Dr. Fabio Lolicato

Portrait

Heidelberg University
Biochemistry Center (BZH)
Im Neuenheimer Feld 328
69120 Heidelberg

Phone Office: +49 6221 54-4181

Phone Lab: +49 6221 54-4746

E-Mail: fabio.lolicato@bzh.uni-heidelberg.de



Position and Status

Group Leader at the Heidelberg University Biochemistry Center (BZH)


Scholarships and awards

2019 – 2023    Post-doctoral research in the laboratory of Prof. Walter Nickel, BZH, Heidelberg, Germany

2016 –  2020    Ph.D. in Computational Biophysics, University of Helsinki, Finland

2013 –  2015    Visiting Researcher, Tampere University of Technology, Finland

2011 –  2013    M.Sc. in Material Chemistry, University of Catania, Italy

2006 –  2011    B.Sc. in Chemistry, University of Catania, Italy     



Since  2024    Group Leader at the Heidelberg University Biochemistry Center (BZH)

2023 - 2024    Principal Investigator at the Heidelberg University Biochemistry Center (BZH)

Coordinating functions and editorial work

2013 – present   Reviewer for scientific journals

2022                   Conference organizer, Levi V at Mediterranean Sea: Biological membrane

                           and related phenomena, Aci Trezza, Italy

2019                    Lecturer at ProLipids Midsummer Workshop on Future Trends in

                            Biomembrane Research, Helsinki, Finland

1. Lolicato, F., Steringer, J. P., Saleppico, R., Beyer, D., Fernandez-Sobaberas, J., Unger, S., Klein, S., Riegerová, P., Wegehingel, S., Müller, H. M., Freund, C., Hof, M., Šachl, R., Chlanda, P., Vattulainen, I. & Nickel, W. Disulfide bridge-dependent dimerization triggers FGF2 membrane translocation into the extracellular space (eLife Sciences Publications, Ltd, 2023). https://doi.org/10.7554/eLife.88579.2

2. Winter, S. L., Golani, G., Lolicato, F., Vallbracht, M., Thiyagarajah, K., Ahmed, S. S., Lüchtenborg, C., Fackler, O. T., Brügger, B., Hoenen, T., Nickel, W., Schwarz, U. S. & Chlanda, P. The Ebola virus VP40 matrix layer undergoes endosomal disassembly essential for membrane fusion. The EMBO Journal 42, e113578 (2023). https://doi.org/10.15252/embj.2023113578

3. Klein, S., Golani, G., Lolicato, F., Lahr, C., Beyer, D., Herrmann, A., Wachsmuth-Melm, M., Reddmann, N., Brecht, R., Hosseinzadeh, M., Kolovou, A., Makroczyova, J., Peterl, S., Schorb, M., Schwab, Y., Brügger, B., Nickel, W., Schwarz, U. S. & Chlanda, P. IFITM3 blocks influenza virus entry by sorting lipids and stabilizing hemifusion. Cell Host & Microbe 31, 616-633.e620 (2023). DOI: 10.1016/j.chom.2023.03.005

4. Lolicato, F., Saleppico, R., Griffo, A., Meyer, A., Scollo, F., Pokrandt, B., Müller, H.-M., Ewers, H., Hähl, H., Fleury, J.-B., Seemann, R., Hof, M., Brügger, B., Jacobs, K., Vattulainen, I. & Nickel, W. Cholesterol promotes clustering of PI(4,5)P2 driving unconventional secretion of FGF2. Journal of Cell Biology 221 (2022). https://doi.org/10.1083/jcb.202106123

5. Tempra, C., La Rosa, C. & Lolicato, F. The role of alpha-helix on the structure-targeting drug design of amyloidogenic proteins. Chemistry and Physics of Lipids 236, 105061 (2021). https://doi.org/10.1016/j.chemphyslip.2021.105061

6. Sciacca, M. F., Lolicato, F., Tempra, C., Scollo, F., Sahoo, B. R., Watson, M. D., García-Viñuales, S., Milardi, D., Raudino, A., Lee, J. C., Ramamoorthy, A. & La Rosa, C. Lipid-Chaperone Hypothesis: A Common Molecular Mechanism of Membrane Disruption by Intrinsically Disordered Proteins. ACS Chemical Neuroscience 11, 4336-4350 (2020). https://doi.org/10.1021/acschemneuro.0c00588

7. Romanucci, V., García-Viñuales, S., Tempra, C., Bernini, R., Zarrelli, A., Lolicato, F., Milardi, D. & Di Fabio, G. Modulating Aβ aggregation by tyrosol-based ligands: The crucial role of the catechol moiety. Biophysical Chemistry 265, 106434 (2020). https://doi.org/10.1016/j.bpc.2020.106434

8. Lucendo, E., Sancho, M., Lolicato, F., Javanainen, M., Kulig, W., Leiva, D., Duart, G., Andreu-Fernández, V., Mingarro, I. & Orzáez, M. Mcl-1 and Bok transmembrane domains: Unexpected players in the modulation of apoptosis. Proceedings of the National Academy of Sciences 117, 27980-27988 (2020). https://doi.org/10.1073/pnas.2008885117

9. Legrand, C., Saleppico, R., Sticht, J., Lolicato, F., Müller, H.-M., Wegehingel, S., Dimou, E., Steringer, J. P., Ewers, H., Vattulainen, I., Freund, C. & Nickel, W. The Na,K-ATPase acts upstream of phosphoinositide PI(4,5)P2 facilitating unconventional secretion of Fibroblast Growth Factor 2. Communications Biology 3, 141 (2020). https://doi.org/10.1038/s42003-020-0871-y