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Proteomic analysis of Rta2p-dependent raft-association of detergent-resistant membranes in Candida albicans
- Source :
- PLoS ONE, Vol 7, Iss 5, p e37768 (2012), PLoS ONE
- Publication Year :
- 2012
- Publisher :
- Public Library of Science (PLoS), 2012.
-
Abstract
- In Candida albicans, lipid rafts (also called detergent-resistant membranes, DRMs) are involved in many cellular processes and contain many important proteins. In our previous study, we demonstrated that Rta2p was required for calcineurin-mediated azole resistance and sphingoid long-chain base release in C. albicans. Here, we found that Rta2p was co-localized with raft-constituted ergosterol on the plasma membrane of C. albicans. Furthermore, this membrane expression pattern was totally disturbed by inhibitors of either ergosterol or sphingolipid synthesis. Biochemical fractionation of DRMs together with immunoblot uncovered that Rta2p, along with well-known DRM-associated proteins (Pma1p and Gas1p homologue), was associated with DRMs and their associations were blocked by inhibitors of either ergosterol or sphingolipid synthesis. Finally, we used the proteomic analysis together with immunoblot and identified that Rta2p was required for the association of 10 proteins with DRMs. These 5 proteins (Pma1p, Gas1p homologue, Erg11p, Pmt2p and Ali1p) have been reported to be DRM-associated and also that Erg11p is a well-known target of azoles in C. albicans. In conclusion, our results showed that Rta2p was predominantly localized in lipid rafts and was required for the association of certain membrane proteins with lipid rafts in C. albicans.
- Subjects :
- Proteomics
Antifungal Agents
Lipoproteins
Science
Gene Expression
Yeast and Fungal Models
Mycology
Biology
Protein Engineering
Biochemistry
Microbiology
chemistry.chemical_compound
Membrane Microdomains
Model Organisms
Candida albicans
Molecular Cell Biology
Protein Interactions
Integral membrane protein
Lipid raft
Fluconazole
Ergosterol
Multidisciplinary
Fungi
Membrane Proteins
Proteins
biology.organism_classification
Sphingolipid
Corpus albicans
Cell biology
Transport protein
Protein Transport
chemistry
Membrane protein
Medicine
Protein Translation
lipids (amino acids, peptides, and proteins)
Protein Abundance
Protein Binding
Research Article
Subjects
Details
- Language :
- English
- ISSN :
- 19326203
- Volume :
- 7
- Issue :
- 5
- Database :
- OpenAIRE
- Journal :
- PLoS ONE
- Accession number :
- edsair.doi.dedup.....bb851c4fc6d0008be456475410c66d23