Insights regarding fungal phosphoproteomic analysis

Liliane F.C. Ribeiro, Cynthia L. Chelius, Steven D. Harris, Mark R. Marten

Research output: Contribution to journalReview articlepeer-review

5 Scopus citations


Protein phosphorylation is a major means of regulation for cellular processes, and is important in cell signaling, growth, and cell proliferation. To study phosphorylated proteins, high throughput phosphoproteomic technologies, such as reverse phase protein array, phospho-specific flow cytometry, and mass spectrometry (MS) based technologies, have been developed. Among them, mass spectrometry has become the primary tool employed for the identification of phosphoproteins and phosphosites in fungi, leading to an improved understanding of a number of signaling pathways. Using mass spectrometry techniques, researchers have discovered new kinase substrates, established connections between kinases and fungal pathogenicity, and studied the evolutionary lineage of kinases between different fungal species. Further, many specific phosphorylation sites recognized by individual kinases have been described. In this review, we will focus on recent discoveries made in yeast and filamentous fungi using phosphoproteomic analysis.

Original languageEnglish (US)
Pages (from-to)38-44
Number of pages7
JournalFungal Genetics and Biology
StatePublished - Jul 1 2017


  • Cellular regulation
  • Filamentous fungi
  • Mass spectrometry
  • Phosphorylation
  • Yeast

ASJC Scopus subject areas

  • Microbiology
  • Genetics


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