Jan Hofsteenge

Modulation of protein function by covalent modification is of increasing importance as a factor in disease and as a therapeutic target. The discovery of new protein modifications and their function remains a challenge. Using protein/peptide purification and mass spectrometry as well as molecular and cell biology techniques, we focus on two unique forms of glycosylation in secreted proteins, C-mannosylation of tryptophan and O-fucosylation of serine or threonine residues. About 50 examples of the former modification are known, in organisms ranging from C. elegans to man. We are studying enzymes involved in the process and analysing specific proteins lacking the modification. Of the two kinds of O-fucose-linked polysaccharides known, O-linked tetrasaccharide appears to function in intercellular signalling. We have found the first protein containing the product of the second pathway, i.e. Glc-Fuc-O-Ser/Thr and are seeking its function.
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