The regulation of the interaction between F-actin and muscle fructose 1,6-bisphosphatase

Rakus, Dariusz; Gizak, Agnieszka; Dżugaj, Andrzej

doi:10.1016/j.ijbiomac.2004.11.006

Cited by 5 publications

(5 citation statements)

References 30 publications

(35 reference statements)

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“…Finally, in mature myotubes with well-developed striation, FBPase accumulated at the Z-lines (Fig. 1E), as it was previously demonstrated for the skeletal muscles of adult mammals [4,5].…”

Section: Localization Experimentssupporting

confidence: 81%

“…However, our recent investigation revealed that, in striated muscles of mammals, FBPase colocalizes with sarcomeric a-actinin [4,5] and in cardiomyocytes and smooth muscle cells it is also present inside the cells' nuclei [6,7]. We have also demonstrated that FBPase transport to a cardiomyocyte nucleus requires the presence of cytosolic factors and proceeds through the nuclear pores [8].…”

Section: Introductionmentioning

confidence: 90%

“…Muscle fructose 1,6-bisphosphatase (FBPase; EC 3.1.3.11)a key enzyme of glycogen synthesis from non-carbohydrates [1][2][3] -for a long time was regarded to be soluble and freely diffused in the cytoplasm. However, our recent investigation revealed that, in striated muscles of mammals, FBPase colocalizes with sarcomeric a-actinin [4,5] and in cardiomyocytes and smooth muscle cells it is also present inside the cells' nuclei [6,7]. We have also demonstrated that FBPase transport to a cardiomyocyte nucleus requires the presence of cytosolic factors and proceeds through the nuclear pores [8].…”

Section: Introductionmentioning

confidence: 90%

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Changes in subcellular localization of fructose 1,6‐bisphosphatase during differentiation of isolated muscle satellite cells

et al. 2006

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Subcellular localization of FBPase, a regulatory enzyme of glyconeogenesis, was examined inside dividing and differentiating satellite cells from rat muscle. In dividing myoblasts, FBPase was located in cytosol and nuclei. When divisions ceased, FBPase became restricted to the cytosolic compartment and finally was found to associate with the Z-lines, as in adult muscle. Moreover, a 12-fold decrease was observed in the number of FBPase-positive nuclei associated with muscle fibres of adult rat, as compared with young muscle, possibly reflecting the reduction in number of active satellite cells during muscle maturation. The data might suggest that FBPase participates in some nuclear processes during development and regeneration of skeletal muscle.

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“…Finally, in mature myotubes with well-developed striation, FBPase accumulated at the Z-lines (Fig. 1E), as it was previously demonstrated for the skeletal muscles of adult mammals [4,5].…”

Section: Localization Experimentssupporting

confidence: 81%

Section: Introductionmentioning

confidence: 90%

Section: Introductionmentioning

confidence: 90%

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Changes in subcellular localization of fructose 1,6‐bisphosphatase during differentiation of isolated muscle satellite cells

et al. 2006

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“…The high sensitivity of free muscle FBPase to AMP inhibition was hypothesized to be a mechanism protecting muscle cell against the loss of energy via futile cycling between PFK and FBPase [25] during muscle contraction. However, contrary to well defined mode of the inhibition of liver FBPase by AMP [27,29–31], the molecular basis of the inhibition of the muscle isozyme is unknown.…”

Section: Resultsmentioning

confidence: 99%

“…On the other hand, the fraction of uncomplexed FBPase is supposed to increase during acceleration of glycolysis [20]. Thus, the high sensitivity of free FBPase to AMP inhibition seems to be a mechanism preventing muscle cells from dissipating energy via futile cycling between PFK and FBPase during muscle contraction [4,25].…”

Section: Introductionmentioning

confidence: 99%

The origin of the high sensitivity of muscle fructose 1,6‐bisphosphatase towards AMP

et al. 2005

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Adenosine 5 0 -monophosphate (AMP) inhibits muscle fructose 1,6-bisphosphatase (FBPase) about 44 times stronger than the liver isozyme. The key role in strong AMP binding to muscle isozyme play K20, T177 and Q179. Muscle FBPase which has been mutated towards the liver enzyme (K20E/ T177M/Q179C) is inhibited by AMP about 26 times weaker than the wild-type muscle enzyme, but it binds the fluorescent AMP analogue, 2 0 ,3 0 -O-(2,4,6-trinitrophenyl)adenosine 5 0 -monophosphate (TNP-AMP), similarly to the wild-type liver enzyme. The reverse mutation of liver FBPase towards the muscle isozyme significantly increases the affinity of the mutant to TNP-AMP. High affinity to the inhibitor but low sensitivity to AMP of the liver triple mutant suggest differences between the isozymes in the mechanism of allosteric signal transmission.

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Evolutionary conserved N‐terminal region of human muscle fructose 1,6‐bisphosphatase regulates its activity and the interaction with aldolase

et al. 2008

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N-terminal residues of muscle fructose 1,6-bisphosphatase (FBPase) are highly conserved among vertebrates. In this article, we present evidence that the conservation is responsible for the unique properties of the muscle FBPase isozyme: high sensitivity to AMP and Ca(2+) inhibition and the high affinity to muscle aldolase, which is a factor desensitizing muscle FBPase toward AMP and Ca(2+). The first N-terminal residue affecting the affinity of muscle FBPase to aldolase is arginine 3. On the other hand, the first residue significantly influencing the kinetics of muscle FBPase is proline 5. Truncation from 5-7 N-terminal residues of the enzyme not only decreases its affinity to aldolase but also reduces its k-(cat) and activation by Mg(2+), and desensitizes FBPase to inhibition by AMP and calcium ions. Deletion of the first 10 amino acids of muscle FBPase abolishes cooperativity of Mg(2+) activation and results in biphasic inhibition of the enzyme by AMP. Moreover, this truncation lowers affinity of muscle FBPase to aldolase about 14 times, making it resemble the liver isozyme. We suggest that the existence of highly AMP-sensitive muscle-like FBPase, activity of which is regulated by metabolite-dependent interaction with aldolase enables the precise regulation of muscle energy expenditures and might contributed to the evolutionary success of vertebrates.

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The regulation of the interaction between F-actin and muscle fructose 1,6-bisphosphatase

Cited by 5 publications

References 30 publications

Changes in subcellular localization of fructose 1,6‐bisphosphatase during differentiation of isolated muscle satellite cells

Changes in subcellular localization of fructose 1,6‐bisphosphatase during differentiation of isolated muscle satellite cells

The origin of the high sensitivity of muscle fructose 1,6‐bisphosphatase towards AMP

Evolutionary conserved N‐terminal region of human muscle fructose 1,6‐bisphosphatase regulates its activity and the interaction with aldolase

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