Identification of Abl-Induced Phosphorylation Sites on WBP2 and Abl- Dependent WBP2 Binding Partners
Date of Completion
2025
Thesis Type
College of Arts and Science Honors
Department
Biology
First Advisor
Bryan Ballif
Keywords
WBP2, Abl, CrkL, mass spectrometry
Abstract
WW domain binding protein 2 (WBP2) is considered an emerging gene involved in the regulation of breast cancer primarily due to its known ability to act as an estrogen receptor transcriptional coactivator. WBP2 contains 11 YXXP (tyrosine-X-X-proline) amino acid motifs and these are essential to WBP2’s Abl-induced binding to the CrkL-SH2 domain. It is hypothesized that Abl induces WBP2 tyrosine phosphorylation in YXXP motifs driving its interaction with CrkL and additional proteins. Using cell culture, immunoprecipitation, immunoblotting, and mass spectrometry techniques, we have identified Abl-induced tyrosine phosphorylation sites on WBP2 and have identified binding partners to WBP2, including Abl- regulated binding partners.
Recommended Citation
Girardet, Meg Boyer, "Identification of Abl-Induced Phosphorylation Sites on WBP2 and Abl- Dependent WBP2 Binding Partners" (2025). UVM College of Arts and Sciences College Honors Theses. 156.
https://scholarworks.uvm.edu/castheses/156