PXD001844

PXD001844 is an original dataset announced via ProteomeXchange.

Title	Analysis of the Candida albicans phosphoproteome
Description	Candida albicans is an important human fungal pathogen in both immunocompetent and immunocompromised individuals. In response to environmental stimuli, C. albicans regulates complex phenotypic transitions between morphological states, mating competence, and biofilm formation. In addition, other processes related to virulence, stress resistance, and cell wall structure are also highly regulated. Based on the phenotypes of mutants lacking different kinases, it is clear that protein phosphorylation plays an important role in the regulation of these pathways. Here, we present a qualitative analysis of the phosphoproteome of C. albicans hyphae. We identified 19,590 unique peptides that corresponded to 15,906 unique phosphosites on 2,896 proteins. The ratios of serine, threonine and tyrosine phosphosites were 80.01%, 18.11%, and 1.81%, respectively. The majority of proteins (2,111) contained at least two detected phosphorylation sites. Consistent with findings in other fungi, cytoskeletal proteins were among the most highly phosphorylated proteins, and there were differences in GO terms for proteins with serine and threonine versus tyrosine phosphorylation sites. This large-scale analysis identified phosphosites in protein components of Mediator, an important transcriptional co-regulatory protein complex. In vitro studies revealed Cdk8 (Ssn3), a kinase within the Mediator complex, was sufficient to catalyze a subset of these phosphorylations suggesting the potential for autoregulation. These data represent the deepest single analysis of a fungal phosphoproteome, and will lay the groundwork for future analyses of the C. albicans phosphoproteome and specific phosphoproteins.
HostingRepository	PRIDE
AnnounceDate	2015-03-25
AnnouncementXML	Submission_2015-03-25_04:54:14.xml
DigitalObjectIdentifier	https://dx.doi.org/10.6019/PXD001844
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Supported dataset by repository
PrimarySubmitter	Arminja Kettenbach
SpeciesList	scientific name: Candida albicans (Yeast); NCBI TaxID: 5476;
ModificationList	Oxidation; Dimethyl; Phospho; Dimethyl:2H(6)13C(2); Carbamidomethyl
Instrument	Q Exactive; Orbitrap Fusion

Revision	Datetime	Status	ChangeLog Entry
0	2015-02-25 05:28:10	ID requested
⏵ 1	2015-03-25 04:54:15	announced

Willger SD, Liu Z, Olarte RA, Adamo ME, Stajich JE, Myers LC, Kettenbach AN, Hogan DA, Analysis of the Candida albicans Phosphoproteome. Eukaryot Cell, 14(5):474-85(2015) [pubmed]

curator keyword: Biological

submitter keyword: Candida albicans, phosphoproteome

Arminja Kettenbach
contact affiliation	Department of Biochemistry Geisel School of Medicine at Dartmouth
contact email	arminja@dartmouth.edu
lab head
Arminja Kettenbach
contact affiliation	Dartmouth Med School
contact email	arminja@dartmouth.edu
dataset submitter

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PRIDE project URI

• PRIDE
  1. PXD001844
     1. Label: PRIDE project
     2. Name: Analysis of the Candida albicans phosphoproteome