The proteins in human cells are extensively entangled with different types of sugar molecules by the process called glycosylation (post-translational modification of proteins). These alterations increase the diversity of protein structure and function which affects proteins folding, their behavior and where they go inside the cells. This study is going to be published in the Journal of Biological Chemistry and the work was supported by National Institutes of Health. In this study, an unusual type of glycosylation deeply affects the protein function which is important for human development and cancer progression.
Protein glycosylation is of 2 types N-linked or O-linked depends on whether the sugar is linked to nitrogen or oxygen-containing sites of the protein respectively. Robert Haltiwanger’s research team at the University of Georgia studied a very rare type of O-linked modification which affects a Notch protein (transmembrane protein), signaling receptor, required for cell development and differentiation. This notch protein is dysregulated in many cancers such as breast cancer, prostate cancer, and leukemia. The enzymes POFUT1 and POGLUT1, attach the glucose and fructose units to the notch protein and is responsible for its modification.
Finally, this indicates, sugar is essential for notch activity (hyperactive/underactive) and manipulating these sugars, helps to correct the dysregulation of the notch protein. The enzymes, POFUT1 and POGLUT1 become the potential targets for cancer treatment.