Date of Award


Publication Type

Master Thesis

Degree Name



Chemistry and Biochemistry

First Advisor

Otis Vacratsis


Pure sciences, Biological sciences



Creative Commons License

Creative Commons Attribution-Noncommercial-No Derivative Works 4.0 License
This work is licensed under a Creative Commons Attribution-Noncommercial-No Derivative Works 4.0 License.


Hierarchical phosphorylation of four Ser/Thr residues orchestrates the ubiquitination and proteasomal degradation of the transcriptional co-activator, β-catenin [16]. To the best of our knowledge, β-catenin is the only known protein with this tetraphosphorylation motif (TPM). However, the sophistication of this scheme prompted our hypothesis that there are other proteins regulated by this TPM.

Herein, we identified two novel TPM-containing proteins, TAZ and KLF7. Characterization of the TAZ and KLF7 TPMs revealed significant similarities and differences with respect to the biochemical role of the β-catenin TPM and demonstrated a functional consequence of their TPMs within the TAZ- and KLF7-mediated inhibition of adipogenesis.

We also provide the first direct evidence that TAZ is highly phosphorylated. Using mass spectrometry, we identified ten TAZ phosphorylation sites, of which three mapped to the TPM. Additionally, we present preliminary functional analyses of phosphorylation sites adjacent to the 14-3-3 binding site and WW domain of TAZ.