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William Weis

Academic Appointments

Professional Snapshot

Administrative Appointments

  • Director, Graduate Program in Biophysics (1999 - 2008)

Professional Education

A.B.: Princeton University, Biochemical Sciences (1981)
Ph.D.: Harvard University, Biochemistry (1988)

Scientific Focus

Research Interests

Cadherin-based adhesion

Several distinct intercellular junctions connect epithelial cells. Two of these, the adherens junction and the desmosome, contain cadherin cell adhesion molecules. The extracellular regions of these transmembrane proteins mediate intercellular binding, while their cytoplasmic domains are linked to the actin- (adherens junction) or intermediate filament- (desmosome) based cytoskeletons. In this way the cytoskeletons of cells comprising a tissue are linked, imparting particular morphologies and mechanical strength to the tissue. The dynamics of these complex assemblies underlie changes in cell and tissue architecture that occur during development and in many cancers. Our research aims to understand the 3-dimensional architecture and dynamics of these junctions.

Wnt signaling
The Wnt signaling pathway controls cell fate determination during embryogenesis and in the normal renewal of tissues in the adult. beta-catenin is the central component of this pathway, where it serves as a transcriptional coactivator. In the absence of a secreted Wnt protein, non-junctional beta-catenin is bound in a multiprotein “destruction complex”. Formation of this complex promotes phosphorylation of beta-catenin, which targets it for degradation by the ubiquitin/proteosome pathway. Binding of a Wnt to cell surface receptors prevents phosphorylation of beta-catenin. The resulting stabilized beta-catenin enters the nucleus and activates transcription of Wnt target genes through its interactions with Tcf-family transcription factors, proteins that contain a beta-catenin-binding domain and a sequence-specific DNA-binding domain.

We are trying to understand the mechanisms by which formation of the destruction complex enhances the phosphorylation of ?-catenin, and how beta-catenin serves as a scaffold to link the sequence-specific Tcfs to components of the general transcription machinery. We are attempting to biochemically reconstitute...

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