Fiorella Galello

Fiorella Galello
Universidad de Buenos Aires | UBA · Institute of Biological Chemistry of the Faculty of Natural Sciences (IQUIBICEN)

PhD

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13
Publications
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101
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Publications

Publications (13)
Article
In Saccharomyces cerevisiae cAMP regulates different cellular processes through PKA. The specificity of the response of the cAMP-PKA pathway is highly regulated. Here we address the mechanism through which the cAMP-PKA pathway mediates its response to heat shock and thermal adaptation in yeast. PKA holoenzyme is composed of a regulatory subunit dim...
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In Saccharomyces cerevisiae, cAMP regulates a number of different cellular processes, such as cell growth, metabolism, stress resistance and gene transcription. The intracellular target for this second messenger in yeast cells is the cAMP-dependent protein kinase (PKA). The way in which a broad specificity protein kinase mediates one right physiolo...
Article
Full-text available
Cellular responses to stress stem from a variety of different mechanisms, including translation arrest and relocation of the translationally repressed mRNAs to ribonucleoprotein particles like stress granules (SGs) and processing bodies (PBs). Here, we examine the role of PKA in the S. cerevisiae heat shock response. Under mild heat stress Tpk3 agg...
Data
Protein expression levels and biochemical analysis on granule-enriched fractions experiments. (A) Expression levels of each PKA subunit under exponential growth (30°C) or after heat stress conditions as described in Fig 1A (37°C or 46°C) were determined by immunoblot with anti-GFP. (B) Expression levels of translation factors in WT, tpk2Δ and tpk3Δ...
Data
Cell viability assay. Strains were grown to exponential phase at 30°C and subjected to 37°C 30 minutes, 46°C 10 minutes or 46° C 30 minutes. Cell viability was verified by spot assay. (TIF)
Data
Table A. Strains used in this study. Table B. Plasmids used in this study. Table C. Primers used in this study. (DOCX)
Article
Yeast cells can adapt their growth in response to the nutritional environment. Glucose is the favorite carbon source of Saccharomyces cerevisiae that prefers a fermentative metabolism despite the presence of oxygen. When glucose is consumed, the cell switches to the aerobic metabolism of ethanol, during the so-called diauxic shift. The difference b...
Article
The cAMP dependent protein kinase (PKA) signaling is a broad pathway that plays important roles in the transduction of environmental signals triggering precise physiological responses. However, how PKA achieves the cAMP-signal transduction specificity is still in study. The regulation of expression of subunits of PKA should contribute to the signal...
Article
Unlabelled: cAMP-dependent protein kinase mediates many extracellular signals in eukaryotes. The compartmentalization of PKA is an important level of control of the specificity of signal transduction mediated by cAMP. Unlike mammalian PKA for which proof insights in the mechanism that controls its localization through anchoring proteins (AKAPs) ha...
Article
Full-text available
The specificity in phosphorylation by kinases is determined by the molecular recognition of the peptide target sequence. In Saccharomyces cerevisiae, the protein kinase A (PKA) specificity determinants are less studied than in mammalian PKA. The catalytic turnover numbers of the catalytic subunits isoforms Tpk1 and Tpk2 were determined, and both en...
Article
We have previously shown that protein kinase A of the medically important zygomycete Mucor rouxii participates in fungal morphology through cytoskeletal organization. As a first step towards finding the link between protein kinase A and cytoskeletal organization we here demonstrate the cloning of the Rho1 gene and the characterization of its protei...

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Project (1)
Project
Sensing and transducing extracellular signals is a fundamental property of all living cells to adjust intracellular processes appropriately to changes in the environment. A classic example of such a second messenger is cAMP, which activates cAMP-dependent protein kinase hence affecting the properties of target proteins by reversible phosphorylation. Compartmentalization of signal transduction pathways has emerged as an important additional level of control to ensure sufficient specificity in cAMP-PKA signaling. In the unicellular eukaryote Saccharomyces cerevisiae, PKA controls the phosphorylation state of transcription activators/repressors, kinases and metabolic enzymes. Considering the pleiotropic role of PKA in a single cell and the diversity of substrates at different subcellular sites, regulatory mechanisms probably exist that ensure phosphorylation of the right substrates under the proper conditions. Budding yeast has only one PKA-regulatory subunit (Bcy1), whereas three different isoforms of catalytic subunits (Tpk1, Tpk2, Tpk3) are present. In vegetative cells, the different catalytic subunits seem to be functionally redundant. The kinase signaling pathway specificity depends on a dynamic interrelationship of several factors: the sequence around the phosphorylation site, the substrate and kinase expression levels, and the presence or absence of kinase anchor proteins that limit kinase–substrate interaction. Two aspects of cAMP–PKA signaling in yeast remain to be elucidated: the identification and characterization of anchoring proteins and the mechanism involved in the regulation of PKA subunits expression. There are evidences suggest that a complex mechanism regulates the expression of PKA subunits. We are studying the transcriptional and post-transcriptional regulation of each PKA subunit during stress condition.