Impact of N-terminal Acetylation on the structure and molecular interactions of the "GRASP65 homolog protein 1" from Saccharomyces cerevisiae

• Grant number: 23/12516-3
• Support Opportunities: Scholarships in Brazil - Master
• Start date: February 01, 2024
• End date: October 31, 2025
• Field of knowledge: Biological Sciences - Biophysics - Molecular Biophysics
• Principal Investigator: Luis Felipe Santos Mendes
• Grantee: Mayra Tamires Santos Silva
• Host Institution: Instituto de Física de São Carlos (IFSC). Universidade de São Paulo (USP). São Carlos , SP, Brazil
• Associated research grant: 22/06006-0 - Elucidating the impact of functional protein liquid and solid condensates in the secretory pathway, AP.GR

Abstract

The Golgi Complex, a vital organelle in eukaryotic cells, plays crucial roles in modifying, storing, and transporting proteins and lipids. Its distinctive architecture is primarily shaped by the Golgi Reassembly and Stacking Proteins (GRASP) and Golgins. The importance of these proteins in Golgi organization is widely recognized, yet a precise understanding of how they modulate the Golgi's architecture, especially at the molecular level, remains elusive.Recently, advancements in understanding the biochemical and biophysical properties of proteins associated with the Golgi, including GRASP and Golgins, have shed new light on Golgi organization, challenging traditional notions. However, the exact molecular mechanisms by which these proteins influence the Golgi's structure remain enigmatic.The membrane anchoring of GRASPs involves a critical post-translational modification at the N-terminal. Yet, studies on these proteins often employ heterologous expressions in prokaryotic systems, which cannot make these necessary modifications.Our project aims to unravel this mystery. We will establish a protocol to investigate the role of N-terminal acetylation in the molecular interactions of the GRASP homolog protein from Saccharomyces cerevisiae (ScGRASP) in biological membrane models. Through this, we intend to provide experimental data that will significantly enhance our understanding of the molecular mechanisms governing the architecture of the Golgi Complex.