The WW domain of WBP2 binds to the WW domain of Yes kinase-associated protein (YAP) through its PY motifs. This interaction is crucial for various cellular processes, including transcriptional regulation and signal transduction . WBP2 interacts with several WW-domain-containing proteins, such as:
These interactions trigger downstream signaling pathways both in vitro and in vivo .
WBP2 has been closely linked to the development of breast cancer. Studies have shown that the phosphorylated form of WBP2 can move into the nucleus and activate the transcription of estrogen receptor (ER) and progesterone receptor (PR), which are indicators of breast cancer development . Overexpression of WBP2 and activation of tyrosine phosphorylation upregulate signal cascades in the cross-regulation of the Wnt and ER signaling pathways in breast cancer .
When WBP2 binds with TAZ, it can accelerate migration and invasion, which are required for the transformed phenotypes of breast cancer cells. This suggests that WBP2 is a key player in regulating cell migration . Conversely, when WBP2 binds with WWOX, a tumor suppressor, ER transactivation and tumor growth can be suppressed .
Recombinant WBP2 is a form of the protein that is produced through recombinant DNA technology. This involves inserting the WBP2 gene into a suitable expression system, such as bacteria or yeast, to produce the protein in large quantities. Recombinant WBP2 is used in various research applications to study its structure, function, and role in diseases like breast cancer .