Research field
Interest of our group is to investigate:
- The physiological role of 14-3-3 proteins in plants. 14-3-3s are a class of regulatory proteins involved in the regulation of diverse physiological processes through phosphorylation-dependent interaction with client proteins. The interest of our group is focused on the biochemical characterization of the interaction between 14-3-3 proteins and the plasma membrane H+-ATPase, the proton pump which controls several physiological processes in the plant cell. Furthermore, we are interested in the identification and characterization of novel targets of 14-3-3 proteins by biochemical and molecular biology approaches. The physiological function of 14-3-3 proteins is also studied by using transgenic Arabidopsis plant overexpressing genes encoding for different 14-3-3 isoforms.
- The mechanism of action of Fusicoccin. The fungal toxin Fusicoccin (FC) is known to affect several processes in plants through its ability to irreversibly stabilize the interaction between the H+-ATPase and 14-3-3 proteins. We contributed to clarify the biochemical mechanism of FC action in plants and we also discovered the FC ability to modulate also some interactions between 14-3-3 proteins and their targets in animal systems. In fact, we discovered the ability of the toxin to induce platelet aggregation through stabilization of the interaction between 14-3-3s and GPIbα, a glycoprotein involved in platelet adhesion and aggregation. We are interested in the identification of novel FC targets in mammals and in the potential exploitation of the pharmacological activity of FC.
- The role of Salt-Tolerant Related Proteins in Abiotic and Biotic Stresses. Salt-Tolerant Related Protein (STRP) is an Arabidopsis protein whose function is still fully uncharacterized. We produced strp knock-out and STRP over-expressing Arabidopsis plants, and we discovered that the protein is implicated in the response to different abiotic and biotic stresses. We are also investigating the activity of the protein at the biochemical level and its participation to hormone signal transduction pathways.
Publications
- Rodolfo, C., Rocco, M., Cattaneo, L., Tartaglia, M., Sassi, M., Aducci, P.,Scaloni, A., Camoni, L., Marra, M. (2016). Ophiobolin A induces autophagy and activates the mitochondrial pathway of apoptosis in human melanoma cells. PLoS ONE, 11(12) doi:10.1371/journal.pone.0167672
- Muzi, C., Camoni, L., Visconti, S., & Aducci, P. (2016). Cold stress affects H+-ATPase and phospholipase D activity in Arabidopsis. Plant Physiology and Biochemistry, 108, 328-336. doi:10.1016/j.plaphy.2016.07.027
- Pallucca R, Visconti S, Camoni L, Cesareni G, Melino S, Panni S, Torreri P, and Aducci P. (2014) Specificity of ε and non-ε isoforms of Arabidopsis 14-3-3 proteins towards the H+-ATPase and other targets. PLoS One. 9(3):e90764. doi: 10.1371/journal.pone.0090764.
- Camoni, L., Visconti, S., and Aducci, P. (2013) The phytotoxin fusicoccin, a selective stabilizer of 14-3-3 interactions? IUBMB Life 65: 513-517.
- Camoni, L., Di Lucente, C., Pallucca, R., Visconti, S., and Aducci, P. (2012) Binding of phosphatidic acid to 14-3-3 proteins hampers their ability to activate the plant plasma membrane H+-ATPase. IUBMB Life 64: 710-716.
- Paiardini, A., Aducci, P., Cervoni, L., Cutruzzolà, F., Di Lucente, C., Janson, G., Pascarella, S., Rinaldo, S., Visconti, S., and Camoni, L. (2014) The phytotoxin fusicoccin differently regulates 14-3-3 proteins association to mode III targets. IUBMB Life. doi: 10.1002/iub.1239.
- Visconti, S., Camoni, L., Marra, M.,and Aducci P. (2008) Role of the 14-3-3 C-terminal region in the interaction with the plasma membrane H+-ATPase. Plant Cell Physiology 49: 1887-1897.
