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Label-free quantitative plasma membrane proteome analysis of Candida glabrata wild-type and Cgvps34∆ (lacks phosphatidylinositol 3- phosphate kinase, CgVps34) strains. Label-free quantitative plasma membrane proteome analysis of Candida glabrata wild-type and Cgvps34∆ (lacks phosphatidylinositol 3- phosphate kinase, CgVps34) strains.

ABSTRACT: The project is aimed at characterizing the effect of loss of phosphatidylinositol 3- phosphate kinase (CgVps34) on the plasma membrane proteome of Candida glabrata.

INSTRUMENT(S): Orbitrap Eclipse

ORGANISM(S): Candida Glabrata (yeast) (torulopsis Glabrata)

SUBMITTER: Rupinder Kaur

LAB HEAD: Rupinder Kaur

PROVIDER: PXD042056 | Pride | 2024-02-19

REPOSITORIES: Pride

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Dataset's files

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			Action	DRS
	FIZZA_CDFD_CADIDA_GLABRATA_ANALYSIS.pdResult	Other
	S1.raw	Raw
	S2.raw	Raw
	S3.raw	Raw
	S4.raw	Raw

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Publications

Phosphatidylinositol 3-phosphate regulates iron transport via PI3P-binding CgPil1 protein.

Askari Fizza F Vasavi Bhogadi B Kaur Rupinder R

Cell reports 20230724 8

Iron homeostasis, which is pivotal to virulence, is regulated by the phosphatidylinositol 3-kinase CgVps34 in the human fungal pathogen Candida glabrata. Here, we identify CgPil1 as a phosphatidylinositol 3-phosphate (PI3P)-binding protein and unveil its role in retaining the high-affinity iron transporter CgFtr1 at the plasma membrane (PM), with PI3P negatively regulating CgFtr1-CgPil1 interaction. PI3P production and its PM localization are elevated in the high-iron environment. Surplus iron a ...[more]

PMID: 37490387

Similar Datasets

Phosphatidylinositol 3-phosphate (PI3P) interactome analysis under varied iron conditions in Candida glabrata.

Project description:The project is aimed at identifying proteins that interact with PI3P in low-iron, regular-iron and high-iron grown Candida glabrata cells.

2024-02-19 | PXD042058 | Pride

Total membrane proteome analysis of Candida glabrata wild-type and eleven CgYapsins-deficient strain Cgyps1-11∆.

Project description:The project is aimed at characterizing the effect of loss of a family of eleven aspartyl proteases (Cg Yapsins) on the global membrane proteome of Candida glabrata.

2022-04-04 | PXD029614 | Pride

Label-free quantitative total membrane proteome analysis of Candida glabrata wild-type and eleven CgYapsins-deficient strain Cgyps1-11∆.

Project description:The project is aimed at characterizing the effect of loss of a family of eleven aspartyl proteases (Cg Yapsins) on the abundance of proteins in the total membrane factions of Candida glabrata.

2022-04-04 | PXD029629 | Pride

Interactome identification of a glycosylphosphatidylinositol-linked aspartyl protease, CgYps1, in the pathogenic yeast Candida glabrata

Project description:The major goal of this project is to identify proteins that interact with CgYps1 aspartyl protease in logarithmic-phase Candida glabrata cells.

2021-02-08 | PXD022766 | Pride

Secretome analysis of Candida glabrata wild-type and aspartyl protease-deficient strains

Project description:The project is aimed at characterizing the secretome of a human opportunistic fungal pathogen Candida glabrata. Additionally, the effect of loss of a family of eleven aspartyl proteases (Cg Yapsins) on the Candida glabrata secretome is studied.

2019-10-25 | PXD015131 | Pride

Candida glabrata transcription profile when grown under Niacin starvation or in human urine

Project description:The transcription profile of Candida glabrata grown under two different Niacin limitation conditions were determined. Condition 1 is comparing log phase C. glabrata cells (O.D. 0.5-0.6) grown in synthetic medium containing 0.016 uM versus 3.25 uM nicotinic acid (NA), a common form of Niacin. The NA concentration of 3.25 uM is the standard concentration in synthetic complete (SC) medium. Condition 2 is comparing log phase C. glabrata cells (O.D. 0.4-0.6) grown in 3 individual human urine samples (supplemented with 2% glucose) versus in SC medium. Keywords: transcriptional profiling by microarray GSM151863, GSM151869 are dye-swap experiment #1 and GSM151880, GSM151881 are dye-swap experiment #2 for Niacin limitation condition 1. GSM151934, GSM152116 are dye-swap experiment #1, GSM152118, GSM152119 are dye-swap experiment #2 and GSM152130, GSM152131 are dye-swap experiment #3 for Niacin limitation condition 2.

2010-06-05 | E-GEOD-6582 | biostudies-arrayexpress

Quantitative secretome profiling of Candida glabrata wild-type and aspartyl protease-deficient strains

Project description:The project is aimed at deciphering the proteins, which are differentially abundant in the secretome of Candida glabrata wild-type and a mutant strain deleted for eleven cell surface-associated aspartyl-proteases (CgYapsins).

2019-10-24 | PXD015147 | Pride

Secretome analysis of Candida glabrata aspartyl protease-deficient strains

Project description:The project is aimed at characterizing the effect of deletion of surface associated aspartyl protease(s) on the secretome of of the human opportunistic fungal pathogen Candida glabrata.

2019-10-24 | PXD015132 | Pride

Defining the transcriptome landscape of Candida glabrata during pH change and nitrosative stress by RNA-Seq

Project description:The yeast Candida glabrata is one of the most important human fungal pathogens and has emerged as a leading cause of nosocomial bloodstream infections. Its resistance to many routinely used antimycotics and its close relationship to the model organism Saccharomyces cerevisiae make this fungus an interesting target of biomedical research. Although the genome sequence was published a decade ago, little is known about the transcriptional dynamics within this pathogen, especially compared to other pathogenic and nonpathogenic yeasts.We provide a detailed RNA-Seq-based analysis of the transcriptomic landscape of C. glabrata in nutrient-rich media as well as under stress conditions and weak acidic and alkaline environments. Using state of the art bioinformatics tools, we were able to refine the annotation of the C. glabrata genome up to 5288 transcriptional active protein-coding ORFs. Introns were identified in 175 of these genes. Based on our data we were able to increase the number of noncoding RNAs to 68. Additionally, we could detect the expression of 50 novel ORFs. This comprehensive analysis of C. glabrataM-bM-^@M-^Ys transcriptomic landscape significantly enhances the annotation of current genome annotation and contributes to a further understanding of the molecular mechanisms of the pathogenicity of this medical important yeast. Candida glabrata was grown in standard nutrient-rich medium(wt_37), ph4(wt_pH4), ph8(w,_pH8) and in nitrosative stress (GSNO) conditions(wt_GSNO). After harvesting RNA, paired-end and strand-specific RNA-Seq was performed on three biological replicates after PolyA filtering respectively. Additionally, a fourth replicate without filtering was sequenced single-end and not strand-specific..

2015-01-27 | E-GEOD-61606 | biostudies-arrayexpress

Fluconazole-induced actin cytoskeleton remodeling requires phosphatidylinositol 3-phosphate 5-kinase in the pathogenic yeast Candida glabrata.

Project description:Known azole antifungal resistance mechanisms include mitochondrial dysfunction and overexpression of the sterol biosynthetic target enzyme and multidrug efflux pumps. Here, we identify, through a genetic screen, the vacuolar membrane-resident phosphatidylinositol 3-phosphate 5-kinase (CgFab1) to be a novel determinant of azole tolerance. We demonstrate for the first time that fluconazole promotes actin cytoskeleton reorganization in the emerging, inherently less azole-susceptible fungal pathogen Candida glabrata, and genetic or chemical perturbation of actin structures results in intracellular sterol accumulation and azole susceptibility. Further, CgFAB1 disruption impaired vacuole homeostasis and actin organization, and the F-actin-stabilizing compound jasplakinolide rescued azole toxicity in cytoskeleton defective-mutants including the Cgfab1Δ mutant. In vitro assays revealed that the actin depolymerization factor CgCof1 binds to multiple lipids including phosphatidylinositol 3,5-bisphosphate. Consistently, CgCof1 distribution along with the actin filament-capping protein CgCap2 was altered upon both CgFAB1 disruption and fluconazole exposure. Altogether, these data implicate CgFab1 in azole tolerance through actin network remodeling. Finally, we also show that actin polymerization inhibition rendered fluconazole fully and partially fungicidal in azole-susceptible and azole-resistant C. glabrata clinical isolates, respectively, thereby, underscoring the role of fluconazole-effectuated actin remodeling in azole resistance.

| S-EPMC6221164 | biostudies-literature

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