The FEBS-IUBMB-ENABLE Conference is a special event entirely organized by and for young researchers under the auspices of the Federation of European Biochemical Societies (FEBS) and the International Union of Biochemistry and Molecular Biology (IUBMB). It is based on a successful ENABLE initiative of four renowned European Research Institutes: IRB Barcelona in Spain, NNF CPR in Denmark, RIMLS in the Netherlands and SEMM in Italy initially funded by the EU Horizon 2020 programme. The FEBS-IUBMB-ENABLE 2022 Conference was hosted by the Institute of Biomedicine of Seville (IBiS) in Spain. The conference took place at the campus of Virgen Del Rocío University Hospital in Sevilla, Spain on… Read more

FEBS Junior Sections November talk already on Thursday

Published by: Martin Toul | 06. 11. 2022 10:17

On 10th November 2022 at 7PM (CET), another FEBS Junior Sections talk will take place as the eleventh online talk of this year's session. This one is coordinated by the SIB Sezione Giovani, the Junior Section of the Italian Society of Biochemistry and Molecular Biology (SIB). It will be an academic talk entitled “The molecular diversity of collagen lysine post-translational modification enzymes” and it will be delivered by Prof. Federico Forneris from the Armenise-Harvard Laboratory of Structural Biology, University of Pavia, Italy.

If you are interested in the topic and would like to join us for the online session, feel free to register via Zoom by clicking on the registration button above.

Talk abstract

Collagen lysine residues are subject to a variety of post-translational modifications (PTM) that impact on the overall organization of mature collagens and confer to these complex macromolecules their unique physico-chemical properties. In humans, the PTM machinery acting on collagen lysines groups multifunctional lysyl hydroxylases-glucosyltransferases (LH), galactosyltransferases (GLT25D), lysyl oxidases (LOX) and glucosidases (PGGHG). Besides their fundamental roles in collagen homeostasis, malfunctions in these molecular machineries due to misfolding, mislocalization or abnormal enzymatic activity have been associated to a wide variety of connective tissue diseases as well as increased metastatic progression of numerous solid tumors. By focusing on lysine hydroxylation and subsequent glycosylation events, in our group we have characterized the different human collagen lysyl hydroxylases-glucosyltransferases isoforms and also the galactosyltransferase GLT25D1 using a combination of biochemistry, structural biology and biophysical approaches. Collectively, our published and unpublished results reveal unexpected quaternary organizations that underpin the molecular complexity of these essential, yet poorly characterized molecular systems, providing insights on their cooperative mechanisms of lysine PTM and templates for structure-based drug discovery campaigns.

For more information, visit the official talk anouncement post at FEBS website. We are looking forward to meeting you online!