Structural and biophysical investigations of Rab GTPase interacting proteins

Abstract

Summary: Rab GTPases are important regulators of cell trafficking steps such as vesicle fusion, budding and motility. They are often described as 'on/off' switches, interacting with specific effectors when bound to GTP. Although their secondary and tertiary structures are largely conserved they bind sometimes very diverse effectors sharing little or no homology. A similar but less prodigious situation is evident with guanosine nucleotide exchange factors, proteins that interact with Rab GTPases in order to facilitate the nucleotide exchange during the Rab GTPase cycling.