Sam Calis

Approximately 80% of all proteins are N-terminally acetylated, yet the functional impact of this co-/post-translational modification has remained largely unknown since its discovery. The enzyme complex mainly responsible is N-terminal acetyltransferase A (NatA). Mutations in the genes encoding the subunits play a role in multiple disorders, including cancer. Depending on the context, they can act both as oncogenes or as tumor suppressors. An example is NAA10 which codes for NAA10p, the catalytic subunit of NatA. NAA10p has a major role in proliferation, migration, differentiation and more, affecting numerous downstream targets. 
Using CRISPR-edited HAP1 cell lines carrying mutations in NAA10, I will apply several mass spectrometry-based techniques to identify changes in secondary and tertiary protein structures on a proteome scale. These techniques include Thermal Proteome Profiling (TPP) and Limited Proteolysis-Coupled Mass Spectrometry (LiP-MS). The aim is to gain fundamental insights in how defective N-terminal acetylation affects protein conformation and stability, supporting potential applications in many areas of cancer research.
 

• MSc in Bioscience Engineering: Cell and Gene Biotechnology, major in Medical Biotechnology
   

• Lab address: Technologiepark-Zwijnaarde 75, UGent-VIB Research Building FSVMII, 9052 Ghent
• Center for Medical Biotechnology  
• Department of Biomolecular Medicine 
• Gevaert lab  
• LinkedIn 
• ORCID