ArticleThe Journal of cell biology1988
Aldolase exists in both the fluid and solid phases of cytoplasm.
Article in The Journal of cell biology, 1988. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 26 papers.
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Who cites it
26 citing papers in PubMed, 120 citations in OpenAlex.
- Endothelial Cell Metabolism in Vascular Functions.Cancers · 2022Review
- Crosstalk between mechanotransduction and metabolism.Nature reviews. Molecular cell biology · 2021Review
- Non-canonical functions of enzymes facilitate cross-talk between cell metabolic and regulatory pathways.Experimental & molecular medicine · 2018Review
- Glycolysis is the primary bioenergetic pathway for cell motility and cytoskeletal remodeling in human prostate and breast cancer cells.Oncotarget · 2015Article
- Article
- Microtubule-assisted mechanism for functional metabolic macromolecular complex formation.Proceedings of the National Academy of Sciences of the United States of America · 2010Article
- MIC6 associates with aldolase in host cell invasion by Toxoplasma gondii.Parasitology research · 2009Article
- Structure of a rabbit muscle fructose-1,6-bisphosphate aldolase A dimer variant.Acta crystallographica. Section D, Biological crystallography · 2008Article
- Glycolytic enzyme interactions with yeast and skeletal muscle F-actin.Biophysical journal · 2006Article
- Enzymes of glycolysis are functionally associated with the mitochondrion in Arabidopsis cells.The Plant cell · 2003Article
- Use of alpha-toxin from Staphylococcus aureus to test for channelling of intermediates of glycolysis between glucokinase and aldolase in hepatocytes.The Biochemical journal · 2000Article
- Fluorescence correlation microscopy of cells in the presence of autofluorescence.Biophysical journal · 1998Article
- The dynamics of local kinetic parameters of glutamate dehydrogenase in rat liver.Histochemistry and cell biology · 1996Article
- Substrate modulation of aldolase B binding in hepatocytes.The Biochemical journal · 1996Article
- Article
- Analysis of enzyme reactions in situ.The Histochemical journal · 1995Review
- Quantitative comparison between the gel-film and polyvinyl alcohol methods for dehydrogenase histochemistry reveals different intercellular distribution patterns of glucose-6-phosphate and lactate dehydrogenases in mouse liver.The Histochemical journal · 1994Article
- The diverse Michaelis constants and maximum velocities of lactate dehydrogenase in situ in various types of cell.The Histochemical journal · 1994Article
- Fluorescent actin analogs with a high affinity for profilin in vitro exhibit an enhanced gradient of assembly in living cells.The Journal of cell biology · 1994Article
- Gradients in the concentration and assembly of myosin II in living fibroblasts during locomotion and fiber transport.Molecular biology of the cell · 1993Article
Corrections and comments
- Erratum issued
Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
We have prepared a functional fluorescent analogue of the glycolytic enzyme aldolase (rhodamine [Rh]-aldolase), using the succinimidyl ester of carboxytetramethyl-rhodamine. Fluorescence redistribution after photobleaching measurements of the diffusion coefficient of Rh-aldolase in aqueous solutions gave a value of 4.7 x 10(-7) cm2/S, and no immobile fraction. In the presence of filamentous actin, there was a 4.5-fold reduction in diffusion coefficient, as well as a 36% immobile fraction, demonstrating binding of Rh-aldolase to actin. However, in the presence of a 100-fold molar excess of its substrate, fructose 1,6-diphosphate, both the mobile fraction and diffusion coefficient of Rh-aldolase returned to control levels, indicating competition between substrate binding and actin cross-linking. When Rh-aldolase was microinjected into Swiss 3T3 cells, a relatively uniform intracellular distribution of fluorescence was observed. However, there were significant spatial differences in the in vivo diffusion coefficient and mobile fraction of Rh-aldolase measured with fluorescence redistribution after photobleaching. In the perinuclear region, we measured an apparent cytoplasmic diffusion coefficient of 1.1 x 10(-7) cm2/s with a 23% immobile fraction; while measurements in the cell periphery gave a value of 5.7 x 10(-8) cm2/s, with no immobile fraction. Ratio imaging of Rh-aldolase and FITC-dextran indicated that FITC-dextran was relatively excluded excluded from stress fiber domains. We interpret these data as evidence for the partitioning of aldolase between a soluble fraction in the fluid phase and a fraction associated with the solid phase of cytoplasm. The partitioning of aldolase and other glycolytic enzymes between the fluid and solid phases of cytoplasm could play a fundamental role in the control of glycolysis, the organization of cytoplasm, and cell motility. The concepts and experimental approaches described in this study can be applied to other cellular biochemical processes.
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