A Glycolytic Enzyme Binding Domain on Tubulin

Völker, Katharina; Knull, Harvey R.

doi:10.1006/abbi.1996.9819

Cited by 74 publications

(54 citation statements)

References 39 publications

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“…All of these molecules display a consensus sequence composed of two acidic stretches flanking a single highly hydrophobic residue (Figure 7). Deletion of either acidic tract or posttranslational modification of the hydrophobic residue correlates with a decreased affinity of these molecules for aldolase (Itin et al, 1993;Volker and Knull, 1997;Eisenmesser and Post, 1998). The participation of ionic bonds in the aldolase-TRAP interaction is also supported by the inhibitory effect of salts (IC 50% reached at 60 mM) and/or ionic detergents (our unpublished data).…”

Section: Discussionmentioning

confidence: 64%

“…This scenario would explain the inhibitory role of aldolase substrate, products, and competitive inhibitors in this interaction (Table 1). Indeed, the association to aldolase of other sequences structurally related to TRAP such as those displayed in Figure 7 is also displaced by aldolase substrate/products (Schneider and Post, 1995;Volker and Knull, 1997;Kao et al, 1999). However, this idea is not supported by the observation that neither the TRAP34mer nor the TRAP25mer peptide inhibited the in vitro PfAldo activity even when tested at 100 M concentration (Table 1).…”

Section: Discussionmentioning

confidence: 97%

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Sites of Interaction between Aldolase and Thrombospondin-related Anonymous Protein inPlasmodium

Buscaglia

Coppens

Hól

et al. 2003

MBoC

153

173

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Gliding motility and host cell invasion by apicomplexan parasites are empowered by an acto-myosin motor located underneath the parasite plasma membrane. The motor is connected to host cell receptors through trans-membrane invasins belonging to the thrombospondin-related anonymous protein (TRAP) family. A recent study indicates that aldolase bridges the cytoplasmic tail of MIC2, the homologous TRAP protein in Toxoplasma, and actin. Here, we confirm these unexpected findings in Plasmodium sporozoites and identify conserved features of the TRAP family cytoplasmic tail required to bind aldolase: a subterminal tryptophan residue and two noncontiguous stretches of negatively charged amino acids. The aldolase substrate and other compounds that bind to the active site inhibit its interaction with TRAP and with F-actin, suggesting that the function of the motor is metabolically regulated. Ultrastructural studies in salivary gland sporozoites localize aldolase to the periphery of the secretory micronemes containing TRAP. Thus, the interaction between aldolase and the TRAP tail takes place during or preceding the biogenesis of the micronemes. The release of their contents in the anterior pole of the parasite upon contact with the target cells should bring simultaneously aldolase, TRAP and perhaps F-actin to the proper subcellular location where the motor is engaged.

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Section: Discussionmentioning

confidence: 64%

Section: Discussionmentioning

confidence: 97%

Sites of Interaction between Aldolase and Thrombospondin-related Anonymous Protein inPlasmodium

Buscaglia

Coppens

Hól

et al. 2003

MBoC

153

173

View full text Add to dashboard Cite

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“…Numerous studies have demonstrated interactions between the cytoskeleton and glycolytic enzymes, especially GAPDH, aldolase and PK. [25][26][27][28][29][30][31][32][33][34][35][36][37][38] In this study, quantities of these glycolytic enzymes, as well as actin, tubulin and tropomyosin, were sufficient in U87 pseudopodia to be detected with Figure 4 DeCyder ratios Coomassie blue staining, thus establishing the potential for the energy-generating portion of the glycolytic pathway to energize cytoskeletal proteins for migration within U87 pseudopodia. Polymerization of actin and tubulin shares a similar use of energy from nucleotide triphosphate hydrolysis.…”

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confidence: 65%

Proteomic characterization of harvested pseudopodia with differential gel electrophoresis and specific antibodies

Beckner

Chen

et al. 2005

Laboratory Investigation

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Malignant gliomas (astrocytomas) are lethal tumors that invade the brain. Invasive cell migration is initiated by extension of pseudopodia into interstitial spaces. In this study, U87 glioma cells formed pseudopodia in vitro as cells pushed through 3 lm pores of polycarbonate membranes. Harvesting pseudopodia in a novel two-step method provided material for proteomic analysis. Differences in the protein profiles of pseudopodia and whole cells were found using differential gel electrophoresis (DIGE) and immunoblotting. Proteins from twodimensional (2D) gels with M R 's of 20-100 kDa and pI's of 3.0-10.0 were identified by peptide mass fingerprinting analysis using mass spectrometry. For DIGE, lysates of pseudopodia and whole cells were each labeled with electrophilic forms of fluorescent dyes, Cy3 or Cy5, and analyzed as mixtures. Analysis was repeated with reciprocal labeling. Differences in protein distributions were detected by manual inspection and computer analysis. Topographical digital maps of the scanned gels were used for algorithmic spot matching, normalization of background, quantifying spot differences, and elimination of artifacts. Pseudopodial proteins in Coomassie-stained 2D gels included isoforms of glycolytic enzymes as the largest group, seven of 24 proteins. Peptide mass fingerprint analysis of DIGE gels demonstrated increased isoforms of annexin (Anx) I, AnxII, enolase, pyruvate kinase, and aldolase, and decreased mitochondrial manganese superoxide dismutase and transketolase in pseudopodia. Specific antibodies showed restricted immunoreactivity of the hepatocyte growth factor (HGF) a chain to pseudopodia, indicating localization of its active form. Met (the HGF receptor), actin, and total AnxI were increased in pseudopodial lysates on immunoblots. Increased constituents of the pseudopodial proteome in glioma cells, identified in this study as actin, HGF, Met, and isoforms of AnxI, AnxII, and several glycolytic enzymes, represent therapeutic targets to consider for suppression of tumor invasion.

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“…Aldolase A is associated to cytoskeletal structures in guinea pig spermatozoa Although glycolysis occurs in the cytoplasm, it has been reported that aldolase is associated to cytoskeletal structures (Gillis & Tamblyn 1984, Volker & Knull 1997, Schindler et al 2001. Indeed, our ability to retrieve aldolase A in Brij-treated spermatozoa suggests that this could be the case in our system; to explore this possibility in more detail, we purified non-ionic detergent-insoluble proteins from Brij-treated spermatozoa suitable for proteomic analysis.…”

Section: Resultsmentioning

confidence: 93%

In guinea pig sperm, aldolase A forms a complex with actin, WAS, and Arp2/3 that plays a role in actin polymerization

Chiquete-Félix¹,

Hernández²,

Méndez³

et al. 2009

Reproduction

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Glycolytic enzymes have, in addition to their role in energy production, other functions in the regulation of cellular processes. Aldolase A has been reported to be present in sperm, playing a key role in glycolysis; however, despite its reported interactions with actin and WAS, little is known about a non-glycolytic role of aldolase A in sperm. Here, we show that in guinea pig spermatozoa, aldolase A is tightly associated to cytoskeletal structures where it interacts with actin, WAS, and Arp2/3. We show that aldolase A spermatozoa treatment increases their polymerized actin levels. In addition, we show that there is a direct correlation between the levels of polymerized actin and the levels of aldolase A-actin interaction. Our results suggest that aldolase A functions as a bridge between filaments of actin and the actin-polymerizing machinery.

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A Glycolytic Enzyme Binding Domain on Tubulin

Cited by 74 publications

References 39 publications

Sites of Interaction between Aldolase and Thrombospondin-related Anonymous Protein inPlasmodium

Sites of Interaction between Aldolase and Thrombospondin-related Anonymous Protein inPlasmodium

Proteomic characterization of harvested pseudopodia with differential gel electrophoresis and specific antibodies

In guinea pig sperm, aldolase A forms a complex with actin, WAS, and Arp2/3 that plays a role in actin polymerization

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