Colocalization of muscle FBPase and muscle aldolase on both sides of the Z-line.
Previously we have reported that in vitro muscle aldolase binds to muscle FBPase [Biochem. Biophys. Res. Commun. 275 (2000) 611-616] which results in the changes of regulatory properties of the latter enzyme. In the present paper, the evidence that aldolase binds to FBPase in living cell is presented. The colocalization experiment, in which aldolase was diffused into skinned fibres that had been pre-incubated with FBPase, has shown that aldolase in the presence of FBPase binds predominantly to the Z-line. The existence of a triple aldolase-FBPase-alpha-actinin complex was confirmed through a real-time interaction analysis using the BIAcore biosensor. The colocalization of FBPase and aldolase on alpha-actinin of the Z-line indicates the existence of glyconeogenic metabolon in vertebrates' myocytes.
Department of Animal Physiology, Institute of Zoology, Wroclaw University, Cybulskiego 30, 50-205 Wroclaw, Poland. dzugajan@biol.uni.wroc.pl
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D000185:Actinin / Q000737:chemistry / Q000378:metabolism* / Q000648:ultrastructure; D000818:Animals; D003067:Coenzymes / Q000378:metabolism / Q000648:ultrastructure; D006597:Fructose-Bisphosphatase / Q000737:chemistry / Q000378:metabolism* / Q000648:ultrastructure; D005634:Fructose-Bisphosphate Aldolase / Q000737:chemistry / Q000378:metabolism* / Q000648:ultrastructure; D046911:Macromolecular Substances; D018485:Muscle Fibers, Skeletal / Q000737:chemistry / Q000166:cytology / Q000201:enzymology*; D011485:Protein Binding; D016658:Psoas Muscles / Q000166:cytology / Q000201:enzymology*; D011817:Rabbits; D014018:Tissue Distribution
D003067:Coenzymes; D046911:Macromolecular Substances; D000185:Actinin; D006597:Fructose-Bisphosphatase; D005634:Fructose-Bisphosphate Aldolase