Exportin 1 (XPO1) mediates one of the most versatile protein transport pathways in the cell, exporting hundreds of different proteins from the nucleus to the cytoplasm. In this dissertation, I employ filamentous phage display coupled with high-throuput DNA sequencing to establish the sequence space of the most common type the nuclear export signals (NESes) recognized by XPO1. I confirm the role of the discovered sequence features in determining the nuclear export efficiency in the cell. I show the utility of the obtained information in engineering of NES-like sequences, including creating artificial NESes or NES-like sequences that bind XPO1 with high affinity. Additionally, I explore the use of the established sequence space parameters for prediction of NESes based on a protein sequence. This thesis could be of interest to biochemists and cell biologists interested in protein localization in the cell as well as specialists in protein-peptide interactions.
