Analysis of Co-Localization of Glycolytic Enzymes in Flight Muscle and its Relation to Muscle Function in Drosophila

  • David Sullivan
  • Norma Slepecky
  • Nicholas Fuda
Part of the NATO Science Series book series (ASHT, volume 74)


During the last several decades substantial evidence has been brought forward that suggests a structural organization in the cytoplasm, including those macromolecules that have often been labelled cytosolic, or “soluble”. The connotation of these labels has supported the view that the “soluble” class of macromolecules is freely diffusing within the cytoplasm and that their function should be thought of as being governed by principles of diffusion. If so, one would not expect that specific cytoplasmic locations are required for the functions of this set of molecules. However, recently it has been demonstrated that a variety of enzymes are found in specific associations either with other enzymes of the same pathway or with structural cytoplasmic elements. In our work, we are attempting extend these observations by bringing the power of genetic analysis, both classic and molecular, to bear on the issue of metabolic pathway organization in cytoplasm and its functional significance. The experimental goal is to identify structural patterns of organization, perturb these genetically and assess the phenotypic consequences. We are using enzymes of the glycolytic pathway of Drosophila as our experimental system.


Creatine Kinase Phosphate Dehydrogenase Glycolytic Enzyme Flight Muscle Arginine Kinase 
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Copyright information

© Springer Science+Business Media Dordrecht 2000

Authors and Affiliations

  • David Sullivan
    • 1
  • Norma Slepecky
    • 2
  • Nicholas Fuda
    • 1
  1. 1.Department of BiologySyracuse UniversitySyracuseUSA
  2. 2.Department of BioengineeringSyracuse UniversitySyracuseUSA

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