Research in the Hanson laboratory focuses on fundamental unknowns of intracellular membrane organization and trafficking, with a special interest in roles played by ATPases of the AAA+ family of protein remodeling enzymes. We use a range of cell biological and biochemical tools to study pathways and processes controlled by these membrane-regulatory AAA+ ATPases and to learn how changes in these pathways contribute to pathogenesis. Current projects focus on two major problems. The first is to understand how the ESCRT machinery and its AAA+ ATPase VPS4 create vesicles inside late endosomes (a.k.a. multivesicular bodies). The second is to define the role of lumenal AAA+ proteins related to torsinA in controlling endoplasmic reticulum (ER) and nuclear envelope (NE) structure and function. Both projects are advancing understanding of key cellular pathways while providing insight into diseases ranging from cancer to dystonia.
Abby and Teri's paper explaining why torsinA resides in the ER is now available on-line at EMBO Journal !
In addition to defining a novel mechanism for ER retention, this paper demonstrates that torsinA and another ell-known monotopic lumenal membrane protein COX1 preferentially reside in sheets instead of tubules in the ER.5
We have opportunities for rotating graduate students on both projects.
We also have occasional opportunities for post-doctoral researchers.
Please contact Dr. Hanson for further information : phanson22@WUSTL.EDU