Article of Significant Interest Selected from This Issue by the Editors.

Many pathways in fungi are regulated in part by protein phosphorylation, but there are only a few studies that characterize fungal phosphoproteomes. Willger et al. (p. 474 – 485) have analyzed the phosphoproteome of the human fungal pathogen Candida albicans in its filamentous form. More than 15,906 phosphorylation sites on 2,896 proteins were identified. GO term enrichment analysis of proteins with serine/threonine or tyrosine phosphorylations found interesting differences. Many of the subunits of the transcriptional coregulator Mediator were phosphorylated and in vitro analyses found that the Cdk8 subunit of Mediator was capable of catalyzing many of these phosphorylations. These data will advance both targeted and large-scale phosphoprotein analyses in C. albicans and other fungi.