STRCTURAL STUDIES OF THE GOLGI REASSEMBLY AND STACKING PROTEIN (GRASP) FROM TRYPANOSOMA CRUZI

The Golgi complex is part of the endomembrane system in eukaryotic cells, and its primary function is to receive transport cargo from the endoplasmic reticulum, modify it, and direct it to its final destinations. Although not much is known about the mechanisms that define its cellular shape, it is understood that the structure and function of the Golgi complex are closely correlated. The organization and function of the Golgi require Golgi matrix proteins that assist in connecting the cisternae of the organelle. One specific type of protein that performs this function is the Golgi reassembly and stacking protein (GRASP), which is also involved in other processes, such as unconventional protein secretion mechanisms. The flagellated protozoan Trypanosoma cruzi possesses organelles similar to those of eukaryotic cells, including the Golgi complex. Therefore, it is inferred that GRASPs are present in T. cruzi and likely participate in the secretion process. The study used biophysical and biochemical techniques, such as electrophoresis, circular dichroism (CD), fluorescence, and microscopic experiments for phase separation observation (LLPS). Although there is no structural information available about Trypanosoma cruzi GRASP (TcGRASP), it is understood that studying and biochemically characterizing this protein can lead to a better understanding of the function of this protein family and its relevance to the life cycle of parasites in the Trypanosomatidae family. Also, studying this structure is important because a better understanding of this parasite's life cycle could potentially aid in developing drugs to treat Chagas disease.

Financial support: FAPESP, CNPq.