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

Gizak, Agnieszka; Wróbel, Edyta; Moraczewski, Jerzy; Dżugaj, Andrzej

doi:10.1016/j.febslet.2006.06.042

Cited by 19 publications

(19 citation statements)

References 27 publications

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“…Recent studies have revealed that a regulatory enzyme of gluconeogenesis—FBPase—is localized in nuclei of proliferating cells and that nuclear transport of the enzyme is regulated by extracellular stimuli (Gizak et al 2005, 2006, 2009; Mamczur et al 2010). In contrast to dividing cells, FBPase is absent in nuclei of terminally differentiated cells (Gizak et al 2006; Mamczur et al 2010).…”

Section: Discussionmentioning

confidence: 99%

“…In contrast to dividing cells, FBPase is absent in nuclei of terminally differentiated cells (Gizak et al 2006; Mamczur et al 2010). These findings point to FBPase as a protein potentially involved in cell cycle regulation and/or progression.…”

Section: Discussionmentioning

confidence: 99%

“…In contrast to the liver isozyme, the muscle FBPase is expressed widely and even in non-gluconeogenic cells (Al-Robaiy and Eschrich 1999). The role for FBP2 in these cells remains unclear, but a growing body of evidence suggests that the physiological function of the muscle isozyme goes beyond participation in the synthesis of glucose/glycogen from non-carbohydrate substrates (Gizak et al 2006, 2009). …”

Section: Introductionmentioning

confidence: 99%

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Cell cycle-dependent expression and subcellular localization of fructose 1,6-bisphosphatase

Mamczur

Sok

Rzechonek³

et al. 2011

Histochem Cell Biol

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Recently a gluconeogenic enzyme was discovered—fructose 1,6-bisphosphatase (FBPase)—that localizes in the nucleus of a proliferating cell, but its physiological role in this compartment remains unclear. Here, we demonstrate the link between nuclear localization of FBPase and the cell cycle progression. Results of our studies indicate that in human and mouse squamous cell lung cancer, as well as in the HL-1 cardiomyocytes, FBPase nuclear localization correlates with nuclear localization of S and G2 phase cyclins. Additionally, activity and expression of the enzyme depends on cell cycle stages. Identification of FBPase interacting partners with mass spectrometry reveals a set of nuclear proteins involved in cell cycle regulation, mRNA processing and in stabilization of genomic DNA structure. To our knowledge, this is the first experimental evidence that muscle FBPase is involved in cell cycle events.Electronic supplementary materialThe online version of this article (doi:10.1007/s00418-011-0884-1) contains supplementary material, which is available to authorized users.

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Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

Cell cycle-dependent expression and subcellular localization of fructose 1,6-bisphosphatase

Mamczur

Sok

Rzechonek³

et al. 2011

Histochem Cell Biol

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“…Our earlier studies have revealed that FBPase localizes within the nuclei of cells that have the potential to proliferate but that are also at least partially differentiated: in some adult mammalian cardiomyocytes (Gizak and Dzugaj 2003), in mouse cardiomyocytes cell line (HL-1) stimulated with norepinephrine leading to their adult phenotype (Gizak et al 2009), and in muscle satellite cells (Gizak et al 2006). The nuclear localization of FBPase in the developing retina suggests that, also in this tissue, the cellular action of the enzyme is related in some manner to cell differentiation.…”

Section: Discussionmentioning

confidence: 99%

Ubiquitous presence of gluconeogenic regulatory enzyme, fructose-1,6-bisphosphatase, within layers of rat retina

2010

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To shed some light on gluconeogenesis in mammalian retina, we have focused on fructose-1,6-bisphosphatase (FBPase), a regulatory enzyme of the process. The abundance of the enzyme within the layers of the rat retina suggests that, in mammals in contrast to amphibia, gluconeogenesis is not restricted to one specific cell of the retina. We propose that FBPase, in addition to its gluconeogenic role, participates in the protection of the retina against reactive oxygen species. Additionally, the nuclear localization of FBPase and of its binding partner, aldolase, in the retinal cells expressing the proliferation marker Ki-67 indicates that these two gluconeogenic enzymes are involved in non-enzymatic nuclear processes.Electronic supplementary materialThe online version of this article (doi:10.1007/s00441-010-1008-2) contains supplementary material, which is available to authorized users.

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“…In some higher eukaryotes, Fbp has been found to be associated with nuclei in different types of cells (35,66). In some cases, the localization of the protein was influenced by the growth phase of the cells (35) or by changing metabolic conditions (66).…”

Section: Vol 7 2008mentioning

confidence: 99%

The Gluconeogenic Enzyme Fructose-1,6-Bisphosphatase Is Dispensable for Growth of the Yeast Yarrowia lipolytica in Gluconeogenic Substrates

2008

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The genes encoding gluconeogenic enzymes in the nonconventional yeast Yarrowia lipolytica were found to be differentially regulated. The expression of Y. lipolytica FBP1 (YlFBP1) encoding the key enzyme fructose-1,6-bisphosphatase was not repressed by glucose in contrast with the situation in other yeasts; however, this sugar markedly repressed the expression of YlPCK1, encoding phosphoenolpyruvate carboxykinase, and YlICL1, encoding isocitrate lyase. We constructed Y. lipolytica strains with two different disrupted versions of YlFBP1 and found that they grew much slower than the wild type in gluconeogenic carbon sources but that growth was not abolished as happens in most microorganisms. We attribute this growth to the existence of an alternative phosphatase with a high K m (2.3 mM) for fructose-1,6-bisphosphate. The gene YlFBP1 restored fructose-1,6-bisphosphatase activity and growth in gluconeogenic carbon sources to a Saccharomyces cerevisiae fbp1 mutant, but the introduction of the FBP1 gene from S. cerevisiae in the Ylfbp1 mutant did not produce fructose-1,6-bisphosphatase activity or growth complementation. Subcellular fractionation revealed the presence of fructose-1,6-bisphosphatase both in the cytoplasm and in the nucleus.The growth of yeasts and other microorganisms in nonsugar carbon sources is dependent on gluconeogenesis. This pathway implicates specific gluconeogenic enzymes, such as fructose-1,6-bisphosphatase (Fbp) and phosphoenolpyruvate carboxykinase (Pck), that bypass the two physiologically irreversible steps in the glycolytic pathway, namely, phosphofructokinase and pyruvate kinase. In addition, under certain growth conditions, the enzymes from the glyoxylate cycle, isocitrate lyase (Icl) and malate synthase, are also required for the function of gluconeogenesis (Fig. 1). Growth in any nonsugar carbon source requires Fbp, which catalyzes the hydrolysis of fructose-1,6-P 2 to fructose-6-phosphate, and therefore, Fbp is a key enzyme in gluconeogenesis. The simultaneous function of specific gluconeogenic enzymes and their glycolytic counterparts would lead to futile cycles, i.e., reactions that waste ATP without yielding a net product (42). Presumably due to evolutionary pressure, a series of control mechanisms have been selected to minimize the functioning of those cycles. In the yeast Saccharomyces cerevisiae, the activities of phosphofructokinase and pyruvate kinase are controlled by a series of activators and inhibitors whose concentrations vary upon growth on sugars or nonsugar carbon sources (12,61,65). The activity of gluconeogenic enzymes is determined by the interplay of a variety of mechanisms. The transcription of the genes encoding them is subjected to catabolite repression, a complex regulatory phenomenon that involves many proteins (13,32,41). In addition, in S. cerevisiae, most of the gluconeogenic enzymes undergo catabolite inactivation (27, 48, 50), a proteolytic degradation that destroys them after glucose addition. Control by metabolites appears to be restricted to Fbp that ...

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

Cited by 19 publications

References 27 publications

Cell cycle-dependent expression and subcellular localization of fructose 1,6-bisphosphatase

Cell cycle-dependent expression and subcellular localization of fructose 1,6-bisphosphatase

Ubiquitous presence of gluconeogenic regulatory enzyme, fructose-1,6-bisphosphatase, within layers of rat retina

The Gluconeogenic Enzyme Fructose-1,6-Bisphosphatase Is Dispensable for Growth of the Yeast Yarrowia lipolytica in Gluconeogenic Substrates

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