Adrian Olivares lab
TorsinA belongs to the superfamily of AAA+ (ATPases Associated with various cellular Activities) macromolecular remodeling enzymes that use the energy from ATP binding and hydrolysis to perform mechanical work, such as protein unfolding. Previous studies have suggested that torsin remodels nuclear envelope proteins such as the components of the LINC (Linker of Nucleoskeleton and Cytoskeleton) complex. My long-term goal is to understand how torsin acts on the LINC complex to affect nuclear membrane position, alter chromosome dynamics, and control gene expression, and to develop chemical probes for the study of torsin function. Torsins are atypical members of the AAA+ enzyme family because they do not contain a well-conserved arginine finger motif, contain a non-canonical Walker A motif, and are able to localize to the endoplasmic reticulum in addition to the nuclear membrane, but the physiological function of torsin is unclear and a detailed mechanistic characterization of the enzyme is lacking. My research project focuses on elucidating the mechanism of torsin function using traditional biochemical approaches, single-molecule force spectroscopy, and by developing novel small molecule effectors.