletterick, R.J., Madsen, N.B., Ann Rev. Biochem. 49 (1980), 31–61.
48. Yeaman, S.J., Hutcheson, E.T., Roche, T.E., Pettit, F.H., Brown, J.R., Reed, L.J., Watson, D.C., Dixon, G.H., Biochemistry 17 (1978), 2364–2370.
49. Soderling, T.R., Mol. Cell. Endocrinol. 16 (1979), 157–179.
50. Cohen, P., Antoniw, J.F., FEBS Lett. 34 (1973), 43–47.
51. Sugden, P.H., Hutson, N.J., Kerbey, A.L., Randle, P.J., Biochem. J. 169 (1978), 433–435.
52. Krebs, E.G., DeLange, R.J., Kemp, R.G., Riley, W.D., Pharmacol. Rev. 18 (1966), 163–171.
53. Walsh, D.A., Perkins, J.P., Krebs, E.G., J. Biol. Chem. 243 (1968), 3763–3765.
54. Graves, D.J., Fischer, E.H., Krebs, E.G., J. Biol. Chem. 235 (1960), 805–809.
55. Fischer, E.H., Hurd, S.S., Koh, P., Teller, D., Natl. Cancer Inst. Monogr. 27 (1967), 47–59.
56. Fischer, E.H., Krebs, E.G., Fed. Proc., Fed. Am. Soc. Exp. Biol. 25 (1966), 1511–1520.
57. Krebs, E.G., Love, D.S., Bratvold, G.E., Trayser, K.A., Meyer, W.L., Fischer, E.H., Biochemistry 3 (1964), 1022–1033.
58. Sutherland, E.W., McElroy, W.D., Glass, G., (eds.) “Phosphorus Metabolism”, 1951, Johns Hopkins Press, Baltimore, 53–61.
59. Nolan, C., Novoa, W.B., Krebs, E.G., Fischer, E.H., Biochemistry 3 (1964), 542–551.
60. Martensen, T.M., Brotherton, J.E., Graves, D.J., J. Biol. Chem. 248 (1973), 8323–8328.
61. Bot, G., Dósa, I., Acta Biochim. Biophys. Acad. Sci. Hung. 6 (1971), 73–87.
62. Holmes, P.A., Mansour, T.E., Biochim. Biophys. Acta 156 (1968), 275–284.
63. Martensen, T.M., Brotherton, J.E., Graves, D.J., J. Biol. Chem. 248 (1973), 8239–8336.
64. Haschke, R.H., Heilmeyer, L.M.G. Jr., Meyer, F., Fischer, E.H., J. Biol. Chem. 245 (1970), 6657–6663.
65. Nakai, C., Thomas, J.A., J. Biol. Chem. 249 (1974), 6459–6467.
66. Kato, K., Bishop, J.S., J. Biol. Chem. 247 (1972), 7420–7429.
67. Yeaman, S.J., Hutcheson, H.T., Roche, T.E., Pettit, F.H., Brown, J.R., Reed, L.J., Watson, D.C., Dixon, G.H., Biochemistry 17 (1978), 2364–2370.
68. Claus, T.H., El-Maghrabi, M.R., Pilkis, S.J., J. Biol. Chem. 254 (1979), 7855–7864.
69. El-Maghrabi, M.R., Haston, W.S., Flockhart, F., Claus, T.H., Pilkis, S.J., J. Biol. Chem. 255 (1980), 668–675.
70. Cohen, P., Burchell, A., Foulkes, J.G., Cohen, P.T.W., Vanaman, T.C., Nairn, A.C., FEBS Lett. 92 (1978), 287–293.
71. Meyer, W.L., Fischer, E.H., Krebs, E.G., Biochemistry 3 (1964), 1033–1039.
72. Ozawa, E., Hosoi, K., Ebashi, S., J. Biochem. 61 (1967), 531–533.
73. Posner, J.B., Stern, R., Krebs, E.G., J. Biol. Chem. 240 (1964), 982–985.
74. Krebs, E.G., Beavo, J.A., Ann. Rev. Biochem. 48 (1979), 923–959.
75. Blackmore, P.F., Dehaye, J.P., Exton, J.H., J. Biol. Chem. 254 (1979), 6945–6950.
76. Roach, P.J., DePaoli-Roach, A.A., Larner, J., J. Cyclic Nucleotide Res. 4 (1978), 245–257.
77. Rylatt, D.B., Cohen, P., FEBS Lett. 98 (1979), 71–75.
78. Pires, E., Perry, S.V., Thomas, M.A.W., FEBS Lett. 41 (1974), 292–296.
79. Walsh, D.A., Krebs, E.G., Reimann, E.M., Brostrom, M.A., Corbin, J.D., Hicken-bottom, J.P., Soderling, T.R., Perkins, J.P., Adv. Biochem. Psychopharmacol. 3 (1970), 265–285.
80. Krebs, E.G., Preiss, J., MTP Int. Rev. Sci. Biochem. Ser. One 5 (1976), 337–389.
81. Nimmo, H.G., Cohen, P., Adv. Cyclic Nucleotide Res. 8 (1977), 145–266.
82. Walsh, D.A., Cooper, R.H., Biochem. Actions Horm. 6 (1979), 1–75.
83. Cohen, P., Eur. J. Biochem. 34 (1973), 1–14.
84. Hayakawa, T., Perkins, J.P., Walsh, D.A., Krebs, E.G., Biochemistry 12 (1973), 367–373.
85. Hayakawa, T., Perkins, J.P., Krebs, E.G., Biochemistry 12 (1973), 574–580.
86. McCullough, T.E., Walsh, D.A., J. Biol. Chem. 254 (1979), 7345–7352.
87. Huang, F.L., Glinsmann, W.H., Proc. Natl. Acad. Sci. U.S.A. 72 (1975), 3004–3008.
88. Huang, F.L., Glinsmann, W.H., FEBS Lett. 62 (1976), 326–329.
89. Nimmo, G.A., Cohen, P., Eur. J. Biochem. 87 (1978), 353–365.
90. Nakai, C., Glinsmann, W., Mol. Cell. Biochem. 15 (1977), 133–139.
91. Ingebritsen, T.S., Lee, H.S., Parker, R.A., Gibson, D.M., Biochem. Biophys. Res. Commun. 81 (1978), 1268–1277.
92. DeLange, R.J., Kemp, R.G., Riley, W.D., Cooper, R.A., Krebs, E.G., J. Biol. Chem. 243 (1978), 2200–2208.
93. Stull, J.T., Brostrom, C.O., Krebs, E.G., J. Biol. Chem. 247 (1972), 5272–5274.
94. Perry, S.V., Cole, H.A., Biochem. J. 141 (1974), 733–743.
95. Krebs, E.G., Beavo, J.A., Bechtel, P.J., England, P.J., Huang, T.S., Stull, J.T., “Exploratory Concepts in Muscular Dystrophy II,”, 1974, Excerpta Medica, Amsterdam, 431–447.
96. Stull, J.T., Adv. Cyclic Nucleotide Res. 13 (1980), 39–93.
97. Krebs, E.G., Stull, J.T., England, P.J., Huang, T.S., Brostrom, C.O., Vandenheede, J.R., Miami Winter Symp. 5 (1973), 31–45.
98. Huang, T.S., Bylund, D.B., Stull, J.T., Krebs, E.G., FEBS Lett. 42 (1974), 249–252.
99. Tan, A.W.H., Nuttall, F.Q., Biochim. Biophys. Acta 522 (1978), 139–150.
100. Laloux, M., Stalmans, W., Hers, H.G., Eur. J. Biochem. 92 (1978), 15–24.
101. Mellgren, R.L., Aylward, J.H., Killilea, S.D., Lee, E.Y.C., J. Biol. Chem. 254 (1979), 648–652.
102. Brandt, H., Capulong, Z.L., Lee, E.Y.C., J. Biol. Chem. 250 (1975), 8038–8044.
103. Gratecos, D., Detwiler, T.C., Hurd, S., Fischer, E.H., Biochemistry 16 (1977), 4812–4817.
104. Khandelwal, R.L., Vandenheede, J.R., Krebs, E.G., J. Biol. Chem. 251 (1976), 4850–4858.
105. Li, H.C., Hsiao, K.J., Sampathkumar, S., J. Biol. Chem. 254 (1979), 3368–3374.