Membrane transport proteins constitute an important part of our genome and are target to many therapeutic drugs, but the complexities inherent to their hydrophobicity have significantly delayed their biochemical and structural studies. ATP binding cassette (ABC) transporters is a large family of proteins that use energy from ATP hydrolysis to move a diverse variety of molecules against their concentration gradient across the membrane. ABC transporters are involved in multiple processes: protection against xenobiotics, problems related to drug/drug interactions, development of multidrug resistance, etc., and their malfunctioning can cause terrible diseases such as Cystic Fibrosis or Stargardt. Despite the importance of these proteins, the molecular details of substrate/drugs recognition and the conformational changes that take place during their transport cycle are still unknown. Our lab wants to contribute to better understand these proteins, and for that we do biochemical, spectroscopic and structural studies of diverse ABC transporters. Currently our research is mainly focused on:
- The human mitochondrial transporter ABCB10, which is essential for heme production and for protection of cells against oxidative stress. Our goals are to identify the substrate that is being transported and the molecular mechanism of transport.
- A multidrug ABC transporter that is a bacterial homolog to P-glycoprotein, a protein implicated in the development of multidrug resistance in cancer cells and in undesired drug-drug interactions. Our goal is understand, at the molecular level, how diverse drugs can modulate the activity of the transporter.