paul housley

Paul R. Housley, Ph.D
Associate Professor
Postdoctoral: University of Michigan
Ph.D: University of Michigan
Contact Information:
Phone: 803-216-3509
FAX: 803-216-3538

Research Focus:

housley lab photoOur lab investigates the fundamental mechanisms involved in steroid receptor-mediated gene regulation. The glucocorticoid receptor is cytoplasmic in the hormone-free state, and becomes localized to the nucleus after hormone binding. We are studying the molecular partners involved in receptor recycling between the nucleus and cytoplasm. The glucocorticoid receptor is phosphorylated on multiple sites, and another project is aimed at defining the biological roles of these phosphorylation events and how this modification alters receptor protein structure. We have found that certain phosphorylation sites may be involved in receptor trafficking or in target gene expression. Additional projects include determining the mechanisms of oncogene repression of glucocorticoid receptor gene expression, exploring the effects of tumors on neurophysiology and behavior, and defining the mechanisms of protein trafficking to the cell surface to form heteromeric glutamate receptors.

Recent Publications

Pubmed Link

  • Fisher JL, Housley PR (2013) Agonist binding to the GluK5 subunit is sufficient for functional surface expression of heteromeric GluK2/GluK5 kainate receptors. Cell Molecular Neurobiology 33:1099-1108.
  • Galigniana MD, Harrell JM, Housley PR, Patterson C, Fisher SK, Pratt WB (2004) Retrograde transport of the glucocorticoid receptor in neurites requires dynamic assembly of complexes with the protein chaperone hsp90 and is linked to the CHIP component of the machinery for proteosomal degradation. Molecular Brain Research 123: 27-36.
  • Cabral ALB, Hays AN, Housley PR, Brentani MM, Martins VR (2001) Repression of glucocorticoid receptor gene transcription by c-Jun. Molecular and Cellular Endocrinology 175: 67-79.
  • Wan Y, Coxe KK, Thackray VG, Housley PR, Nordeen SK (2001) Separable features of the ligand-binding domain determine the differential subcellular localization and ligand-binding specificity of glucocorticoid receptor and progesterone receptor. Molecular Endocrinology 15: 17-31.