Characterization of GEXP15 as a Potential Regulator of Protein Phosphatase 1 in Plasmodium falciparum

The Protein Phosphatase type 1 catalytic subunit (PP1c) (PF3D7_1414400) operates in combination with various regulatory proteins to specifically direct and control its phosphatase activity. However, there is little information about this regulators the human malaria parasite, Plasmodium falciparum. To address knowledge gap, we conducted a comprehensive investigation into structural functional characteristics of conserved Plasmodium-specific regulator called Gametocyte EXported 15, GEXP15 (PF3D7_1031600). Through silico analysis, identified three significant regions interest GEXP15: an N-terminal region housing PP1-interacting RVxF motif, domain whose function unknown, GYF-like that potentially facilitates specific protein–protein interactions. further elucidate role GEXP15, vitro interaction studies demonstrated between PP1 via RVxF-binding motif. This was found enhance activity PP1. Additionally, utilizing transgenic GEXP15-tagged line live microscopy, observed high expression late asexual stages localization predominantly nucleus. Immunoprecipitation assays followed by mass spectrometry analyses revealed ribosomal- RNA-binding proteins. Furthermore, through pull-down recombinant domains His-tagged confirmed binding ribosomal complex GYF domain. Collectively, our study sheds light on PfGEXP15–PP1–ribosome interaction, which plays crucial protein translation. These findings suggest PfGEXP15 could serve as potential target for development drugs.