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Glycobiology

Prof. Dr. Sabine Strahl

Prof. Dr. Sabine Strahl
Prof. Dr. Sabine Strahl
Im Neuenheimer Feld 360
69120 Heidelberg
Fon +49 6221 54-6286
Fax +49 6221 54-5859
ed.grebledieh-inu.soc TEA lharts.enibas

Office hours Monday 1:15- 2:00 pm

 

The Strahl Lab - Glycobiology: Sweet Science

Glycosylation is one of the most abundant and complex protein modifications known. In many biological systems more than half of all proteins are glycosylated and glycan chains are highly crucial for a wide range of biological processes. Our laboratory is interested in various aspects of glycobiology in eukaryotic organisms with a main focus on O-mannosylation, an evolutionarily conserved, essential protein modification with immense impact on a variety of cellular processes in humans. Defective O-mannosylation results in severe muscular dystrophy and malfunctions of the brain and the eyes. Having identified the first protein O-mannosyltransferase PMT1 in the model organism yeast, our work has substantially contributed to the understanding of protein O-mannosylation in eukaryotes. The laboratory continues to work on the molecular organization of the O-mannosylation machinery in the endoplasmic reticulum (ER) and the role of O-mannosyl glycans for growth and development of fungi and mammals.

Protein O-Mannosylation, an essential modification that is conserved from yeast to human

Figure2r.jpgO-mannosyl glycans are short linear oligosaccharides linked via an alpha-glycosidically-bound mannose to Ser and Thr residues. Biosynthesis is initiated at the endoplasmic reticulum (ER) by the transfer of mannose from dolichyl phosphate-activated mannose to Ser or Thr residues of proteins that are entering the secretory pathway. Further chain elongation takes place in the Golgi apparatus using nucleotide-activated sugars as donors.

The initial mannosyltransfer reaction is catalyzed by an essential family of Dol-P-mannose: protein O-mannosyl-transferases (PMTs) that is evolutionarily conserved from yeast to humans. Focusing on PMTs we aim to understand how the ER O-mannosylation machinery works. Further, we analyze the occurrence and functions of O-mannosyl glycans in the eukaryotic model system  baker's yeast and in mammals.

 

 

Latest News

 

Latest Publications

Bartels M.F., Winterhalter P.R., Yu J., Liu Y., Lommel M., Möhrlen F., Hu H., Feizi T., Westerlind U., Ruppert T. and Strahl S. (2016) Protein O-Mannosylation in the Murine Brain: Occurrence of Mono-O-Mannosyl Glycans and Identification of New Substrates. PlosOne [Accepted]

 

Bausewein D, Engel J, Jank T, Schoedl, M and Strahl, S (2016). Functional similarities between the protein O-mannosyltransferases Pmt4 from baker's yeast and human POMT1. J Biol Chem. 291(34):18006-15. doi: 10.1074/jbc.M116.739128.

 

Carvalho, S, Oliveira, T, Bartels, MF, Miyoshi, E, Pierce, M, Taniguchi, N, Carneiro, F, Seruca, R, Reis, CA, Strahl, S and Pinho, SS (2016). O–mannosylation and N-glycosylation: two coordinated mechanisms regulating the tumour suppressor functions of E-cadherin in cancer. Oncotarget. doi: 10.18632/ oncotarget.11245. [Epub ahead of print]


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