Phyllis I. Hanson, M.D., Ph.D.

Professor
Cell Biology and Physiology

Molecular Cell Biology Program
Neurosciences Program
Biochemistry, Biophysics, and Structural Biology Program

  • 314-747-4233

  • 314-747-4360

  • 314-362-7463

  • 8228

  • 4625 Cancer Research Building

  • phanson22@wustl.edu

  • http://www.hansonlab.wustl.edu

  • cell membrane, endocytosis, intracellular trafficking, molecular chaperones, nuclear envelope, dystonia

  • Regulation of membrane trafficking

Research Abstract:

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). We are also interested in how ESCRTs and VPS4 modulate trafficking and downregulation of signalling receptors and the biogenesis of secreted exosomes. 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.

Selected Publications:

Vander Heyden AB, Naismith TV, Snapp EL, and Hanson PI (2011). Static retention of the lumenal monotopic membrane protein torsinA in the endoplasmic reticulum. EMBO J Epub Jul 22.

Merrill SA and Hanson PI (2010). Activation of human VPS4A by ESCRT-III proteins reveals ability of substrates to relieve enzyme autoinhibition. J. Biol. Chem. 285:35428-38.

Hurley JH and Hanson PI (2010). Membrane budding and scission by the ESCRT machinery: it’s all in the neck. Nat. Rev. Mol. Cell Biol. 11:556-566.

Naismith TV, Dalal S, and Hanson PI (2009). Interaction of TorsinA with its major binding partners is impaired by the dystonia associated DGAG deletion. J. Biol. Chem. 284: 27866-74.

Vander Heyden AB, Naismith TV, Snapp EL, Hodzic D, and Hanson PI (2009). LULL1 retargets TorsinA to the nuclear envelope revealing an activity that is impaired by the DYT1 dystonia mutation. Mol. Biol. Cell. 20: 2661-72.

Hanson PI, Roth R, Lin Y, and Heuser JE (2008). Plasma membrane deformation by circular arrays of ESCRT-III protein filaments. J. Cell Biol. 180: 389-402.

Last Updated: 8/25/2011 8:55:31 AM

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