Structural Biology:
Dr. Monika Oberer
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Link to the Austrian gene research program

Dr. Monika Oberer
Institut für Molekulare Biowissenschaften
Strukturbiologie

Karl Franzens Universität
Humboldtstrasse 50/3
A-8010 Graz
phone: +43 316 380 5483, FAX: +43 316 380 9897
e-mail: m.oberer@uni-graz.at
web: http://strubi.uni-graz.at/

 
 
Research Interests

The long-term objective of our research is to establish the structural basis of lipid metabolism, in particular, proteins involved in the pathway by which adipose tissue takes up and releases fatty acids. Most dietary lipids are ingested in the form of triacylglycerols (TG) but must be degraded to fatty acids for absorption. Free fatty acids (FA) are not only insoluble in the cytosol but also toxic to the cells. Therefore, the metabolism of dietary lipids is characterized by tightly defined stages of TG hydrolysis and re-estrification processes. TG are packaged into lipoprotein transport particles called chylomicrons and transported in the blood and lymph system. Lipoprotein lipase (LPL) hydrolyzes TG in chylomicrons and the released FA are taken up into adipocytes where they are re-estrified to TG for storage. In order to mobilize the stored energy, each TG is degraded step-by-step to three molecules of FA and glycerol. In the first step, TG are hydrolyzed into diacylgycerols (DG) and FA. This reaction is catalyzed mainly by the enzyme 'Adipose triglyceride lipase' (ATGL) and to a some extent by the enzyme 'Hormone sensitive lipase' (HSL). HSL is also responsible for the hydrolysis of DG to monoacylglycerol (MG) and FA. Monoacylgycerol lipase (MGL) then hydrolyzes MG to glycerol and FA. The produced molecules of FA are then released from the adipose tissue and transported to energy requiring tissues. There, the FA are activated and oxidized in response to the energy demand of the cell.

With an overall goal of understanding specific steps of fatty acid metabolism at atomic detail, we use molecular biology, biochemical and biophysical approaches, with special emphasis on X-ray crystallography and NMR spectroscopy.
 
 
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