Glucose repression/derepression in budding yeast: SNF1 protein kinase is activated by phosphorylation under derepressing conditions, and this correlates with a high AMP:ATP ratio

Current Biology

Volumn 6, Issue 11, 1996, Pages 1426-1434

  Wilson, Wayne A ^a,b   Hawley, Simon A ^a   Hardie, D Grahame ^a  

^a UNIVERSITY OF DUNDEE   (United Kingdom)

^b INDIANA UNIVERSITY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

EID: 0030293885     PISSN: 09609822     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0960-9822(96)00747-6     Document Type: Article

References (43)

1. Ronne H: Glucose repression in fungi. Trends Genet 1995, 11:12-17.
2. Gancedo JM: Carbon catabolite repression in yeast. Eur J Biochem 1992, 206:297-313.
3. Ciriacy M: Isolation and characterization of yeast mutants defective in intermediary carbon metabolism and in carbon catabolite repression. Mol Gen Genet 1977, 154:213-220.
4. Zimmermann FK, Kaufmann I, Rasenberger H, Haussman P: Genetics of carbon catabolite repression in Saccharomyces cerevisiae: genes involved in the derepression process. Mol Gen Genet 1977, 1951:95-103.
5. Carlson M, Osmond BC, Botstein D: Mutants of yeast defective in sucrose utilization. Genetics 1981, 98:25-40.
6. Celenza JL, Carlson M: A yeast gene that is essential for release from glucose repression encodes a protein kinase. Science 1986, 233:1175-1180.
7. Muranaka T, Banno H, Machida Y: Characterization of tobacco protein kinase NPK5, a homolog of Saccharomyces cerevisiae SNF1 that constitutively activates expression of the glucose-repressible SUC2 gene for a secreted invertase of S. cerevisiae. Mol Cell Biol 1994, 14:2958-2965.
8. Alderson A, Sabelli PA, Dickinson JR, Cole D, Richardson M, Kreis M, et al.: Complementation of snf1, a mutation affecting global regulation of carbon metabolism in yeast, by a plant protein kinase cDNA. Proc Natl Acad Sci USA 1991, 88:8602-8605.
9. Schuller HJ, Entian KD: Molecular characterization of yeast regulatory gene CATS necessary for glucose derepression and nuclear localization of its product. Gene 1988, 67:247-257.
10. Woods A, Munday MR, Scott J, Yang X, Carlson M, Carling D: Yeast SNF1 is functionally related to mammalian AMP-activated protein kinase and regulates acetyl-CoA carboxylase in vivo. J Biol Chem 1994, 269:19509-19515.
11. Celenza JL, Carlson M: Mutational analysis of the Saccharomyces cerevisiae SNF1 protein kinase and evidence for functional interaction with the SNF4 protein. Mol Cell Biol 1989, 9:5034-5044.
12. Celenza JL, Eng FJ, Carlson M: Molecular analysis of the SNF4 gene of Saccharomyces cerevisiae: evidence for physical association of the SNF4 protein with the SNF1 protein kinase. Mol Cell Biol 1989, 9:5045-5054.
13. Estruch F, Treitel MA, Yang X, Carlson M: N-terminal mutations modulate yeast SNF1 protein kinase function. Genetics 1992, 132:639-650.
14. Fields S, Song OK: A novel genetic system to detect protein-protein interactions. Nature 1989, 340:245-246.
15. Yang X, Jiang R, Carlson M: A family of proteins containing a conserved domain that mediates interaction with the yeast SNF1 protein kinase complex. EMBO J 1994, 13:5878-5886.
16. Mitchelhill KI, Stapleton D, Gao G, House C, Michell B, Katsis F, et al.: Mammalian AMP-activated protein kinase shares structural and functional homology with the catalytic domain of yeast Snf1 protein kinase. J Biol Chem 1994, 269:2361-2364.
17. Carling D, Aguan K, Woods A, Verhoeven AJM, Beri RK, Brennan CH, et al:. Mammalian AMP-activated protein kinase is homologous to yeast and plant protein kinases involved in the regulation of carbon metabolism. J Biol Chem 1994, 269:11442-11 448.
18. Hardie DG, Carling D, Halford NG: Roles of the Snf1/Rkin1/AMP-activated protein kinase family in the response to environmental and nutritional stress. Semin Cell Biol 1994, 5:409-416.
19. Corton JM, Gillespie JG, Hardie DG: Role of the AMP-activated protein kinase in the cellular stress response. Curr Biol 1994, 4:315-324.
20. Carling D, Clarke PR, Zammit VA, Hardie DG: Purification and characterization of the AMP-activated protein kinase. Copurification of acetyl-CoA carboxylase kinase and 3-hydroxy-3-methylglutaryl-CoA reductase kinase activities. Eur J Biochem 1989, 186:129-136.
21. Ferrer A, Caelles C, Massot N, Hegardt FG: Activation of rat liver cytosolic 3-hydroxy-3-methylglutaryl coenzyme A reductase kinase by adenosine 5′-monophosphate. Biochem Biophys Res Comm1985, 132:497-504.
22. 2+/calmodulin the calmodulin-dependent protein kinase I cascade, via three independent mechanisms. J Biol Chem 1995, 270:27186-27191.
23. Davies SP, Helps NR, Cohen PTW, Hardie DG: 5′-AMP inhibits dephosphorylation, as well as promoting phosphorylation, of the AMP-activated protein kinase. Studies using bacterially expressed human protein phosphatase-2Cα and native bovine protein phosphatase-2AC. FEBS Lett 1995, 377:421-425.
24. Davies SP, Hawley SA, Woods A, Carling D, Haystead TAJ, Hardie DG: Purification of the AMP-activated protein kinase on ATP-γ-Sepharose and analysis of its subunit structure. Eur J Biochem 1994, 223:351-357.
25. Gao G, Fernandez S, Stapleton D, Auster AS, Widmer J, Dyck. JRB, et al:. Non-catalytic β- and γ-subunit isoforms of the 5′-AMP-activated protein kinase. J Biol Chem 1996, 271:8675-8681.
26. Woods A, Cheung PCF, Smith FC, Davison MD, Scott J, Beri RK, Carling D: Characterization of AMP-activated protein kinase β and γ subunits: assembly of the heterotrimeric complex in vitro. J Biol Chem 1996, 271:10282-10290.
27. Gao G, Widmer J, Stapleton D, Teh T, Cox T, Kemp BE, Witters LA: Catalytic subunits of the porcine and rat 5′-AMP-activated protein kinase are members of the SNF1 protein kinase family. Biochim Biophys Acta 1995, 1266:73-82.
28. Dale S, Wilson WA, Edelman AM, Hardie DG: Similar substrate recognition motifs for mammalian AMP-activated protein kinase, higher plant HMG-CoA reductase kinase-A, yeast SNF1, and mammalian calmodulin-dependent protein kinase I. FEBS Lett 1995, 361:191-195.
29. Davies SP, Sim ATR, Hardie DG: Location and function of three sites phosphorylated on rat acetyl-CoA carboxylase by the AMP-activated protein kinase. Eur J Biochem 1990, 187:183-190.
30. Davies SP, Carling D, Hardie DG: Tissue distribution of the AMP-activated protein kinase, and lack of activation by cyclic AMP-dependent protein kinase, studied using a specific and sensitive peptide assay. Eur J Biochem 1989, 186:123-128.
31. Hawley SA, Davison M, Woods A, Davies SP, Beri RK, Carling D, Hardie DG: Characterization of the AMP-activated protein kinase kinase from rat liver, and identification of threonine-172 as the major site at which it phosphorylates and activates AMP-activated protein kinase. J Biol Chem 1996, in press.
32. Johnson LN, Noble MEM, Owen DJ: Active and inactive protein kinases: structural basis for regulation. Cell 1996, 85:149-158.
33. Davies SP, Carling D, Munday MR, Hardie DG: Diurnal rhythm of phosphorylation of rat liver acetyl-CoA carboxylase by the AMP-activated protein kinase, demonstrated using freeze-clamping. Effects of high fat diets. Eur J Biochem 1991, 203:615-623.
34. Entian KD: Genetic and biochemical evidence for hexokinase PII as a key enzyme involved in carbon catabolite repression in yeast. Mol Gen Genet 1980, 178:633-637.
35. Rose M, Albig WKDE: Glucose repression in Saccharomyces cerevisiae is directly associated with hexose phosphorylation by hexokinases PI and PII. Eur J Biochem 1991, 199:511-518.
36. Witt I, Kronau R, Holzer H: Repression von alkoholdehydrogenase, malatdehydrogenase, isocitratlyase und malatsynthase in hefe durch glucose. Biochim Biophys Acta 1966, 118:522-537.
37. Gancedo C, Gancedo M: Phosphorylation of 3-O-methyl-D-glucose and catabolite repression in yeast. Eur J Biochem 1985, 148:593-597.
38. Nehlin JO, Ronne H: Yeast MIG1 repressor is related to the mammalian early growth response and Wilms' tumour finger proteins. EMBO J 1990, 9:2891-2898.
39. Treitel MA, Carlson M: Repression by SSN6-TUP1 is directed by MIG1, a repressor/activator protein. Proc Natl Acad Sci USA 1995, 92:3132-3136.
40. Alessi DR, Street AJ, Cohen P, Cohen PTW: Inhibitor-2 functions like a chaperone to fold 3 expressed isoforms of mammalian protein phosphatase-1 into a conformation with the specificity and regulatory properties of the native enzyme. Eur J Biochem 1993, 213:1055-1066.
41. Cohen P, Alemany S, Hemmings BA, Resink. TJ, Strålfors P, Lim TH: Protein phosphatase-1 and protein phosphatase-2A from rabbit skeletal muscle. Methods Enzymol 1988, 159:390-408.
42. 2+-dependent enzyme. Methods Enzymol 1988, 159:416-426.
43. Bradford MM: A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 1976, 72:248-254.