2013 Karl Meyer Award Goes to Markus AebiThe Society for Glycobiology is pleased to announce that the recipient of the 2013 Karl Meyer Award is Markus Aebi. The Karl Meyer Award was established in 1990 to honor the distinguished career of Karl Meyer and his outstanding contributions to the field of Glycobiology. This international award is presented to well-established scientists with currently active research programs who have made widely recognized major contributions to the field of Glycobiology. Dr. Markus Aebi (Professor, Swiss Federal Institute of Technology, Zurich, Switzerland) has been a pioneer in the application of yeast genetic tools to identify the enzymes involved in endoplasmic reticulum N-glycosylation. His interest for glycobiology started with the serendipitous identification of the essential subunit WBP1 of yeast oligosaccharyltransferase. This discovery was rapidly followed by the description of several components of the eukaryotic oligosaccharyltransferase complex, thereby unraveling the intricate regulatory mechanisms underlying the transfer of oligosaccharides to nascent glycoproteins. The work of Dr. Aebi also led to the description of a novel class of mannosyltransferases and glucosyltransferases that utilize dolichol-phosphate-mannose and dolichol-phosphate-glucose for the assembly of the lipid-linked oligosaccharide substrate of oligosaccharyltransferase. The genetic and biochemical characterization of these endoplasmic reticulum glycosyltransferases established the structural requirements for recognition of lipid-linked oligosaccharides by oligosaccharyltransferase. Similar applications of yeast genetics yielded essential insights on the importance of dolichol recycling for N-glycosylation and on the function of N-linked carbohydrates in the processing of glycoproteins. Dr. Aebi showed that defined N-glycan structures serve as signals in the quality control process that leads to the degradation of misfolded proteins in the endoplasmic reticulum, an important step forward in the deciphering of the "glyco-code" of eukaryotic cells. The use of the model system Saccharomyces cerevisiae was not only instrumental for the detailed description of the conserved pathway of N-linked protein glycosylation in eukaryotes but also provided the necessary tools to identify and describe multiple types of human congenital disorders that affect this process. |