SYNJ2BP contains a PDZ domain, which is crucial for its interaction with other proteins. This domain allows SYNJ2BP to bind to the C-terminal PDZ domain-binding motif of its interaction partners . The protein is predominantly localized in the mitochondria and the plasma membrane, where it plays a role in cellular signaling and adhesion .
SYNJ2BP has been shown to interact with the cell adhesion molecule TMIGD1. This interaction is mediated by the PDZ domain of SYNJ2BP and the C-terminal PDZ domain-binding motif of TMIGD1 . SYNJ2BP can actively recruit TMIGD1 to mitochondria, providing a potential mechanism for the localization of TMIGD1 at mitochondria .
In addition to its role in cellular adhesion, SYNJ2BP is involved in the regulation of sprouting angiogenesis, a process critical for the formation of new blood vessels . This function is particularly important in the context of cancer, where SYNJ2BP has been shown to inhibit tumor growth and metastasis by activating the DLL4-mediated Notch signaling pathway .
SYNJ2BP has been implicated in various diseases, including hepatocellular carcinoma (HCC) and Loeys-Dietz Syndrome 4 . In HCC, SYNJ2BP expression is decreased, and its low expression is associated with poor prognosis . Studies have shown that SYNJ2BP inhibits HCC cell invasion, migration, and proliferation, suggesting its potential as a therapeutic target .
The recombinant form of SYNJ2BP is used in various research applications to study its function and interactions. Understanding the role of SYNJ2BP in cellular processes and disease mechanisms can provide insights into potential therapeutic strategies for conditions such as cancer and genetic disorders.