Bundling of microtubules by glyceraldehyde‐3‐phosphate dehydrogenase and its modulation by ATP

Huitorel, Philippe; Pantaloni, Dominique

doi:10.1111/j.1432-1033.1985.tb09016.x

Cited by 179 publications

(96 citation statements)

References 37 publications

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“…The ubiquity of GAPDH has been the subject of several reports in the literature (Huitorel and Pantolini, 1985;Kawamoto and Caswell, 1986;Allen et al, 1987;Meyer-Siegler et al, 1991;Pancholi and Fischetti, 1992;Singh and Green, 1993;Robbins et al, 1995;GilNavarro et al, 1997) and the results presented in this paper clearly show that this GAPDH protein (p37) has other functions than its glycolytic enzymatic activity, as its oversynthesis in¯uences growth, biomass yield, cell wall stability, cell morphology and aggregation. There is now evidence that p37 can induce cell aggregation in Saccharomyces, although it is a Kluyveromyces protein.…”

Section: Discussionsupporting

confidence: 58%

Flocculation of Saccharomyces cerevisiae is induced by transformation with the GAP1 gene from Kluyveromyces marxianus

Moreira¹,

Ferreira‐da‐Silva²,

Fernandes

et al. 2000

Yeast

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A non-¯occulent strain of Saccharomyces cerevisiae was transformed with the GAP1 gene which encodes p37, a GAPDH-like protein present in the cell wall of Kluyveromyces marxianus¯occulent cells. The transformed cells were characterized with respect to¯occulation behaviour, morphology, growth, cell wall integrity and GAPDH activity. A¯occulent phenotype was acquired by the transformed cells, showing a behaviour in respect tō occulation/de¯occulation very similar to that of K. marxianus. The presence of p37 in the cell wall was assessed by immunoprecipitation of biotinylated cell wall proteins and an accumulation of p37 was evident in the cell wall of transformed cells. This result was con®rmed by studies using a chimeric protein resulting from fusing the p37 with a yeast-enhanced green¯uorescent protein, yEGFP. The recombinant protein was localized mainly in the cell wall of the transformed strain, although the presence of p37 in the cytosol was indicated by an increase in GAPDH activity. Calco¯uor white sensitivity tests indicated that the cell wall structure is affected by the accumulation of p37. These results provided further evidence of p37 function regarding¯occulation and that although lacking a N-terminal signal peptide p37 is targeted to the cell wall.

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Section: Discussionsupporting

confidence: 58%

Flocculation of Saccharomyces cerevisiae is induced by transformation with the GAP1 gene from Kluyveromyces marxianus

Moreira¹,

Ferreira‐da‐Silva²,

Fernandes

et al. 2000

Yeast

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“…Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) has been described on the surface of phagocytic cells and has a role in signal transduction (26)(27)(28). More recently, GAPDH has been found to associate with ␤-tubulin recruitment to membrane (26,28).…”

Section: Discussionmentioning

confidence: 99%

Identification ofMycobacterium aviumpathogenicity island important for macrophage and amoeba infection

Danelishvili

Stang

et al. 2007

Proc. Natl. Acad. Sci. U.S.A.

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The ability to infect macrophages is a common characteristic shared among many mycobacterial species. Mycobacterium avium, Mycobacterium tuberculosis, and Mycobacterium kansasii enter macrophages, using the complement receptors CR1, CR3, CR4, and the mannose receptor. To identify M. avium genes and host cell pathways involved in the bacterial uptake by macrophages, we screened a M. avium transposon mutant library for the inability to enter macrophages. Uptake-impaired clones were selected. Sequence of six M. avium clones identified one gene involved in glycopeptidolipid biosynthesis, one gene encoding the conserved membrane protein homologue to the M. avium subsp. paratuberculosis MAP2446c gene and four others belonging to the same region of the chromosome. Analysis of the chromosome region revealed a pathogenicity island inserted between two tRNA sequences with 58% of G؉C content versus 69% in the M. avium genome. The region is unique for M. avium and is not present in M. tuberculosis or M. paratuberculosis. Although the mutants did not differ from the WT bacterium regarding the binding to macrophage cell membrane, analysis of macrophage proteins after 1 h infection revealed a deficiency in the mutant to phosphorylate certain proteins on uptake. To understand M. avium interaction with two evolutionarily distinct hosts, the mutants were evaluated for Acanthamoeba castellanii invasion. The defect in the ability of the mutants to invade both cells was highly similar, suggesting that M. avium might have evolved mechanisms that are used to enter amoebas and human macrophages. uptake M ycobacterium avium complex is an intracellular pathogen that can infect a variety of host cells (1-4). M. avium, like the majority of pathogenic mycobacteria, infects and replicates within macrophages (5, 6), which are the phagocytic cells where M. avium establishes a long-term infection (7).A number of studies in vitro have determined that M. avium, in a manner similar to Mycobacterium tuberculosis, is taken up by macrophages using the complement receptors CR3, CR4, and CR1 (8-10), and/or the mannose receptor (8, 11). M. tuberculosis has been found to bind to the CD11b chain of the ␤-integrin of the CR3 and CR4 receptors, which happened without participation of the serum complement proteins (10). Other studies demonstrated that the mannose capped lipoarabinomannan antigen of virulent M. tuberculosis cell wall is capable to recognize and bind to the mannose receptors on the macrophage membrane (11).It has been hypothesized that virulent mycobacteria bind to many receptors because pathogenic mycobacteria would use several different receptors on the macrophage membrane to be internalized, as a strategy to guarantee phagocytosis, even when a sitespecific macrophage would not contain one or more membrane receptors. In addition, this property would address the possibility that mycobacteria may not express all of the ligands during all phases of infection. Most mycobacteria evolved to survive inside phagocytic cells, although they can enter ...

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“…GAPDH may associate with other cellular compartments, such as lysozymes (36), synaptic vesicles (37), the cytoskeleton (38), and the plasma membrane (39). As a small soluble protein, GAPDH might serve as a chaperone, translocating proteins between intracellular sites.…”

Section: Discussionmentioning

confidence: 99%

Glyceraldehyde-3-phosphate dehydrogenase: Nuclear translocation participates in neuronal and nonneuronal cell death

Sawa

Khan

Hester

et al. 1997

Proc. Natl. Acad. Sci. U.S.A.

308

219

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Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) protein levels increase in particulate fractions in association with cell death in HEK293 cells, S49 cells, primary thymocytes, PC12 cells, and primary cerebral cortical neuronal cultures. Subcellular fractionation and immunocytochemistry reveal that this increase primarily ref lects nuclear translocation. Nuclear GAPDH is tightly bound, resisting extraction by DNase or salt treatment. Treating primary thymocytes, PC12 cells, and primary cortical neurons with antisense but not sense oligonucleotides to GAPDH prevents cell death. Because cell-death-associated nuclear translocation of GAPDH and antisense protection occur in multiple neuronal and nonneuronal systems, we propose that GAPDH is a general mediator of cell death and uses nuclear translocation as a signaling mechanism.

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Bundling of microtubules by glyceraldehyde‐3‐phosphate dehydrogenase and its modulation by ATP

Cited by 179 publications

References 37 publications

Flocculation of Saccharomyces cerevisiae is induced by transformation with the GAP1 gene from Kluyveromyces marxianus

Flocculation of Saccharomyces cerevisiae is induced by transformation with the GAP1 gene from Kluyveromyces marxianus

Identification ofMycobacterium aviumpathogenicity island important for macrophage and amoeba infection

Glyceraldehyde-3-phosphate dehydrogenase: Nuclear translocation participates in neuronal and nonneuronal cell death

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