Interactions of enolase isoforms with tubulin and microtubules during myogenesis

Keller, Andreas; Peltzer, J.; Carpentier, Gilles; Horváth, István; Oláh, Judit; Duchesnay, Arlette; Orosz, Ferenc; Ovádi, Judit

doi:10.1016/j.bbagen.2007.01.015

Cited by 65 publications

(54 citation statements)

References 38 publications

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“…2A). The remaining enzymes have either not been tested (PGK) or their activities are unaltered by MT binding (enolase [Keller et al, 2007]). Enzymes showing reduced activity when bound to MTs are PFK (muscle isoform [Lehotzky et al, 1993;Vertessy et al, 1997]) and TPI [Orosz et al, 2000].…”

Section: Cytoskeletonmentioning

confidence: 99%

“…Others, including hexokinase (HK), phosphofructokinase (PFK), GAPDH, enolase, and PK, have been shown to colocalize with MTs in brain extracts (HK, Wagner et al [2001]; PK, Kovacs et al [2003]), myoblasts/muscle (enolase [Keller et al, 2007]), BHK cells (GAPDH [Andrade et al, 2004]) or melanoma cells (PFK [Glass-Marmor and Beitner, 1999]). Several enzymes bind both tubulin dimers and MT polymers, including HK [Wagner et al, 2001], enolase [Keller, 2007], and PK [Kovacs et al, 2003]. Most of the above observations Metabolites cross the outer mitochondrial membrane through VDAC (purple channels).…”

Section: Most Glycolytic Enzymes Bind Mtsmentioning

confidence: 99%

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Fueled by microtubules: Does tubulin dimer/polymer partitioning regulate intracellular metabolism?

et al. 2012

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Microtubules (MTs) or their subunits, tubulin dimers, interact with multiple components that contribute to intracellular metabolic pathways. MTs are required for insulin-dependent transport of glucose transporter 4 to the plasma membrane, they bind most glycolytic enzymes and are required for translation of the mRNA encoding hypoxia inducible factor-1a. Tubulin dimers bind the voltage-dependent anion channel of the mitochondrial outer membrane; this channel functions in metabolite transport in and out of mitochondria. We hypothesize that tubulin partitioning between dimer and polymer pools regulates multiple steps in metabolism, where metabolic output is greatest when both tubulin dimers and MT polymers are present and reduced by drug treatments that disrupt this normal balance. Experimental evidence from these drug-induced changes in tubulin dimer/polymer partitioning supports our model for several metabolic steps. Signal transduction pathways that stabilize or destabilize MTs can shift the normal ratio between unpolymerized and polymerized tubulin dimers, and one downstream consequence of this shift in tubulin partitioning could be a change in metabolic output. V C 2012 Wiley Periodicals, Inc Key Words: glycolysis, oxidative phosphorylation, glucose transport, voltage-dependent anion channel, tubulin IntroductionT he microtubule (MT) cytoskeleton has well-characterized roles in cell polarity, motility, mitosis, and vesicle traffic. The dynamic turnover of MTs is critical to most of these processes, allowing the cell to reorganize an array of MTs rapidly for specific functions. Here we posit an additional role for MTs in regulating metabolic processes and propose that metabolism is greatest when both MTs and their tubulin subunits are present in cells. Disruption of this normal balance, to either inhibit or promote MT polymerization, is expected to decrease metabolic output. Our hypothesis predicts that chemotherapies that stabilize or destabilize MTs will significantly impact metabolic pathways and reduce ATP levels. Importantly, even a small decrease in ATP production can slow cell proliferation. For example, a 19% decrease in ATP production was sufficient to induce senescence in mouse embryo fibroblasts [Kondoh et al., 2005], indicating that even a relatively small contribution of the MT cytoskeleton to metabolic output could have a significant impact on cell fate.The metabolic components and pathways we consider here include glucose transporters (GLUTs), glycolysis, the pentose phosphate pathway (PPP), and mitochondrial oxidative phosphorylation. Glucose enters cells through glucose transporters called GLUTs; the concentration of GLUTs at the plasma membrane can be regulated by insulin and requires trafficking of GLUT-containing vesicles along MTs to reach the plasma membrane. Within the cytoplasm, glucose is broken down to pyruvate during glycolysis, yielding ATP and NADH. Several intermediate products of glucose breakdown, including glucose-6-phosphate (G6P) and glyceraldehyde-3-phosphate (GAP), can also ...

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Section: Cytoskeletonmentioning

confidence: 99%

Section: Most Glycolytic Enzymes Bind Mtsmentioning

confidence: 99%

Fueled by microtubules: Does tubulin dimer/polymer partitioning regulate intracellular metabolism?

et al. 2012

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“…When the glycolytic enzymes are associated and anchored to the sarcomere, ATP is produced more efficiently (Keller et al, 2007). The interaction of enzymes with themselves and with the cytoskeleton confers more stability to the enzyme activity and to the whole network (Keleti et al, 1989;Volker et al, 1995;Walsh et al, 1989).…”

Section: Stationary Statementioning

confidence: 99%

“…Association to microtubules regulates the energetic metabolism (Keleti et al, 1989;Keller et al, 2007;Walsh et al, 1989) at the level of some glycolytic enzymes such as pyruvate kinase, phosphofructokinase (Kovács et al, 2003) and enolase (Keller et al, 2007). When the glycolytic enzymes are associated and anchored to the sarcomere, ATP is produced more efficiently (Keller et al, 2007).…”

Section: Stationary Statementioning

confidence: 99%

Metabolic Optimization by Enzyme-Enzyme and Enzyme-Cytoskeleton Associations

Araiza‐Olivera¹,

Uribe‐Carvajal²,

Chiquete-Félix³

et al. 2012

Cell Metabolism - Cell Homeostasis and Stress Response

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“…16 It could be important during pathological conditions as well because of its ability to function as a heat-shock protein and to bind cytoskeletal and chromatin structures. Several experimental evidence noted how this enzyme plays a key role in the mechanisms involved in cellular motility, 17,18 interacts with microtubules and has a potential role in the regulation of energy metabolism. 19,20 The association of glycolytic enzymes, including alpha-enolase, seems to be important for human sperm motility.…”

Section: View Article Onlinementioning

confidence: 99%

Unravelling the bull fertility proteome

et al. 2013

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In the last few decades a negative association between the level of milk production and fertility has been observed. Currently, the most utilized method of measuring male fertility employed by the livestock industry is related to the Non-Return Rate (NRR). Through differential proteome analysis, this study evaluated changes in the expression of the protein profile of spermatozoa collected from 16 bulls with different levels of field fertility expressed as an estimated relative conception rate (ERCR). The main aim is to identify putative protein markers to be used as putative indices of fertility. Two dimensional electrophoresis coupled with mass spectrometry analysis was used for protein separation and identification. To improve differential proteome analysis among experimental groups, a part of shotgun MS analysis was also performed. Three protein spots showed a differential expression pattern among all ERCR classes. Alpha enolase was significantly down-regulated in the ERCRÀ group, while two other proteins, isocitrate dehydrogenase and triosephosphate isomerase, were up-regulated in ERCRÀ in comparison to ERCR+. Alpha-enolase and isocitrate dehydrogenase subunit alpha (IDH-alpha) have been described in the literature for having a potential role in bull fertility. The possibility of determining protein biomarkers for fertility is more useful and less expensive than ERCR for acquiring rapid estimation of fertility because it does not require the use of field insemination trials. Shotgun MS analysis conducted on the same samples revealed 7 proteins down-regulated in the ERCRÀ group and 1 protein up-regulated. Among these proteins, calmodulin, ATP synthase mitochondrial subunits alpha and delta, malate dehydrogenase and sperm equatorial segment protein 1 were shown to be linked with sperm fertility.

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Interactions of enolase isoforms with tubulin and microtubules during myogenesis

Cited by 65 publications

References 38 publications

Fueled by microtubules: Does tubulin dimer/polymer partitioning regulate intracellular metabolism?

Fueled by microtubules: Does tubulin dimer/polymer partitioning regulate intracellular metabolism?

Metabolic Optimization by Enzyme-Enzyme and Enzyme-Cytoskeleton Associations

Unravelling the bull fertility proteome

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