Penn Medicine
   
 

Erika L. F. Holzbaur, Ph.D.

Department of Physiology, University of Pennsylvania

Contact Information

Department of Physiology
D400 Richards Building
Philadelphia, PA 19104-6085
Phone: (215) 573-3257
Fax: (215) 573-5851
E-mail: holzbaur@mail.med.upenn.edu
Position: Assistant Professor

Expertise

Our laboratory is interested in the mechanisms of microtubule-based motility- the directed motility of vesicles, organelles, and chromosomes along the microtubule cytoskeleton. Our research focuses on understanding the cellular role and function of cytoplasmic dynein, and its required activator dynactin. Dynactin is a unique oligomeric complex which binds to microtubules, to cytoplasmic dynein, and to spectrin via a filament formed from an actin-related protein. In Drosophila, both dynein and dynactin are essential: we are currently examining the roles of these proteins in vesicle trafficking in cells, including the rapid microtubule-based transport required in the extended axons of neuronal cells.

Representative Publications

  1. Holleran, E.A., Tokito, M.K., Karki, S., and Holzbaur, E.L.F. 1996. Centractin (Arp1) associates with spectrin revealing a potential mechanism to link dynactin to intracellular organelles. J. Cell Biol. 135:1815-1829.
  2. Tokito, M.K., Howland, D.S., Lee, V., M.-Y., and Holzbaur, E.L.F. 1996. Functionally distinct isoforms of dynactin are expressed in human neurons. Mol. Biol. Cell 7:1167-1180.
  3. Karki, S., and Holzbaur, E.L.F. 1995. Affinity chromatography demonstrates a direct binding between cytoplasmic dynein and the dynactin complex. J. Biol.Chem. 270:28806-28811.
  4. Waterman-Storer, C.M., Karki, S., and Holzbaur, E.L.F. 1995. The p150Glued component of the dynactin complex binds to both microtubules and the actin-related protein centractin (Arp-1). Proc. Natl. Acad. Sci. USA 92:1634-1638.
  5. Holzbaur, E.L.F., Hammarback, J.A., Paschal, B.P., Dravit, N.G., Pfister, K.K., and Vallee, R.B. 1991. Homology of a 150K cytoplasmic dynein-associated polypeptide with the Drosophila gene Glued. Nature. 351:579-583.
  6. Sweeney, H.L., and Holzbaur, E.L.F. 1996. Mutational analysis of molecular motors. Ann. Rev. Phys. 58:751-792.
  7. Holzbaur, E.L.F., and Vallee, R.B. 1994. Dyneins: Molecular structure and cellular function. Ann. Rev. Cell Biology. 10:339-372.
 
Pennsylvania Muscle Institute
Perelman School of Medicine University of Pennsylvania
Director: E. Michael Ostap, Ph.D.

700A Clinical Research Building Philadelphia, PA 19104-6085 Phone: (215) 573-9758 Fax: (215) 898-2653