The phosphoproteome of Aspergillus nidulans reveals functional association with cellular processes involved in morphology and secretion

Nikhil Ramsubramaniam, Steven D. Harris, Mark R. Marten

Research output: Contribution to journalArticlepeer-review

15 Scopus citations

Abstract

We describe the first phosphoproteome of the model filamentous fungus Aspergillus nidulans. Phosphopeptides were enriched using titanium dioxide, separated using a convenient ultra-long reverse phase gradient, and identified using a "high-high" strategy (high mass accuracy on the parent and fragment ions) with higher-energy collisional dissociation. Using this approach 1801 phosphosites, from 1637 unique phosphopeptides, were identified. Functional classification revealed phosphoproteins were overrepresented under GO categories related to fungal morphogenesis: "sites of polar growth," "vesicle mediated transport," and "cytoskeleton organization." In these same GO categories, kinase-substrate analysis of phosphoproteins revealed the majority were target substrates of CDK and CK2 kinase families, indicating these kinase families play a prominent role in fungal morphogenesis. Kinase-substrate analysis also identified 57 substrates for kinases known to regulate secretion of hydrolytic enzymes (e.g. PkaA, SchA, and An-Snf1). Altogether this data will serve as a benchmark that can be used to elucidate regulatory networks functionally associated with fungal morphogenesis and secretion. All MS data have been deposited in the ProteomeXchange with identifier PXD000715 (http://proteomecentral.proteomexchange.org/dataset/PXD000715).

Original languageEnglish (US)
Pages (from-to)2454-2459
Number of pages6
JournalProteomics
Volume14
Issue number21-22
DOIs
StatePublished - Nov 1 2014

Keywords

  • Aspergillus nidulans
  • Morphology
  • Phosphoproteomic analysis
  • Secretion
  • Systems biology

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology

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