Jieya Shao.jpg

Jieya Shao, PhD

Assistant Professor
Department of Medicine
Oncology Division
Molecular Oncology

Research Interests

  • Breast cancer
  • Molecular mechanisms
  • Translational research


  • 314-362-8695 (office)
  • 314-747-9310 (lab)
  • 314-747-9320 (fax)
  • Room 3308, 4515 McKinley Research Building (office)
  • Division of Oncology
    Campus Box 8076
    Washington University School of Medicine
    660 South Euclid Avenue
    St. Louis, MO 63110
  • Lab website (www.shaolab.org)


Our lab is interested in mechanism-based translational research. We are particularly interested in understanding the biology of novel cancer targets with known clinical relevance but poorly understood molecular mechanisms. We believe by pursuing this type of research we may open doors to new therapeutic opportunities to complement the existing treatments. Currently we are focusing on two main projects in the context of breast cancer.

1. Profilin-1: an old protein with new functions

Profilin-1 is a well-characterized actin-binding protein essential for cell proliferation, survival and migration, yet showing paradoxical antitumor and anti-metastatic effects in several types of cancer including breast. Our recent work has shed light on the underlying mechanism and suggested a “spatial confinement” model to reconcile its opposing functions. Our data suggest that profilin-1 has important yet poorly understood functions in the nucleus in addition to its well-characterized role as an actin-binding and regulatory factor in the cytoplasm. We propose that it is this “moonlighting” activity of profilin-1 in the nucleus that gives rise to its antitumor effects. We are currently investigating the molecular mechanisms by which nuclear profilin-1 inhibits tumor growth and exploring opportunities to therapeutically target its activity.

2. VCP and DNA damage response

Valosin-containing protein (VCP) is an evolutionarily conserved AAA+ ATPase involved in diverse cellular processes. Functioning as a “segregase”, VCP facilitates protein homeostasis by extracting ubiquitinated proteins from various cellular locations or complexes for subsequent turnover. Recent studies have linked VCP to chromatin-associated protein degradation and genome stability maintenance particularly in the context of DNA damage response (DDR). In response to DNA double strand breaks, VCP is rapidly recruited to the damage sites and facilitates the proper assembly of multiple proteins (e.g. BRCA1 and 53BP1) needed for DNA damage repair. Nevertheless, detailed understanding of its mechanism of action (e.g. identity of its chromatin-associated client proteins), its mode of (de)regulation in cancer, and its relevance to cancer treatments (e.g. radiotherapy and chemotherapy) is lacking, and we are currently pursuing all these revenues.