Group I.C. Forster



2010 - 2015
We continued investigation of the structure-function relations of sodium-coupled phosphate transporters (NaPi-II, SLC34 family) previously started by the Murer group. We focused on the voltage clamp fluorometry technique, combined with high resolution determination of charge relaxations recorded from oocytes over-expressing constructs containing point mutations. With these experimental tools, we gained important insights into substrate interactions and voltage dependence of transport function. In the absence of a crystal structure for bacterial homologs of SLC34 proteins, we also adopted a homology modelling strategy in collaboration with US colleagues, using the bacterial VcINDY dicarboxylate transporter as template. This work, complemented with experimental studies yielded a 3-D structural model for SLC34 proteins and allowed us to locate the substrate and cation binding sites and predict molecular rearrangements during the transport cycle.



Ian Forster

Monica Patti
Carlos Muñoz Hernando
Olga Andrini
Chiara Ghezzi