Interaction of phosphofructokinase with tubulin and microtubules. Quantitative evaluation of the mutual effects

Lehotzky, Attila; Telegdi, M; Liliom, Károly; Ovádi, Judit

doi:10.1016/s0021-9258(18)82068-3

Cited by 83 publications

(37 citation statements)

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“…Effect of DdPFK on Tubulin Polymerization. Figure shows the effect of DdPFK on microtubule formation by measuring turbidity and sedimentation of the assembled microtubules in comparison with that of RmPFK, which is known ( , ) not to affect the initial rate of this process under similar polymerization conditions. Addition of taxol to the tubulin solution in the absence of PFK (control) induced polymerization (Figure A), as indicated by the rapid increase in turbidity that leveled off after about 10 min.…”

Section: Resultsmentioning

confidence: 99%

“…Since the activity of DdPFK was not influenced by tubulin, their association into a heterocomplex does not appear to be important for the regulation of this metabolic pathway in the slime mold, but for the control of microtubule formation. Although several enzymes of glycolysis have been described to be affected upon interaction with tubulin ( − ), this is the first example to the best of our knowledge in which a glycolytic enzyme acts not only as a catalyst but also as a potent protein factor affecting tubulin dynamics.…”

Section: Discussionmentioning

confidence: 98%

“…In addition to the above-mentioned implications of microtubules in cellular processes, several glycolytic enzymes have been found to interact in vitro with cytoskeletal proteins, such as actin, tubulin, and microtubules, the interaction leading to a change in catalytic activity (reviewed in refs 11 and 12). In particular, phosphofructokinase (PFK) (13), aldolase (14), glyceraldehyde-3-phosphate dehydrogenase (15), and lactate dehydrogenase (16) were shown to be inhibited by tubulin. A possible involvement of metabolic regulation was therefore suggested (11)(12)(13) for the binding of enzymes to structural elements.…”

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confidence: 99%

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Phosphofructokinase from Dictyostelium discoideum Is a Potent Inhibitor of Tubulin Polymerization

Orosz¹,

Santamaría²,

Ovádi³

et al. 1999

Biochemistry

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We identified the nonallosteric phosphofructokinase from the slime mold Dictyostelium discoideum as a potent protein factor that inhibits the rate of polymerization of tubulin at a molar ratio of 1 molecule to about 300 tubulin dimers for half-maximal action (IC50 = 32 nM). This effect was (i) assessed by turbidity measurements, pelleting of microtubules, and electron microscopy, (ii) observed when tubulin assembly was induced by taxol as well as by GTP in the presence of microtubule-associated proteins or glutamate, and (iii) specific as it was not produced by the phosphofructokinase from rabbit muscle. Also in contrast to the latter, neither tubulin nor microtubules modified the catalytic activity of the slime mold isozyme. Immunoelectron microscopy provided further evidence that D. discoideumphosphofructokinase physically interacts with tubulin, leading to the formation of aggregates. The process seems to be reversible since microtubules eventually formed in the presence of the inhibitor with concomitant reduction of tubulin aggregates. Limited proteolysis by subtilisin showed that the hypervariable C-termini of tubulin is not involved in the interaction with the enzyme. The possible physiological relevance of this novel function of D. discoideum phosphofructokinase different from its glycolytic action is discussed.

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Section: Resultsmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 98%

mentioning

confidence: 99%

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Phosphofructokinase from Dictyostelium discoideum Is a Potent Inhibitor of Tubulin Polymerization

Orosz¹,

Santamaría²,

Ovádi³

et al. 1999

Biochemistry

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“…In heart muscle, a fraction of PFK-M is associated with phospholipase A 2 (9). In skeletal muscle, PFK-M associates with tubulin under certain conditions (10). Insulin plays a key role in this process, as it stimulates binding of both PFK and aldolase to the muscle cytoskeleton (11).…”

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confidence: 99%

Association of Phosphofructokinase-M with Caveolin-3 in Differentiated Skeletal Myotubes

Scherer¹,

Lisanti²

1997

Journal of Biological Chemistry

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Caveolin-3 is a member of the caveolin family of proteins that is primarily expressed in striated muscle cell types (skeletal and cardiac). Here, we show that an approximately 80-kDa protein specifically co-immunoprecipitates with caveolin-3 expressed in differentiated skeletal C2C12 myotubes. Microsequence analysis of this approximately 80-kDa polypeptide revealed its identity as a key regulatory enzyme in the glycolytic pathway, namely phosphofructokinase-M (PFK-M). Pulse-chase experiments demonstrate that PFK-M associates with caveolin-3 with a significant time lag after the biosynthesis of PFK-M. In addition, we show that this interaction is (i) highly regulated by the extracellular concentration of glucose and (ii) can be stabilized by a number of relevant intracellular metabolites, such as fructose 1,6-bisphosphate and fructose 2,6-bisphosphate, which are known allosteric activators of PFK. While the bulk of these experiments were performed in C2C12 cells, identical results were obtained using mouse skeletal muscle extracts. Taken together, our results suggest that glucose-dependent plasma membrane recruitment of activated PFK-M by caveolin-3 could have important implications for understanding the mechanisms that regulate energy metabolism in skeletal muscle fibers.

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“…Nonetheless, it is noteworthy that such a phenomenon has been observed in a variety of cell types from diverse phyla ( Table 1 ), which suggests that the physical and functional association of the enzymes and ion channels with the actin cytoskeleton is a physiologically and evolutionally significant strategy of cells. On the other hand, relatively less is known about similar physical and functional links to other forms of cytoskeleton, although it has been intermittently reported that some metabolic and signaling enzymes are associated with microtubules and intermediate filaments [ 121 , 122 , 123 ].…”

Section: Discussionmentioning

confidence: 99%

Signaling Enzymes and Ion Channels Being Modulated by the Actin Cytoskeleton at the Plasma Membrane

Vasilev

Ezhova

Chun

2021

IJMS

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A cell should deal with the changing external environment or the neighboring cells. Inevitably, the cell surface receives and transduces a number of signals to produce apt responses. Typically, cell surface receptors are activated, and during this process, the subplasmalemmal actin cytoskeleton is often rearranged. An intriguing point is that some signaling enzymes and ion channels are physically associated with the actin cytoskeleton, raising the possibility that the subtle changes of the local actin cytoskeleton can, in turn, modulate the activities of these proteins. In this study, we reviewed the early and new experimental evidence supporting the notion of actin-regulated enzyme and ion channel activities in various cell types including the cells of immune response, neurons, oocytes, hepatocytes, and epithelial cells, with a special emphasis on the Ca2+ signaling pathway that depends on the synthesis of inositol 1,4,5-trisphosphate. Some of the features that are commonly found in diverse cells from a wide spectrum of the animal species suggest that fine-tuning of the activities of the enzymes and ion channels by the actin cytoskeleton may be an important strategy to inhibit or enhance the function of these signaling proteins.

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Interaction of phosphofructokinase with tubulin and microtubules. Quantitative evaluation of the mutual effects

Cited by 83 publications

References 0 publications

Phosphofructokinase from Dictyostelium discoideum Is a Potent Inhibitor of Tubulin Polymerization

Phosphofructokinase from Dictyostelium discoideum Is a Potent Inhibitor of Tubulin Polymerization

Association of Phosphofructokinase-M with Caveolin-3 in Differentiated Skeletal Myotubes

Signaling Enzymes and Ion Channels Being Modulated by the Actin Cytoskeleton at the Plasma Membrane

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