K. Kevin Pfister, PhD, University of Virginia

K. Kevin Pfister, PhD
K. Kevin Pfister, PhD

The Pfister lab investigates the mechanisms that underlie intracellular transport, in particular the microtubule-based movements driven by the motor protein cytoplasmic dynein. Defects in dynein function have a role in the development of cancer. They can result in a failure to properly assemble the mitotic spindle, to properly regulate the spindle checkpoint, or to separate chromosomes which lead to chromosome loss and polyploidy, and the development of tumorogenesis. Dynein is responsible for the proper localization of the tumor suppressor protein p53. In addition to its roles in mitosis, dynein is responsible for the positioning of the nucleus during cell migration; the movement of membranous organelles; and the transport or localization of many signal transduction proteins, mRNAs, and viruses. Dynein is the motor which moves growth factors and their receptors (Trks) from the synapse to the nucleus, an important step in neuronal and synaptic differentiation and maintenance.

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  1. Ha J, Lo KW, Myers KR, Carr TM, Humsi MK, Rasoul BA, Segal RA, Pfister KK. A neuron-specific cytoplasmic dynein isoform preferentially transports TrkB signaling endosomes. J Cell Biol. 2008 Jun 16;181(6):1027-39.
  2. Lo KW, Kogoy JM, Rasoul BA, King SM, Pfister KK. Interaction of the DYNLT (TCTEX1/RP3) light chains and the intermediate chains reveals novel intersubunit regulation during assembly of the dynein complex. J Biol Chem. 2007 Dec 21;282(51):36871-8.
  3. Lo KW, Kogoy JM, Pfister KK. The DYNLT3 light chain directly links cytoplasmic dynein to a spindle checkpoint protein, Bub3. J Biol Chem. 2007 Apr 13;282(15):11205-12.
  4. Myers KR1, Lo KW, Lye RJ, Kogoy JM, Soura V, Hafezparast M, Pfister KK. Intermediate chain subunit as a probe for cytoplasmic dynein function: biochemical analyses and live cell imaging in PC12 cells. J Neurosci Res. 2007 Sep;85(12):2640-7.