Biophysical Characterization of the Golgi Reassembly and Stacking Protein from Plasmodium falciparum

Abstract

GRASPs, a family of peripheral membrane-associated proteins, were initially recognized as essential factors in the reassembly of Golgi cisternae after mitotic events. More recently, their involvement in unconventional protein secretion (UPS) pathways has emerged as a more significant aspect than their role as Golgi structural factors. UPS has garnered considerable attention due to its crucial role in cellular homeostasis and the implications of its dysregulation. Nevertheless, there is still a lack of comprehensive understanding regarding the molecular mechanisms underlying UPS. Several key features have been identified within UPS pathways, particularly their participation in cellular stress responses. The precise function of GRASPs in these UPS pathways is only beginning to be unveiled. In this project, we aim to investigate the biophysical/biochemical properties of the GRASPs from P. falciparum (PfGRASP), the causative agent of malaria. Specifically, we intend to express, purify, and characterize the behavior of PfGRASP in solution, comparing it to the pattern of intrinsic disorder previously observed by our group for other GRASPs. Additionally, we will test the liquid-liquid phase separation capacity of PfGRASP, thus helping to determine whether the formation of protein biocondensates is another common property among all family members.