Activation of the plasma membrane H+‐ATPase of Saccharomyces cerevisiae by glucose is mediated by dissociation of the H+‐ATPase–acetylated tubulin complex

Campetelli, Alexis N.; Previtali, Gabriela; Arce, Carlos A.; Barra, Héctor S.; Casale, César H.

doi:10.1111/j.1742-4658.2005.04959.x

Cited by 39 publications

(36 citation statements)

References 23 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…Furthermore tubulin seems to co-migrate with the P-type ATPase. Interestingly it was recently reported that acetylated tubulin interacts with and regulates the activity of the orthologous H ϩ -ATPase in yeast plasma membranes (63), and it is conceivable that it does the same also with the P-type ATPase in D. salina. Other reports demonstrated that tubulin interacts with plasma membranes in plants and algae and functions as a nucleation site for the association of microtubules and hence controls cell expansion and morphology (34,64,65).…”

Section: A Functional Network Involved In Salinity Tolerancementioning

confidence: 99%

Salt-induced Changes in the Plasma Membrane Proteome of the Halotolerant Alga Dunaliella salina as Revealed by Blue Native Gel Electrophoresis and Nano-LC-MS/MS Analysis

Katz

Waridel

Shevchenko

et al. 2007

Molecular & Cellular Proteomics

154

144

View full text Add to dashboard Cite

The halotolerant alga Dunaliella salina is a recognized model photosynthetic organism for studying plant adaptation to high salinity. The adaptation mechanisms involve major changes in the proteome composition associated with energy metabolism and carbon and iron acquisition. To clarify the molecular basis for the remarkable resistance to high salt, we performed a comprehensive proteomics analysis of the plasma membrane. Plasma membrane proteins were recognized by tagging intact cells with a membrane-impermeable biotin derivative. Proteins were resolved by two-dimensional blue native/SDS-PAGE and identified by nano-LC-MS/MS. Of 55 identified proteins, about 60% were integral membrane or membraneassociated proteins. We identified novel surface coat proteins, lipid-metabolizing enzymes, a new family of membrane proteins of unknown function, ion transporters, small GTP-binding proteins, and heat shock proteins. The abundance of 20 protein spots increased and that of two protein spots decreased under high salt. The major salt-regulated proteins were implicated in protein and membrane structure stabilization and within signal transduction pathways. The migration profiles of native protein complexes on blue native gels revealed oligomerization or co-migration of major surface-exposed proteins, which may indicate mechanisms of stabilization at high salinity. Molecular & Cellular Proteomics 6:1459 -1472, 2007.The halotolerant alga Dunaliella salina uses a unique osmoregulatory mechanism and is able to proliferate in environments with extreme salt content (1). This is achieved through remarkable changes in metabolism and ion transport brought about by up-regulation or down-regulation of multiple enzymes and membrane proteins. Elucidation of the molecular basis for this remarkable adaptation might provide tools to improve the resistance of crop plants to the progressive salinization of soils, which is already a major limitation for agricultural productivity worldwide. By characterizing the changes in the soluble subproteome of D. salina, we demonstrated previously that the alga responds to hypersaline conditions by up-regulating key enzymes in photosynthetic CO 2 fixation and in energy metabolism that divert carbon metabolism to massive synthesis of glycerol, the osmotic element in Dunaliella (2).Salinity stress destabilizes biological membranes and affects the solubility of many essential substrates and ions (3). Adaptation to salinity stress might also alter the composition and organization of the membrane proteome associated with the stabilization and enhancement of ion transporters. Early studies revealed the accumulation of two carbonic anhydrases, dCAI 1 and dCAII (4, 5), and a transferrin-like protein (6) that presumably compensated the impaired availability of bicarbonate and iron under high salt. Salt-induced changes in organellar membranes, such as the expression of ER fatty acid elongase, were also reported (7). High salinity also affects sodium transport (8), lipid organization (9, 10), and activation of PM pr...

show abstract

Section: A Functional Network Involved In Salinity Tolerancementioning

confidence: 99%

Salt-induced Changes in the Plasma Membrane Proteome of the Halotolerant Alga Dunaliella salina as Revealed by Blue Native Gel Electrophoresis and Nano-LC-MS/MS Analysis

Katz

Waridel

Shevchenko

et al. 2007

Molecular & Cellular Proteomics

154

144

View full text Add to dashboard Cite

show abstract

“…All protein-lipid “islands” are also thought to be bound to cytoskeleton elements [23]. This idea has aroused particular interest due to the finding of an acetylated tubulin-Pma1 complex in glucose-starved yeast and its dissociation under glucose addition [24]. Research has shown that the acetylated tubulin-Pma1 complex is dissociated very rapidly and that the glucose-induced increase in Pma1 activity occurs after its disintegration [24].…”

Section: Introductionmentioning

confidence: 99%

“…This idea has aroused particular interest due to the finding of an acetylated tubulin-Pma1 complex in glucose-starved yeast and its dissociation under glucose addition [24]. Research has shown that the acetylated tubulin-Pma1 complex is dissociated very rapidly and that the glucose-induced increase in Pma1 activity occurs after its disintegration [24]. On the other hand, in S. cerevisiae , the formation and stability of Pma1-containing patches have been shown not to depend on the integrity of the actin and tubulin structures [25].…”

Section: Introductionmentioning

confidence: 99%

Activation of H+-ATPase of the Plasma Membrane of Saccharomyces cerevisiae by Glucose: The Role of Sphingolipid and Lateral Enzyme Mobility

2012

View full text Add to dashboard Cite

Activation of the plasma membrane H+-ATPase of the yeast Saccharomyces cerevisiae by glucose is a complex process that has not yet been completely elucidated. This study aimed to shed light on the role of lipids and the lateral mobility of the enzyme complex during its activation by glucose. The significance of H+-ATPase oligomerization for the activation of H+-ATPase by glucose was shown using the strains lcb1-100 and erg6, with the disturbed synthesis of sphyngolipid and ergosterol, respectively. Experiments with GFP-fused H+-ATPase showed a decrease in fluorescence anisotropy during the course of glucose activation, suggesting structural reorganization of the molecular domains. An immunogold assay showed that the incubation with glucose results in the spatial redistribution of ATPase complexes in the plasma membrane. The data suggest that (1) to be activated by glucose, H+-ATPase is supposed to be in an oligomeric state, and (2) glucose activation is accompanied by the spatial movements of H+-ATPase clusters in the PM.

show abstract

“…The process of proton extrusion is a phenomenon associated with enzyme activity which is stimulated in presence of glucose [33]. The inhibition of this protein causes the intracellular acidification which may result in cell death.…”

Section: Resultsmentioning

confidence: 99%

Effect of quinoline based 1,2,3-triazole and its structural analogues on growth and virulence attributes of Candida albicans

et al. 2017

View full text Add to dashboard Cite

Candida albicans, along with some other non-albicans Candida species, is a group of yeast, which causes serious infections in humans that can be both systemic and superficial. Despite the fact that extensive efforts have been put into the discovery of novel antifungal agents, the frequency of these fungal infections has increased drastically worldwide. In our quest for the discovery of novel antifungal compounds, we had previously synthesized and screened quinoline containing 1,2,3-triazole (3a) as a potent Candida spp inhibitor. In the present study, two structural analogues of 3a (3b and 3c) have been synthesized to determine the role of quinoline and their anti-Candida activities have been evaluated. Preliminary results helped us to determine 3a and 3b as lead inhibitors. The IC50 values of compound 3a for C. albicans ATCC 90028 (standard) and C. albicans (fluconazole resistant) strains were 0.044 and 2.3 μg/ml, respectively while compound 3b gave 25.4 and 32.8 μg/ml values for the same strains. Disk diffusion, growth and time kill curve assays showed significant inhibition of C. albicans in the presence of compounds 3a and 3b. Moreover, 3a showed fungicidal nature while 3b was fungistatic. Both the test compounds significantly lower the secretion of proteinases and phospholipases. While, 3a inhibited proteinase secretion in C. albicans (resistant strain) by 45%, 3b reduced phospholipase secretion by 68% in C. albicans ATCC90028 at their respective MIC values. Proton extrusion and intracellular pH measurement studies suggested that both compounds potentially inhibit the activity of H+ ATPase, a membrane protein that is crucial for various cell functions. Similarly, 95–97% reduction in ergosterol content was measured in the presence of the test compounds at MIC and MIC/2. The study led to identification of two quinoline based potent inhibitors of C. albicans for further structural optimization and pharmacological investigation.

show abstract

Activation of the plasma membrane H⁺‐ATPase of Saccharomyces cerevisiae by glucose is mediated by dissociation of the H⁺‐ATPase–acetylated tubulin complex

Cited by 39 publications

References 23 publications

Salt-induced Changes in the Plasma Membrane Proteome of the Halotolerant Alga Dunaliella salina as Revealed by Blue Native Gel Electrophoresis and Nano-LC-MS/MS Analysis

Salt-induced Changes in the Plasma Membrane Proteome of the Halotolerant Alga Dunaliella salina as Revealed by Blue Native Gel Electrophoresis and Nano-LC-MS/MS Analysis

Activation of H+-ATPase of the Plasma Membrane of Saccharomyces cerevisiae by Glucose: The Role of Sphingolipid and Lateral Enzyme Mobility

Effect of quinoline based 1,2,3-triazole and its structural analogues on growth and virulence attributes of Candida albicans

Contact Info

Product

Resources

About