title: Insights regarding fungal phosphoproteomic analysis.
abstract: 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.
authors.affiliation: University of Maryland Baltimore County (UMBC), Department of Chemical, Biochemical and Environmental Engineering, United States.
authors.forename: Liliane F C
authors.initials: LFC
authors.lastname: Ribeiro
authors.affiliation: University of Maryland Baltimore County (UMBC), Department of Chemical, Biochemical and Environmental Engineering, United States.
authors.forename: Cynthia L
authors.initials: CL
authors.lastname: Chelius
authors.affiliation: University of Nebraska, Lincoln, Center for Plant Science Innovation, United States.
authors.forename: Steven D
authors.initials: SD
authors.lastname: Harris
authors.affiliation: University of Maryland Baltimore County (UMBC), Department of Chemical, Biochemical and Environmental Engineering, United States. Electronic address: marten@umbc.edu.
authors.forename: Mark R
authors.initials: MR
authors.lastname: Marten
mesh_terms: D005075:Biological Evolution; D020134:Catalytic Domain; D005656:Fungal Proteins / Q000378:metabolism*; D005658:Fungi / Q000378:metabolism* / Q000472:pathogenicity; D010750:Phosphoproteins / Q000378:metabolism*; D010766:Phosphorylation; D010770:Phosphotransferases / Q000378:metabolism; D040901:Proteomics
chemical_list: D005656:Fungal Proteins; D010750:Phosphoproteins; D010770:Phosphotransferases
keywords: Cellular regulation; Filamentous fungi; Mass spectrometry; Phosphorylation; Yeast