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PFK2  -  6-phosphofructokinase subunit beta

Saccharomyces cerevisiae S288c

Synonyms: ATP-PFK, ATP-dependent 6-phosphofructokinase, ATP-dependent 6-phosphofructokinase subunit beta, Phosphofructokinase 2, Phosphohexokinase, ...
 
 
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High impact information on PFK2

  • A stimulation of the HOG-MAPK pathway by increasing the medium osmolarity through addition of salt or glucose to cultivated yeast leads to an activation of 6-phosphofructo-2-kinase (PFK2), which is accompanied by a complex phosphorylation pattern of the enzyme [1].
  • In the case of hyperosmolar glucose a 5-fold PFK2 activation was achieved by a single phosphorylation with protein kinase A near the carboxyl terminus of the protein on Ser(644) and an additional 5-fold phosphorylation within the same amino-terminal fragment as in the presence of salt [1].
  • When intracellular glucose-6-P levels were increased by mutating the PFK2 gene, glycogen storage due to the wild-type enzyme was increased, whereas that associated with R579A/R580A/R582A [corrected] was not greatly changed [2].
  • Yeast cells containing PFK2 accumulate three times more glycerol than cells lacking PFK2, which are not able to grow under hypertonic stress [1].
  • The activation of PFK2 leads to an activation of the upper part of glycolysis, which is a precondition for glycerol accumulation [1].
 

Biological context of PFK2

  • By in vitro mutagenesis, we introduced this mutation in either PFK1 or PFK2 and found that the exchange in either subunit drastically reduced the sensitivity of the holoenzyme to ATP inhibition [3].
  • PFK2 was mapped previously to the right arm of chromosome XIII, locating the latter three genes to the same chromosome [4].
  • Interactions between the two phosphofructo-1-kinase subunits PFK1 and PFK2, interactions between the phosphofructo-2-kinase subunits, and dimerization of phosphoglucose isomerase were demonstrated [5].
  • By contrast, like glucose, these agents also caused, under most experimental conditions, a detectable rise in cyclic AMP concentration and a series of cyclic-AMP-dependent effects such as an activation of phosphofructokinase 2 and of trehalase and an increase in the concentration of fructose 2,6-bisphosphate and in the rate of glycolysis [6].
  • Wild-type PFK2 without any tag sequence was found to be acetylated and two times phosphorylated at the N-terminal peptide T(1-40) carrying the acetylation [7].
 

Anatomical context of PFK2

 

Associations of PFK2 with chemical compounds

  • Loss of PFK2 causes elevated levels of metabolites such as glucose-6-P, hyperaccumulation of glycogen, and activation of glycogen synthase, whereas glucose-6-P is reduced in snf1 cells [9].
  • A 'hyper-allosteric' mutant altered in the regulatory subunit encoded by the gene PFK2 showed characteristics of glucose fermentation and ethanol oxidation very similar to those of wild-type organisms [10].
  • Here we provide data demonstrating that an alanine residue at positions 874 (for the PFK1-encoded alpha-subunit) or 868 (for the PFK2-encoded beta-subunit) is crucial to achieve this structure [11].
  • Phosphate also enhances the inactivation of PFK2 by citrate, suggesting that phosphate acts as a regulator of PFK2 [12].
  • Inorganic phosphate also activates PFK2, and the optimum pH for the PFK2 activity varies with the concentration of phosphate [12].
 

Regulatory relationships of PFK2

  • This has been achieved by overexpression of the latter in a PFK-deficient strain of Saccharomyces cerevisiae under the control of the PFK2 promoter [13].
 

Other interactions of PFK2

  • From a genetic screen, we have found that mutation of the PFK2 gene, which encodes the beta-subunit of 6-phosphofructo-1-kinase, restores glycogen accumulation in snf1 cells [9].
  • 6-Phosphofructo-2-kinase (PFK2) is activated by a cAMP-dependent protein kinase, and inactivated by phosphatase, indicating the interconversion of PFK2 [12].
  • The latter is not capable of complementing an icl1 deletion for growth on ethanol neither in its original context, nor when expressed under the control of the glycolytic PFK2 promoter [14].
  • Higher level expression under the control of the yeast PFK2 promoter partially complemented the gpm1 defects, without restoring detectable enzymatic activity [15].
  • Reaction of phosphofructokinase 2/fructose 2,6-bisphosphatase with monoclonal antibodies. A proof of the bifunctionality of the enzyme [16].
 

Analytical, diagnostic and therapeutic context of PFK2

References

  1. High osmolarity glycerol (HOG) pathway-induced phosphorylation and activation of 6-phosphofructo-2-kinase are essential for glycerol accumulation and yeast cell proliferation under hyperosmotic stress. Dihazi, H., Kessler, R., Eschrich, K. J. Biol. Chem. (2004) [Pubmed]
  2. Glycogen synthase sensitivity to glucose-6-P is important for controlling glycogen accumulation in Saccharomyces cerevisiae. Pederson, B.A., Wilson, W.A., Roach, P.J. J. Biol. Chem. (2004) [Pubmed]
  3. Single point mutations in either gene encoding the subunits of the heterooctameric yeast phosphofructokinase abolish allosteric inhibition by ATP. Rodicio, R., Strauss, A., Heinisch, J.J. J. Biol. Chem. (2000) [Pubmed]
  4. PFK2, ISP42, ERG2 and RAD14 are located on the right arm of chromosome XIII. Heinisch, J.J. Yeast (1993) [Pubmed]
  5. A two-hybrid system analysis shows interactions between 6-phosphofructo-1-kinase and 6-phosphofructo-2-kinase but not between other glycolytic enzymes of the yeast Saccharomyces cerevisiae. Müller, S., Boles, E., Zimmermann, F.K. Eur. J. Biochem. (1996) [Pubmed]
  6. The control of glycogen metabolism in yeast. 1. Interconversion in vivo of glycogen synthase and glycogen phosphorylase induced by glucose, a nitrogen source or uncouplers. François, J., Villanueva, M.E., Hers, H.G. Eur. J. Biochem. (1988) [Pubmed]
  7. Lysine 3 acetylation regulates the phosphorylation of yeast 6-phosphofructo-2-kinase under hypo-osmotic stress. Dihazi, H., Kessler, R., Müller, G.A., Eschrich, K. Biol. Chem. (2005) [Pubmed]
  8. Characterization of glucokinase-binding protein epitopes by a phage-displayed peptide library. Identification of 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase as a novel interaction partner. Baltrusch, S., Lenzen, S., Okar, D.A., Lange, A.J., Tiedge, M. J. Biol. Chem. (2001) [Pubmed]
  9. Glucose-6-P control of glycogen synthase phosphorylation in yeast. Huang, D., Wilson, W.A., Roach, P.J. J. Biol. Chem. (1997) [Pubmed]
  10. Mutations in phosphofructokinases alter the control characteristics of glycolysis in vivo in Saccharomyces cerevisiae. Lloyd, D., James, C.J., Maitra, P.K. Yeast (1992) [Pubmed]
  11. A single point mutation leads to an instability of the hetero-octameric structure of yeast phosphofructokinase. Kirchberger, J., Edelmann, A., Kopperschläger, G., Heinisch, J.J. Biochem. J. (1999) [Pubmed]
  12. Activation of yeast 6-phosphofructo-2-kinase by protein kinase and phosphate. Yamashoji, S., Hess, B. FEBS Lett. (1984) [Pubmed]
  13. Functional complementation of yeast phosphofructokinase mutants by the non-allosteric enzyme from Dictyostelium discoideum. Estévez, A.M., Heinisch, J.J., Aragón, J.J. FEBS Lett. (1995) [Pubmed]
  14. Molecular genetics of ICL2, encoding a non-functional isocitrate lyase in Saccharomyces cerevisiae. Heinisch, J.J., Valdés, E., Alvarez, J., Rodicio, R. Yeast (1996) [Pubmed]
  15. Investigation of two yeast genes encoding putative isoenzymes of phosphoglycerate mutase. Heinisch, J.J., Müller, S., Schlüter, E., Jacoby, J., Rodicio, R. Yeast (1998) [Pubmed]
  16. Reaction of phosphofructokinase 2/fructose 2,6-bisphosphatase with monoclonal antibodies. A proof of the bifunctionality of the enzyme. Van Schaftingen, E., Coulie, P.G., Van Snick, J., Hers, H.G. Eur. J. Biochem. (1986) [Pubmed]
  17. Interaction of 6-phosphofructokinase with cytosolic proteins of Saccharomyces cerevisiae. Schwock, J., Kirchberger, J., Edelmann, A., Kriegel, T.M., Kopperschläger, G. Yeast (2004) [Pubmed]
  18. Characterization of phosphofructokinase 2 and of enzymes involved in the degradation of fructose 2,6-bisphosphate in yeast. François, J., Van Schaftigen, E., Hers, H.G. Eur. J. Biochem. (1988) [Pubmed]
  19. Identification and cloning of yeast phosphofructokinase 2. Kretschmer, M., Tempst, P., Fraenkel, D.G. Eur. J. Biochem. (1991) [Pubmed]
 
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