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PXD027612

PXD027612 is an original dataset announced via ProteomeXchange.

Dataset Summary
TitleThe SR protein kinase Sky2 is involved in regulation of dipeptide transport in Candida albicans
DescriptionMetabolic adaption to different host niches is one of the most important virulence traits of human fungal pathogens. The metabolic versatility of fungi and other cellular processes such as proliferation, morphogenesis and stress responses are tightly regulated by complex networks in which protein kinases play a crucial role. Serine-arginine (SR) protein kinases are highly conserved in all eukaryotes, but their function in pathogenic Candida spp. has not yet been investigated. C. albicans genome encodes two (Sky1, Sky2) and Candida glabrata one (Sky1) homolog of the human SR protein kinase 1 (SRPK1). We utilized deletion strains of the respective genes in both fungi in order to examine their cellular functions. C. glabrata and C. albicans strains lacking SKY1 exhibited higher resistance to osmotic stress and toxic polyamine concentrations to their ortholog in the model yeast Saccharomyces cerevisiae Sky1. Deletion of SKY2 in C. albicans resulted in impaired utilization of dipeptides as the sole nitrogen source. Subsequent phosphoproteomic analysis identified Ptr22, a transporter of di- and tri-peptides in C. albicans, as a potential Sky2 substrate. Overexpression of PTR22 in the sky2∆ restored the ability to grow on dipeptides as the sole nitrogen source and rendered the cells more susceptible to the dipeptide antibiotics Polyoxin D and Nikkomycin Z. Altogether, our results demonstrate that the two SR-like protein kinases in C. albicans have divergent functions: C. albicans and C. glabrata Sky1 is functionally similar to Sky1 in S. cerevisiae, whereas Sky2 regulates uptake of dipeptides.
HostingRepositoryPRIDE
AnnounceDate2022-05-09
AnnouncementXMLSubmission_2022-05-09_09:21:49.865.xml
DigitalObjectIdentifier
ReviewLevelPeer-reviewed dataset
DatasetOriginOriginal dataset
RepositorySupportUnsupported dataset by repository
PrimarySubmitterThomas Krüger
SpeciesList scientific name: Candida albicans (Yeast); NCBI TaxID: 5476;
ModificationListphosphorylated residue; acetylated residue; monohydroxylated residue; iodoacetamide derivatized residue
InstrumentQ Exactive HF
Dataset History
RevisionDatetimeStatusChangeLog Entry
02021-07-27 22:47:02ID requested
12022-05-09 09:21:50announced
Publication List
Dataset with its publication pending
Keyword List
submitter keyword: Candida albicans, phosphoproteomics, protein kinase, LC-MS/MS, Sky2
Contact List
Axel A. Brakhage
contact affiliationStress- and Immunoproteomics group Department of Molecular and Applied Microbiology Leibniz Institute for Natural Product Research and Infection Biology - Hans Knöll Institute Jena
contact emailaxel.brakhage@leibniz-hki.de
lab head
Thomas Krüger
contact affiliationLeibniz Institute for Natural Product Research and Infection Biology - Hans Knöll Institute
contact emailthomas.krueger@leibniz-hki.de
dataset submitter
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