Flight muscle function in Drosophila requires colocalization of glycolytic enzymes

Molecular Biology of the Cell

Volumn 8, Issue 9, 1997, Pages 1665-1675

  Wojtas, Kathy ^a,c   Slepecky, Norma ^b   Von Kalm, Laurence ^a,d   Sullivan, David ^a  

^a SYRACUSE UNIVERSITY   (United States)

^b Syracuse University   (United States)

^c PURDUE UNIVERSITY   (United States)

^d UNIVERSITY OF CENTRAL FLORIDA   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

FRUCTOSE BISPHOSPHATE ALDOLASE; GLYCERALDEHYDE 3 PHOSPHATE DEHYDROGENASE; GLYCEROL 3 PHOSPHATE DEHYDROGENASE; GLYCOLYTIC ENZYME;

ANIMAL TISSUE; ARTICLE; CONTROLLED STUDY; DROSOPHILA; ENZYME LOCALIZATION; FLIGHT MUSCLE; GLYCOLYSIS; MUSCLE FIBER CONTRACTION; MUSCLE METABOLISM; NONHUMAN; PRIORITY JOURNAL; TISSUE DISTRIBUTION;

ANIMALIA;

EID: 0030768060     PISSN: 10591524     EISSN: None     Source Type: Journal    
DOI: 10.1091/mbc.8.9.1665     Document Type: Article

References (50)

1. 3 mutant of Drosophila melanogaster is caused by a splicing defect affecting selected troponin I isoforms. Mol. Cell. Biol. 13, 1433-1439.
2. Batke, J. (1989). Remarks on the supramolecular organization of the glycolytic system in vivo. FEBS Lett. 251, 13-16.
3. Bernstein, S.I., O'Donnell, P.T., and Cripps, R.M. (1993). Molecular genetic analysis of muscle development, structure and function in Drosophila. In International Review of Cytology, ed. K.W. Jeon, M. Friedlander, and J. Jarvik, San Diego, CA: Academic Press.
4. Bewley, G.C. (1983). The genetic and epigenetic control of sn-glycerol-3-phosphate dehydrogenase isozyme expression during the development of Drosophila melanogaster. In Isozymes: Current Topics in Biological and Medical Research, vol. 9, ed. M.C. Rattazzi, J.G. Scandalios, and G.S. Whitt, New York, NY: Alan R, Liss.
5. Bewley, G.C., and Miller, S. (1979). Origin and differentiation of the soluble α-glycerolphosphate dehydrogenase isozymes in Drosophila melanogaster. In: Isozymes: Current Topics in Biological and Medical Research, vol. 3, ed. M.C. Rattazzi, J.G. Scandalios, and G.S. Whitt, New York, NY: Alan R. Liss.
6. Brooks, S.P., and Storey, K.B. (1991). Where is the glycolytic complex? A critical evaluation of present data from muscle tissue. FEBS Lett. 278, 135-138.
7. Collier, G.E., Sullivan, D.T., and MacIntyre, R.J. (1976). Purification of α-glycerolphosphate dehydrogenase from Drosophila melanogaster. Biochim. Biophs. Acta 429, 216-223.
8. Cook, J.L., Bewley, G.C., and Shaffer, J.B. (1988). Drosophila snglycerol-3-phosophate dehydrogenase isozymes are generated by alternate pathways of RNA processing resulting in different carboxyl-terminal amino acid sequences. J. Biol. Chem. 263, 10858-10864.
9. Cripps, R.M., Becker, K.D., Mardahl, M., Kronert, W.A., Hodges, D., and Bernstein, S.I. (1994). Transformation of Drosophila melanogaster with the wild-type myosin heavy-chain gene: rescue of mutant phenotypes and analysis of defects caused by overexpression. J. Cell Biol. 226, 689-699.
10. Gould, S., Keller, G.A., Schneider, M., Howell, S.H., Garrad, L.J., Goodman, J.M., Distel, B., Tabak, H., and Subramani, S. (1990). Peroxisomal protein import is conserved between yeast, plants, insects and mammals. EMBO J. 9, 85-90.
11. Harris, S.J., and Winzor, D.J. (1989). Equilibrium partition studies of the myofibrillar interactions of glycolytic enzymes. Arch. Biochem. Biophys. 275, 185-191.
12. Holtham, K.A., and Slepecky, N.B. (1995). A simplified method for obtaining 0.5 μm sections of small tissue specimens embedded in PEG. J. Histochem. Cytochem. 43, 637-643.
13. Klemenz, R., Weber, U., and Gehring, W.J. (1987). The white gene as a marker in a new P-element vector for gene transfer in Drosophila. Nucleic Acids. Res. 15, 3947-3959.
14. Knull, H.R., and Walsh, J.L. (1992). Association of glycolytic enzymes with the cytoskeleton. Curr. Top. Cell. Regul. 33, 15-30.
15. Kotarski, M.A., Pickert, S., Leonard, D.A., LaRosa, G.J., and MacIntyre, R.J. (1983). The characterization of α-glycerolphosphate dehydrogenase mutants in Drosophila melanogaster. Genetics 105, 387-407.
16. Kronert, W.A., O'Donnell, P.T., and Bernstein, S.I. (1994). A charge change in an evolutionary-conserved region of the myosin globular head prevents myosin and thick filament accumulation in Drosophila. J. Mol. Biol. 236, 697-702.
17. Kronert, W.A., O'Donnell, P.T., Frieck, A., Lawn, A., Vigoreaux, J.O., Sparrow, J.C., and Bernstein, S.I. (1995). Defects in the Drosophila myosin rod permit sarcomere assembly but cause flight muscle degeneration. J. Mol. Biol. 249, 111-125.
18. Kvassman, J., Pettersson, G., and Ryde-Pettersson, U. (1988). Mechanism of glyceraldehyde-3-phosphate transfer from aldolase to glyceraldehyde-3-phosphate dehydrogenase. Eur. J. Biochem. 172, 427-431.
19. Lang, A.B., Wyss, C., and Eppenberger, H.M. (1980). Localization of arginine kinase in muscle fibers of Drosophila melanogaster. J. Muscle Res. Cell Motil. 1, 147-161.
20. Lynch, R.M., and Paul, R.J. (1983). Compartmentation of glycolyitc and glycogenolytic metabolism in vascular smooth muscle. Science 222, 1344-1366.
21. MacIntyre, R.J., and Davis, M.B. (1987). A genetic and molecular analysis of the α-glycerolphosphate cycle in Drosophila melanogaster. In Isozymes: Current Topics in Biological and Medical Research, ed. M.C. Rartazzi, J.G. Scandalios, and G.S. Whitt, New York, NY: Alan R. Liss.
22. Masters, C. (1989). Interactions of glycolytic enzymes. Trends Biochem. Sci. 24, 361.
23. Masters, C.J., Reid, S., and Don, M. (1987). Glycolysis-new concepts in an old pathway. Mol. Cell. Biochem. 76, 3-14.
24. Maughan, D., and Wegner, E. (1989). On the organization and diffusion of glycolytic enzymes in skeletal muscle. Prog. Clin. Biol. Res. 325, 137-147.
25. Mejean, C., Pons, F., Benyamin, Y., and Roustan, C. (1989). Antigenie probes locate binding sites for the glycolytic enzymes glyceraldehyde-3-phosphate dehydrogenase, aldolase, and phosphofructokinase on the actin monomeric microfilaments. Biochem. J. 264, 671-677.
26. O'Brien, S.J., and Shimada, Y. (1974). The α-glycerolphosphate cycle in Drosophila melanogaster. IV. Metabolic, ultrastructural, and adaptive consequences of alpha Gpdh-1 "null" mutations. J. Cell Biol. 63, 864-882.
27. Offer, G., Starr, R., and Trinick, J. (1988). Phosphofructokinase: a component of the thick filament? Adv. Exp. Med. Biol. 226, 61-73.
28. Opperdoes, F.R. (1988). Glycosomes may provide clues to the import of peroxisomal proteins. Trends Biochem. Sci. 13, 255-260.
29. Ovadi, J. (1988). Old pathway-new concept: control of glycolysis by metabolite-modulated dynamic enzyme associations. Trends Biochem. Sci. 23, 486-489.
30. Ovadi, J., and Srere, P.A. (1992). Channel your energies. Trends Biochem. Sci. 17, 445-447.
31. Pierce, G.N., and Philipson, K.D. (1985). Binding of glycolytic enzymes to cardiac sarcolemmal and sarcoplasmic reticular membranes. J. Biol. Chem. 260, 6862-6870.
32. Roberts, S.J., and Somero, G.N. (1987). Binding of phosphofructokinase to filamentous actin. Biochemistry 26, 3437-3442.
33. Rubin, G.M., and Spradling, A.C. (1982). Genetic transformation of Drosophila with transposable element vectors. Science 218, 348-353.
34. Saide, J.D., Chin-Bow, S., Hogan-Sheldon, J., Busquets, L., Vigoreaux, J.O., Valqeirsdottir, K., and Pardue, M.L. (1989). Characterization of components of Z-bands in the fibrillar flight muscle of Drosophila melanogaster. J. Cell Biol. 209, 2157-2167.
35. Skuse, G.R., and Sullivan, D.T. (1985). Developmentally regulated alternate modes of expression of the Gpdh locus of Drosophila. EMBO J. 4, 2275-2280.
36. Sommer, J.M., and Wang, C.C. (1994). Targeting proteins to the glycosomes of African trypanosomes. Annu. Rev. Microbiol. 48, 105-138.
37. Srere, P.A. (1987). Complexes of sequential metabolic enzymes. In: Annual Review of Biochemistry, ed. P. Boyer, I. Dawid, and A. Meister, Palo Alto, CA: Annual Reviews.
38. Srivastava, D.K., and Bernhard, S.A. (1986a). Enzyme-enzyme interactions and the regulation of metabolic reaction pathways. In: Current Topics in Cellular Regulation, ed. B.L. Horecker and E.R. Stadtman, Orlando, FL: Academic Press.
39. Srivastava, D.K., and Bernhard, S.A. (1986b). Metabolic transfer via enzyme-enzyme complexes. Science 234, 1081-1086.
40. Sullivan, D.T., Carroll, W.T., Kanik-Ennulat, C.L., Hitti, Y.S., Lovett, J.A., and von Kalm, L. (1985). Glyceraldehyde-3-phosphate dehydrogenase from Drosophila melanogaster. identification of two isozymes forms encoded by separate genes. J. Biol. Chem. 260, 4345-4350.
41. Sullivan, D.T., Donovan, F.A., and Skuse, G. (1983). Developmental regulation of glycerol-3-phosphate dehydrogenase synthesis in Drosophila. Biochem. Genet. 21, 49-62.
42. Tompa, P., Bar, J., and Batke, J. (1986). Interaction of enzymes involved in triosephosphate metabolism. Comparison of yeast and rabbit muscle cytoplasrnic systems. Eur. J. Biochem. 759, 117-124.
43. Turner, D.C., Walliman, T., and Eppenberger, H.M. (1973). A protein that binds specifically to the M-line of skeletal muscle is identified as the muscle form of creatine kinase. Proc. Natl. Acad. Sci. USA 70, 702-705.
44. 31P NMR study. J. Biol. Chem. 265, 914-923.
45. Vigoreaux, J.O. (1994). Alterations in flightin phosphorylation in Drosophila flight muscles are associated with myofibrillar defects engendered by actin and myosin heavy-chain mutant alleles. Biochem. Genet. 32, 301-314.
46. von Kalm, L., Weaver, J., DeMarco, J., MacIntyre, R.J., and Sullivan, D.T. (1989). Structural characterization of the α-glycerol-3-phosphate dehydrogenase-encoding gene of Drosophila melanogaster. Proc. Natl. Acad. Sci. USA 86, 5020-5024.
47. Walliman, T., Kuhn, H.J., Pelloni, G., Turner, D.C., and Eppenberger, H.M. (1977a). Localization of creatine kinase isoenzymes in myofibrils. II. Chicken heart muscle. J. Cell Biol. 75, 318-325.
48. Walliman, T., Turner, D.C., and Eppenberger, H.M. (1977b). Localization of creatine kinase isoenzymes in myofibrils. I. Chicken skeletal muscle. J. Cell Biol. 75, 297-317.
49. Wojtas, K. (1996). Analysis of glycerol-3-phosphate dehydrogenase isoforms in Drosophila melanogaster. Ph.D. Thesis. Syracuse, NY: Syracuse University.
50. Wu, X.M., Gutfreund, H., Lakatos, S., and Chock, P.B. (1991). Substrate channeling in glycolysis: a phantom phenomenon. Proc. Natl. Acad. Sci. USA 88, 497-501.