Update! Watch a recording of this talk.
This talk is an activity from the FEBS Junior Section, an initiative set up by students and young researchers from some of the FEBS Constituent Societies. Each month a Junior Section from one of the participant Societies organizes an online event on either a research or a career topic. This November event is the eleventh of their 2022 series and is an academic talk organised by SIB Sezione Giovani, the Junior Section of the SIB.
Speaker: Federico Forneris, Armenise-Harvard Laboratory of Structural Biology, University of Pavia, Italy
Topic: “The molecular diversity of collagen lysine post-translational modification enzymes”
Time: 10 November, 19:00 (CET)
For more information, see the presentation abstract below and visit the Armenise-Harvard Laboratory website.
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 Collectively, our published and unpublished results reveal unexpected quaternary organizations that underpin the molecular complexity of these essential, yet poorly characterized molecular systems,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.
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