Human WIPI proteins in the process of autophagy

Tassula Proikas-Cezanne

TassulaProikasCezanne23-11-2012-04 cropped
  • PhD (Dr. rer. nat.) 1995 from the University of Hamburg (external thesis at the MPI for Plant Breeding, Cologne)
  • Postdoctoral scientist at the Marie Curie Research Institute, Oxted, and Temple University, Philadelphia
  • Scientific consultant at Onconova Therapeutics, Princeton
  • Since 2004 group leader at the Interfaculty Institute for Cell Biology, University of Tübingen

Research Interest

We aim to contribute to the molecular understanding of autophagy in health and disease. Autophagy is an evolutionarily conserved lysosomal degradation pathway that secures cellular homeostasis and that also contributes to a variety of age-related human diseases. The main focus of my group is the molecular characterization of the human WIPI gene and protein family that we identified previously. We have found that WIPI proteins are essential phospholipid effectors during the process of autophagy in human cells, and that WIPI genes are aberrantly expressed in human cancer.

Our current aims are to identify signaling networks that regulate WIPI proteins, and to identify synthetic and natural compounds that can modulate autophagy in pathophysiological circumstances such as cancer.

  • IMPRS Tassula Figure
    click to enlarge

WIPI-1 is a membrane protein of both the outer (OM) and inner membrane (IM) of autophagosomes (AP). See reference (2) below.

Available PhD Projects

The role of human WIPI proteins in cancer

Selected Reading

1) Codogno P, Mehrpour M, Proikas-Cezanne T (2011). Canonical and non-canonical autophagy: variations on a common theme of self-eating? Nat Rev Mol Cell Biol. 13(1):7-12.

2) Proikas-Cezanne T, Robenek H (2011). Freeze-fracture replica immunolabelling reveals human WIPI-1 and WIPI-2 as membrane proteins of autophagosomes. J Cell Mol Med. 15(9):2007-2010.

3) Proikas-Cezanne T et al. (2004). WIPI-1alpha (WIPI49), a member of the novel 7-bladed WIPI protein family, is aberrantly expressed in human cancer and is linked to starvation-induced autophagy. Oncogene 23(58):9314-9325.