A novel protein, CSG2p, is required for Ca2+ regulation in Saccharomyces cerevisiae.

Beeler, Troy; Gable, Kenneth; Zhao, Calvin; Dunn, Teresa M.

doi:10.1016/s0021-9258(17)37280-0

Cited by 104 publications

(19 citation statements)

References 35 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…68 Furthermore, two of the proteins in Fig. S4 (ESI†), namely CSG2 and SLM1, interact directly or indirectly with calcium ions: CSG2 is a regulatory protein that has a binding site for calcium, 69 and mediates in the cation translocation across cell membranes, and its release; 70 SLM1, is a substrate of the Ca 2+ -dependent calcineurin, which promotes yeast survival in environmental stress conditions through sphingolipid-mediated processes. 71 Hence, protein–protein network analysis suggested that the yeast response to gadolinium through sphingolipid-related processes might have included the modulation of vesicle-mediated transport and the repurposing of calcium regulatory processes to promote metal efflux.…”

Section: Resultsmentioning

confidence: 99%

Delineating toxicity mechanisms associated with MRI contrast enhancement through a multidimensional toxicogenomic profiling of gadolinium

Pallares

Hébert

et al. 2022

Mol. Omics

View full text Add to dashboard Cite

show abstract

Section: Resultsmentioning

confidence: 99%

Delineating toxicity mechanisms associated with MRI contrast enhancement through a multidimensional toxicogenomic profiling of gadolinium

Pallares

Hébert

et al. 2022

Mol. Omics

View full text Add to dashboard Cite

show abstract

“…It has an EF-Ca + + -binding domain and 9-10 predicted transmembrane domains. 26,257 As discussed below, it is likely that IPC is delivered to the Golgi apparatus with the inositol-phosphate head group facing the cytosol. It is then flipped across the membrane so that it can be mannosylated in the lumen of the Golgi.…”

Section: Sphingolipid Biosynthetic Pathway: Genes Enzymes and Phenotypesmentioning

confidence: 99%

“…61,107 Potential processes signalled by one or more of these compounds are trehalose accumulation and induction of transcription of TPS2, encoding a subunit of trehalose synthase. 61 Calcium homeostasis or components in calciummediated signalling pathways may be regulated by sphingolipids or vice versa, 26,56,193,303 but the mechanisms await characterization. It has been suggested that ceramide regulates cell cycle arrest at G1 via a pathway that utilizes a ceramideactivated protein phosphatase encoded by SIT4, TPD3 and CYC55.…”

Section: Cellular Location Sites Of Synthesis and Functions Of Sphingolipidsmentioning

confidence: 99%

Biochemistry, cell biology and molecular biology of lipids ofSaccharomyces cerevisiae

Daum

Lees

Bard

et al. 1998

Yeast

580

380

View full text Add to dashboard Cite

The yeast Saccharomyces cerevisiae is a powerful experimental system to study biochemical, cell biological and molecular biological aspects of lipid synthesis. Most but not all genes encoding enzymes involved in fatty acid, phospholipid, sterol or sphingolipid biosynthesis of this unicellular eukaryote have been cloned, and many gene products have been functionally characterized. Less information is available about genes and gene products governing the transport of lipids between organelles and within membranes, turnover and degradation of complex lipids, regulation of lipid biosynthesis, and linkage of lipid metabolism to other cellular processes. Here we summarize current knowledge about lipid biosynthetic pathways in S. cerevisiae and describe the characteristic features of the gene products involved. We focus on recent discoveries in these fields and address questions on the regulation of lipid synthesis, subcellular localization of lipid biosynthetic steps, cross‐talk between organelles during lipid synthesis and subcellular distribution of lipids. Finally, we discuss distinct functions of certain key lipids and their possible roles in cellular processes. © 1998 John Wiley & Sons, Ltd.

show abstract

“…Proper Ca 2+ concentration in the endoplasmic reticulum (ER) organelle is critical to its functions; in S. cerevisiae it is maintained at 10 μ M ( Strayle et al, 1999 ), well below the concentration found in this compartment in higher eukaryotes, where it is the main internal storage for calcium ions ( Stefan C. J. et al, 2013 ). Cls2/Csg2, an ER-localized protein, was originally proposed to play a role in Ca 2+ efflux from the ER ( Beeler et al, 1994 ; Tanida et al, 1996 ). However, Csg2 is likely implicated in the mannosylation of the inositol-phosphoceramide (IPC), corroborating the evidences about the sphingolipid roles in regulating ionic channels ( Birchwood et al, 2001 ; Montefusco et al, 2014 ).…”

Section: Biological Backgroundmentioning

confidence: 99%

Modeling Calcium Signaling in S. cerevisiae Highlights the Role and Regulation of the Calmodulin-Calcineurin Pathway in Response to Hypotonic Shock

Spolaor

Rovetta

Nobile

et al. 2022

Front. Mol. Biosci.

View full text Add to dashboard Cite

Calcium homeostasis and signaling processes in Saccharomyces cerevisiae, as well as in any eukaryotic organism, depend on various transporters and channels located on both the plasma and intracellular membranes. The activity of these proteins is regulated by a number of feedback mechanisms that act through the calmodulin-calcineurin pathway. When exposed to hypotonic shock (HTS), yeast cells respond with an increased cytosolic calcium transient, which seems to be conditioned by the opening of stretch-activated channels. To better understand the role of each channel and transporter involved in the generation and recovery of the calcium transient—and of their feedback regulations—we defined and analyzed a mathematical model of the calcium signaling response to HTS in yeast cells. The model was validated by comparing the simulation outcomes with calcium concentration variations before and during the HTS response, which were observed experimentally in both wild-type and mutant strains. Our results show that calcium normally enters the cell through the High Affinity Calcium influx System and mechanosensitive channels. The increase of the plasma membrane tension, caused by HTS, boosts the opening probability of mechanosensitive channels. This event causes a sudden calcium pulse that is rapidly dissipated by the activity of the vacuolar transporter Pmc1. According to model simulations, the role of another vacuolar transporter, Vcx1, is instead marginal, unless calcineurin is inhibited or removed. Our results also suggest that the mechanosensitive channels are subject to a calcium-dependent feedback inhibition, possibly involving calmodulin. Noteworthy, the model predictions are in accordance with literature results concerning some aspects of calcium homeostasis and signaling that were not specifically addressed within the model itself, suggesting that it actually depicts all the main cellular components and interactions that constitute the HTS calcium pathway, and thus can correctly reproduce the shaping of the calcium signature by calmodulin- and calcineurin-dependent complex regulations. The model predictions also allowed to provide an interpretation of different regulatory schemes involved in calcium handling in both wild-type and mutants yeast strains. The model could be easily extended to represent different calcium signals in other eukaryotic cells.

show abstract

A novel protein, CSG2p, is required for Ca2+ regulation in Saccharomyces cerevisiae.

Cited by 104 publications

References 35 publications

Delineating toxicity mechanisms associated with MRI contrast enhancement through a multidimensional toxicogenomic profiling of gadolinium

Delineating toxicity mechanisms associated with MRI contrast enhancement through a multidimensional toxicogenomic profiling of gadolinium

Biochemistry, cell biology and molecular biology of lipids ofSaccharomyces cerevisiae

Modeling Calcium Signaling in S. cerevisiae Highlights the Role and Regulation of the Calmodulin-Calcineurin Pathway in Response to Hypotonic Shock

Contact Info

Product

Resources

About