THE MALAKER LAB

Over the last few decades, mass spectrometry (MS) has revolutionized the study of proteins, and workflows for unmodified proteins have become routine. Generally, proteins are digested with trypsin, subjected to positive mode electrospray ionization, fragmented by well-documented methods, and the resultant spectra can be searched using a wide variety of reliable search algorithms.

 

However, the O-glycoproteome is wholly uncharted territory, as densely O-glycosylated domains (aka mucin domains) do not fit into the workflows developed for traditional proteomics. My laboratory develops original methods to tackle these problems, thus shedding light on the mucinome. We apply these technologies broadly to understand how glycosylation regulates protein structure, function, and disease biology across diverse biological systems. In addition to advancing analytical and computational methods for glycoproteomics, our work spans biomarker discovery, immune interactions, cell-surface signaling, and the molecular mechanisms underlying various diseases associated with aberrant glycosylation. By combining method development with biological application, we are expanding the toolkit available for studying complex glycoproteomes and uncover new roles for glycosylation in human health and disease.