Abstract
The glycolytic control enzyme phosphofructokinase from the parasitic nematodeAscaris lumbricodies is regulated by reversible phosphorylation. The enzyme is phosphorylated by an atypical cyclic adenosine monophosphate (cAMP)-dependent protein kinase whose substrate specificity deviates from that of the mammalian protein kinase. This variation is explained by structural peculiarities on the surface part of the catalytic groove of the protein kinase. Also, the protein phosphatases responsible for the reversal of phosphorylation appear to act specifically in glycolysis and are different from those participating in regulation of glycogenolysis.
Similar content being viewed by others
References
Berridge, M., Inositol trisphosphate and diacylglycerol as second messengers. Biochem. J.220 (1984) 345–360.
Biethinger, M., Hoffmann, R., and Hofer, H. W., Phosphofructokinase from mollusc muscle is activated by phosphorylation. Archs Biochem. Biophys.287 (1991) 263–267.
Bollen, M., and Stalmans, W., The structure, role and regulation of type 1 protein phosphatases. Crit. Rev. Biochem. Mol., Biol.27 (1992) 227–281.
Cohen, P., The structure and regulation of protein phosphatases. A. Rev. Biochem.58 (1989) 453–508.
Cohen, P. T. W., Brewis, N. D., Hughes, V., and Mann, D. J. Protein serine/threonine phosphatases, an expanding family. FEBS Lett.268 (1990) 355–359.
Daum, G., Thalhofer, H. P., Harris, B. G., and Hofer, H. W., Reversible activation and inactivation of phosphofructokinase fromAscaris suum by the action of tissue-homologous protein phosphorylating and dephosphorylating enzymes. Biochem. biophys. Res. Commun.139 (1986) 215–221.
Daum, G., Schmid, B., MacKintosh, C., Cohen, P., and Hofer, H. W., Characterization of the major phosphofructokinase-dephosphorylating protein phosphatases fromAscaris suum muscle. Biochim. Biophys. Acta1122 (1992) 23–32.
Gibbs, C. S., Knighton, D. R., Sowadski, J. M., Taylor, S. S., and Zoller, M. J., Systematic mutational analysis of cAMP-dependent protein kinase identifies unregulated catalytic subunits and defines regions important for the recognition of the regulatory subunit. J. Biol. Chem.267 (1992) 4806–4814.
Debondt, H. L., Rosenblatt, J., Jancarik, J., Hones, H. D., Morgan, D. O., and Kim, S. H., Crystal structure of cyclin-dependent kinase-2. Nature363 (1993) 595–602.
Donahue, M. J., Masaracchia, R. A., and Harris, B. G., The role of cAMP-mediated regulation of glycogen metabolism in Levamisole-perfusedAscaris suum muscle. Molecular Pharmacol.A23 (1982) 378–383.
Hanks, S. K., Quinn, A. M., and Hunter, T., The protein kinase family: conserved features and deduced phylogeny of the catalytic domains. Science241 (1988) 42–52.
Harris, B. G., Kaeini, M., and Hofer, H. W., Glycolytic regulation inAscaris suum muscle by phosphofructokinase and protein kinases. Molec. Biochem. Parasitol.3 Suppl. (1982), 139–140.
Hofer, H. W., Allen, B. L., Kaeini, M. R., and Harris, B. G., Phosphofructokinase fromAscaris suum: the effect of phosphorylation on activity near physiological conditions. J. biol. Chem.257 (1982) 3801–3806.
Hoffmann, R., Jung, S., and Hofer, H. W., Association of a heat-stable inhibitor protein with cyclic-3′,5′-AMP-dependent protein kinase from the nematodeAscaris suum. Purification and characterization of the inhibitor. Archs Biochem. Biophys.297 (1992) 296–303.
Hoffmann, R., Jung, S., Ehrmann, M., and Hofer, H. W., TheSaccharomyces cerevisiae gene PPH3 encodes a protein phosphatase with properties different from PPX, PP1 and PP2A. Yeast10 (1994) 567–578.
Hubbard, S. R., Wei, L., Elis, L., Hendrickson, W. A., Crystal structure of the tyrosine kinase domain of the human insulin receptor. Nature, Lond.372 (1994) 746–754.
Jung, S., Hoffmann, R., Rodriguez, P. H., Mutzel, R., and Hofer, H. W., The catalytic subunit of cAMP-dependent protein kinase fromAscaris suum. The cloning and structure of a novel subtype of protein kinase A. Eur. J. Biochem.232 (1995) 111–117.
Knighton, D. R., Zheng, J., Ten Eyck, L. F., Ashford, V. A., Xuong, N. H., Taylor, S. S., and Sowadski, J. M., Crystal structure of the catalytic subunit of cyclic adenosine monophosphate-dependent protein kinase. Science253 (1991) 407–414.
Knighton, D. R., Zheng, J., Ten Eyck, L. G., Xuong, N., Taylor, S. S., and Sowadski, J. M., Structure of a peptide inhibitor bound to the catalytic subunit of cyclic adenosine monophosphate-dependent protein kinase. Science253 (1991) 414–420.
Kulkarni, G., Rao, G. S. J., Srinivasan, N. G., Hofer, H. W., Yuan, P. M., and Harris, B. G.,Ascaris suum PFK. Phosphorylation by protein kinase and sequence of the phosphopeptide. J. biol. Chem.262 (1987) 32–34.
Mansour, T. E., Serotonin receptors in parasitic worms. Adv. Parasitol.23 (1984) 1–36.
Okimoto, R., Macfarlane, J. L., Clary, D. O., and Wolstenholme, D. R., The mitochondrial genomes of two nematodes,Caenorhabditis elegans andAscaris suum. Genetics130 (1992) 471–498.
Rall, T. W., and Sutherland, E. W., Formation of a cyclic adenine ribonucleotide by tissue particles. J. biol. Chem.232 (1958) 1065–1076.
Thalhofer, H. P., Daum, G., Harris, G. G., and Hofer, H. W., Identification of two different phosphofructokinase-phosphorylating protein kinases fromAscaris suum muscle. J. biol. Chem.263 (1988) 952–957.
Thalhofer, H. P., Starz, W., Daum, G., Wurster, B., Harris, B. G., and Hofer, H. W., Purification and properties of the cyclic 3′,5′-AMP binding protein from the muscle of the nematodeAscaris suum. Archs Biochem. Biophys.271 (1989) 471–478.
Saz, H. J., Energy metabolism of parasitic helminths: adaption to parasitism. Annu. Rev. Physiol.43 (1981) 323–341.
Treptau, T., Piram, P., Cook, P. F., Rodriguez, P., Hoffmann, R., Jung, S., Thalhofer, H. P., Harris, B. G., and Hofer, H. W., Comparison of the substrate specificities of cAMP-dependent protein kinase from bovine heart andAscaris suum muscle. Biological Chemistry Hoppe-Seyler377 (1996) 203–209.
Author information
Authors and Affiliations
Rights and permissions
About this article
Cite this article
Hofer, H.W. Conservation, evolution, and specificity in cellular control by protein phosphorylation. Experientia 52, 449–454 (1996). https://doi.org/10.1007/BF01919314
Issue Date:
DOI: https://doi.org/10.1007/BF01919314