Glycosylation is a dynamic post translational modification (PTM) in which glycans are attached to proteins or lipids by controlled biosynthetic pathways that (i) cannot be deduced from genetic and transcriptomic data alone and (ii) are highly dependent on the physiological status of a cell. This glycocode (or glycome) is absolutely essential in the regulation of intercellular communication, protein structure and stability or pathogen recognition, to name a few examples. The glycocode also changes in many diseases such as cancer and infection. A deeper understanding on how the glycocode is involved in health and disease pathogenesis harbours enormous potential for advancing diagnosis and treatment of diseases such as cancer.
The presentation will focus on how we employ proteomics and glycomics technologies to understand the role glycosylation plays for erythropoiesis. Specifically, we have been investigating the role that glycosylation of the cytokine Stem Cell Factor (SCF) plays in interaction with its receptor cKIT (CD117) and its downstream signalling. Using an established ex vivo model of erythropoiesis, we revealed that glycosylated SCF is better in promoting cell expansion, upregulating translation-relevant pathways while downregulating cell-stress associated protein groups. We also show for the first time that the budding erythrocyte glycome undergoes development-specific changes that remain yet to be better understood. Nonetheless, our findings substantiate that protein glycosylation plays a fundamental role in erythropoiesis, and that integrated, multi-omics oriented techniques are better suited to dissect and understand the complex network of biomolecules governing biochemical processes.