Structure/function study of the CFTR (ABCC7) chloride channel

ABC transporters are a family of proteins which play numerous important roles in organisms' physiology, from bacteria to humans. They transport a wide variety of molecules such as sugars, vitamins and even small proteins from different compartments of the cell or outside of cells. The 48 human ABC proteins are mostly involved in secretions, drug detoxification, and identification of pathogens by the immune system. Structural studies of bacterial ABC proteins have been instrumental in discovering their 3D structure and providing numerous information on how they work. Unfortunately, for complex ABC proteins, such as the ones fund in humans, current advanced technologies are not developed enoughto permit extraction from cells in a way which would enable researchers to visualise their precise 3D structure. Most of the characteristics and functional properties of human ABC proteins are deduced from models based on predicted similarities with bacterial ABCs. Current models of human ABC proteins thus need to be validated by further testing for their functional and physiological relevance. This is the type of research that we do in our lab. In particular, we study the CFTR protein, an important human ABC transporter which plays a crucial role in the regulation of salts and water movement across epithelial cells of the lungs, pancreas, intestine and reproductive tract.By analyzing multiple aspects of this protein our aim is to obtain critically missing information of the transport mechanism which enables the CFTR protein to function and maintain the integrity and good function of the respiratory and digestive systems. Our findings will be applicable to other related ABC proteins which are anticipated to function similarly.