A new study exploring the NUDIX hydrolases in human cells provides attractive opportunities for expanding the use of this enzyme family as biomarkers and potential novel drug targets.
The NUDIX enzymes are involved in several cellular processes, yet their biological role has remained largely unclear. A highly collaborative study led by Professor Thomas Helleday (Karolinska Institutet/SciLifeLab) has now generated comprehensive data on the individual structural, biochemical and biological properties of 18 human NUDIX proteins, as well as how they relate to and interact with each other.
The data reveal that human NUDIX enzymes can be divided into four major classes, based on their molecular structure. To a certain extent, which substrates the different NUDIX enzymes prefer, were found to correlate with their structural classification. Also, the expression of NUDIX in normal and cancer tissues, and how knock-down of these enzymes affected proliferation and cell cycle progression in both cases, were investigated.
Through collaborations with i.a. the SciLifeLab Biochemical and Cellular Screening unit, members of the Human Protein Atlas and teams supervised by Carolina Wählby (Uppsala University/SciLifeLab), Erik Sonnhammer (Stockholm University/SciLifeLab), and Pål Stenmark (Stockholm University), a comprehensive overview of the human NUDIX hydrolases has been produced. This plethora of data can be used to evaluate NUDIX family members as biomarkers or future drug targets.
Read the full paper in Nature Communications