Marco Lolicato, PI, Associate Professor
Cristina Arrigoni, PI
Alessandro Bontà (PhD student)
Stefano Conti Nibali (post-doc)
The laboratory mainly works on the biophysics of ion channels and transporters involved both in neoplastic pathologies and in the neurodevelopment process.
The goal of the laboratory is the identification (1) of the role of the Hv1 channel in breast cancer metastases; (2) of the molecular mechanisms of the interactome of the KCC2 channel; (3) of the molecular structure of the divalent VDAC1-Hexokinase complex.
In the laboratory we are able to purify sufficient quantities of protein targets for structural and functional studies and we are actively collaborating with international companies for the development of new anticancer molecules. We are, also, exploring new directions in protein de novo design to create proteins with novel functions starting from Nature's building blocks: peptides and protein domains.
Methodology: Electrophysiology, cell biology, X-ray crystallography, cryo-electron microscopy, protein expression and purification, cell biology and computational methods (docking, molecular dynamics, protein engineering).
Arrigoni C., Lolicato M., Shaya D., Rohaim A., Findeisen F., Colleran C.M., Dominik P., Kim S.S., Schuermann J., Kossiakoff A.A., and Minor D.L. Quaternary structure independent folding of voltage-gated ion channel pore domain subunits. Nat Struct Mol Biol., page 2021.08.15.456357 (2022).
Lolicato M., Natale A.M., Abderemane-Ali F., Crottès D., Capponi S., Duman R., Wagner A., Rosenberg J.M., Grabe M., and Minor D.L. K2P channel C-type gating involves asymmetric selectivity filter order-disorder transitions. Science advances, 6(44) (October 2020).
Lolicato M., Arrigoni C., Mori T., Sekioka Y., Bryant C., Clark K.A., and Minor D.L. K2P2.1 (TREK-1)-activator complexes reveal a cryptic selectivity filter binding site . Nature, 547(7663):364–368 (July 2017).
Arrigoni C., Rohaim A., Shaya D., Findeisen F., Stein R.A., Nurva S.R., Mishra S., Mchaourab H.S., and Minor D.L. Unfolding of a Temperature-Sensitive Domain Controls Voltage-Gated Channel Activation. Cell, 164(5):922–936 (February 2016). http://www.cell.com/cell/fulltext/S0092-8674(16)30067-8.