Abstract
OFD1 is a protein involved in many cellular processes, including cilia biogenesis, mitotic spindle assembly, translation, autophagy and the repair of double-strand DNA breaks. Despite many potential interactors identified in high-throughput studies, only a few have been directly confirmed with their binding sites identified. We performed an analysis of the evolutionary conservation of the OFD1 sequence in three clades: 80 Tetrapoda, 144 Vertebrata or 26 Animalia species, and identified 59 protein-binding motifs localized in the OFD1 regions conserved in various clades. Our results indicate that OFD1 contains 14 potential post-translational modification (PTM) sites targeted by at least eight protein kinases, seven motifs bound by proteins recognizing phosphorylated aa residues and a binding site for phosphatase 2A. Moreover, OFD1 harbors both a motif that enables its phosphorylation by mitogen-activated protein kinases (MAPKs) and a specific docking site for these proteins. Generally, our results suggest that OFD1 forms a scaffold for interaction with many proteins and is tightly regulated by PTMs and ligands. Future research on OFD1 should focus on the regulation of OFD1 function and localization.