Federico Forneris - Associate Professor
Phone: +39 0382 985228 (Office) - 0382 985549 (Office) - 0382 985554 (Lab) - 0382 985584 (Lab)
- Born Aug 07th, 1978 in Piedmont, Italy - Guarene, my beautiful hometown
- Languages known: Italian, English, French
- 2023-now: Full Professor (Tenured), University of Pavia, Italy
- 2017-2023: Associate Professor (Tenured), University of Pavia, Italy
- 2014-2017: Assistant Professor (Tenure-Track), University of Pavia, Italy
- 2009-2013: Postdoctoral research assistant, University of Utrecht, The Netherlands
- 2007-2009: Postdoctoral research assistant, University of Pavia, Italy
- 2009-2013: Post-doc research in Protein Structural Biology, Crystal and Structural Chemistry, Bijvoet Centre for Biomolecular Research, Utrecht University, The Netherlands
- 2003-2008: PhD research in Basic and Applied Biomolecular Sciences, Institute for Superior Studies (IUSS) and University of Pavia, Italy
Title of Thesis: Investigating the Structural and Biochemical Properties of human Lysine-Specific Demethylase LSD1.
- 1997-2002: Master degree in physical chemistry, cum laude with special mention and recommendation for publication, University of Turin, Italy
Title of Thesis: Crystallographic studies of Artificial Metalloproteins with four-helical bundle motifs.
- 1992-1997: High school diploma in Accountancy, Istituto Tecnico Commerciale E. Tesauro, Fossano, Italy
The common theme of the active research projects of my lab is the elucidation of the intricate mechanisms of extracellular protein-protein interaction and signaling. The various
processes that fall under the description of "molecular recognition" (ranging from transient inter-molecular interactions, conformational changes,
proteolysis-mediated activation and inhibition, to many others) represent for me one of the most fascinating aspects of nature elegance and complexity.
In my research lab, we merge structural biology with biochemistry and biophysics to characterize large macromolecular complexes and elucidate their structure-function
relationship to put the molecular insights in the proper biological context. For more information about current research and targets, please visit the Research section of the lab website.
I am co-author of several publications in international peer-reviewed scientific journals of high profile (14 papers as first author) including Science, PNAS, Nature Communications, Science Advances, Cell Reports J. Neurosci, EMBO J and JACS and 3 book chapters (Complete publications list in Pubmed).
During my PhD in the lab of Prof. Andrea Mattevi, I have applied enzymology, biophysics and structural biology to study several flavin-containing enzymes and explore their catalytic properties. The main result of these efforts was the detailed characterization of the structural and biochemical features of the first ever discovered human histone demethylase LSD1 ad its complexes. Being able to express and purifiy recombinant LSD1 and its complex with the co-repressor CoREST, I have explored LSD1 substrate recognition mechanism, and enphasized the role of LSD1 as a potential drug target and provided the bases for a large number of investigations involving this enzyme complex and its multiple functions (Review Link).
During my postdoc in Utrecht, I worked as NIH/ERC funded postdoctoral fellow on a collaborative project coordinated by Prof. Piet Gros and Prof. John Lambris on the structural characterization of macromolecular complexes of the complement system (for a general overview about the structural biology of the complement system, see this page). I combined low-resolution x-ray crystallography of large macromolecular complexes, biochemistry and biophysics to characterize multiple intermediate steps of the complement cascade. (Key Publications 1, 2, 3 - Movie).
I also contributed to the characterization of the complex between the stem cell signaling molecule R-spondin 1, its receptor LGR5 and its antagonist ZNRF3. LGRs are receptors for R-spondins, potent Wnt agonists that exert profound trophic effects on Wnt-driven stem cells compartments. Using a combination of structural and cellular biology analyses, our data revealed binding of R-spondins to conserved sites on LGRs and suggested a direct signalling role for LGRs in addition to forming Wnt receptors/co-receptors complexes. (Key Publications 1, 2).
- Scietti, L., Chiapparino, A., De Giorgi, F., Fumagalli, M., Khoriauli, L., Nergadze, S., Basu, S., Olieric, V., Cucca, L., Banushi, B., Profumo, A., Giulotto, E., Gissen, P., Forneris, F. (2018) Molecular architecture of the multifunctional collagen lysyl hydroxylase and glycosyltransferase LH3, Nature Communications, 9, 3163. PubMed Link
- Banushi, B., Forneris, F.*, Straatman-Iwanowska, A., Strange, A., Lyne, A., Rogerson, C., Burden, J.J., Heywood, W.E., Hanley, J., Doykov, I., Straatman, K.R., Smith, H., Bem, D., Kriston-Vizi, J., Ariceta, G., Risteli, M., Wang, C., Ardill, R.E., Zaniew, M., Latka-Grot, J., Waddington, S.N., Howe, S.J., Ferraro, F., Gjinovci, A., Lawrence, S., Marsh, M., Girolami, M., Bozec, L., Mills, K., Gissen, P.* (2016) Regulation of post-Golgi LH3 trafficking is essential for collagen homeostasis, Nature Communications, 7, 12111. PubMed Link *Corresponding Authors
- Forneris, F., Wu, J., Xue X., Ricklin, D., Lin, Z., Sfyroera, G., Tzekou, A., Volokhina, E., Granneman, J.C.M., Hauhart, R., Bertram, P., Liszewski, M.K., Atkinson, J.P., Lambris, J.D., Gros, P. (2016) Regulators of complement activity mediate inhibitory mechanisms through a common C3b-binding mode, The EMBO Journal, 35, 1133-1149. PubMed Link
- Forneris, F., Ricklin, D., Wu, J., Tzekou, A., Wallace, R.S., Lambris, J.D., Gros, P. (2010) Structures of C3b in complex with factors B and D give insight into complement convertase formation. Science, 330, 1816-1820. PubMed Link
- Forneris, F., Mattevi, A. (2008) Enzymes without borders: Mobilizing substrates, Delivering products. Science 321, 213-216. PubMed Link
- Forneris, F., Binda, C., Adamo, A., Battaglioli, E., Mattevi, A. (2007) Structural basis of LSD1-CoREST selectivity in histone H3 recognition. J. Biol. Chem. 282, 20070-20074. PubMed Link