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| JAN HOFSTEENGE |
| Molecular and functional aspects of
co- and posttranslational protein
modifications |
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| 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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For further information, please contact
Administrative Assistant Rebekka Kaufmann
(+41 61 6977623) |
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To contact FMI members directly, click
here for the FMI Directory. |
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