FPD: A comprehensive phosphorylation database in fungi.

Area of Science:

• * Molecular Biology
• * Biochemistry
• * Mycology

Background:

• * Protein phosphorylation is a crucial post-translational modification regulating key cellular processes like cell cycle and signal transduction.
• * Existing data on fungal phosphorylation is limited, hindering comprehensive research in this area.
• * Understanding fungal phosphorylation is vital for fields ranging from basic biology to agricultural and medical applications.

Purpose of the Study:

• * To establish a centralized, high-confidence resource for fungal phosphorylation data.
• * To identify and characterize novel phosphorylation motifs specific to fungi.
• * To facilitate comparative analysis of phosphorylation patterns across different eukaryotic kingdoms.

Main Methods:

• * Compilation of high-confidence in vivo phosphosites identified through MS-based proteomics.
• * Data curation and integration from eight diverse fungal species.
• * Comparative motif analysis of phosphorylation sites across fungi, plants, and animals.

Main Results:

• * Creation of the Fungi Phosphorylation Database (FPD) with 62,272 non-redundant phosphosites in 11,222 proteins.
• * Coverage of eight significant fungal species, including model organisms and pathogens.
• * Discovery of a fungi-specific phosphothreonine motif and other conserved phosphorylation patterns.

Conclusions:

• * The FPD provides a valuable resource for fungal research, enabling deeper insights into cellular regulation.
• * Identification of novel motifs enhances the understanding of kinase specificity and signaling networks in fungi.
• * Comparative analysis highlights both conserved and unique aspects of phosphorylation across eukaryotes.