Myotubularin-Related Protein 5 (SBF1) Antibody

Background

SBF1, also known as SET-binding factor 1, is a pseudophosphatase that is structurally related to the myotubularin family of phosphoinositide phosphatases but lacks enzymatic activity due to mutations in its active site. Instead, SBF1 functions as a scaffolding protein involved in various cellular signaling pathways, particularly those regulating cell growth, differentiation, and cytoskeletal organization. It is implicated in membrane trafficking and endosomal sorting processes, often in association with its partner protein, SBF2. SBF1 has been shown to interact with the SET domain of histone-modifying enzymes, suggesting a role in epigenetic regulation, though its precise mechanisms remain under investigation. It is widely expressed in human tissues, with high expression levels in the nervous system and muscle, reflecting its potential roles in neuronal signaling and muscle function. Mutations or dysregulation of SBF1 have been linked to Charcot-Marie-Tooth disease, a hereditary peripheral neuropathy, highlighting its significance in maintaining neuronal integrity. Structural studies have revealed conserved domains responsible for protein-protein interactions, allowing SBF1 to act as a molecular hub in signaling pathways. Functional analyses suggest that SBF1 modulates growth factor receptor signaling, particularly pathways involving PI3K-AKT and Ras, contributing to its role in cell survival and proliferation. Emerging evidence indicates that SBF1 may also regulate autophagy and intracellular trafficking, although these roles require further confirmation.