c/o Complesso Biologico Interdipartimentale
Viale Giuseppe Colombo 3
My research training has been focused on the function, structure and regulation of mitochondrial (F1FO) and plasma membrane ATPases. After structural and functional studies of the enzymes, the use of native protein extraction and separation (BN-page) allowed the identification of (i) Cyclophilin D as a F1FO ATP synthase interactor at the mitochondrial level; this interaction has been proved to be crucial for the modulation of the F1FO ATP synthase catalysis in native conditions; (ii) the presence of the native multi-subunit complex (F1FO ATP synthase) at level of the plasma membrane, an observation which can be potentially useful in the investigation of mechanisms involved in neurodegenerative diseases. Moreover, the collaboration with Paolo Bernardi gave the opportunity for the identification of ATP synthase dimers in the Permeability Transition Pore (PTP) formation.
Other activities have been aimed to study, through fluorescent microscopy and in situ oxygen consumption measurements, the pathogenic mechanisms involved in mitochondrial diseases and possibly to identify new therapeutic compounds able to improve the energetic performance in patients.
Granatiero V, Giorgio V, Calì T, Patron M, Brini M, Bernardi M, Tiranti V, Zeviani M, Pallafacchina G, De Stefani D and Rizzuto R (2015), Reduced mitochondrial Ca2+ transients stimulate autophagy in human fibroblasts carrying the 13514A>G mutation of the ND5 subunit of NADH dehydrogenase. Cell Death and Differentiation, doi:10.1038/cdd.2015.84
Carraro M, Giorgio V, Sileikyte J, Sartori G, Forte M, Lippe G, Zoratti M, Szabò I, Bernardi P (2014) Channel formation by yeast F-ATP synthase and the role of dimerization in the mitochondrial permeability transition. J Biol Chem, 289(23):15980-5.
Giorgio V, von Stockum S, Antoniel M, Astrid Fabbro A, Fogolari F, Forte M, Glick G.D, Petronilli V, Zoratti M, Szabó I, Lippe G, Bernardi P(2013) , Dimers of mitochondrial ATP synthase form the permeability transition pore. PNAS, 110(15):5887–5892.
Giorgio V, Petronilli V, Ghelli A, Carelli V, Rugolo M, Lenaz G, Bernardi P(2012), The Effects of Idebenone on Mitochondrial Bioenergetics. Biochim Biophys Acta, 1817(2):363-9
Giorgio V, Bisetto E, Soriano ME, Debbeni-Sala F, Basso E, Petronilli V, Forte MA, Bernardi P, Lippe G (2009), Cyclophilin D Modulates Mitochondrial F0F1-ATP Synthase by Interacting with the Lateral Stalk of the Complex, J Biol Chem 284, 33982-33988.