RFFL (Ring Finger and FYVE-like Domain Containing E3 Ubiquitin Protein Ligase), also known as RNF189 or HAROSIN, is a member of the E3 ubiquitin ligase family characterized by its N-terminal RING finger domain and a C-terminal FYVE-like domain. These structural motifs enable RFFL to mediate protein ubiquitination, a critical post-translational modification that regulates protein stability, localization, and interactions. RFFL plays a role in diverse cellular processes, including apoptosis, autophagy, and signal transduction, often by targeting specific substrates for proteasomal degradation.
Research has linked RFFL to several pathological conditions. It interacts with and ubiquitinates proteins involved in inflammatory pathways (e.g., RIPK1/NF-κB) and tumorigenesis, suggesting roles in cancer progression and immune regulation. For instance, RFFL overexpression has been observed in certain cancers, where it may promote cell survival or metastasis. Conversely, its dysregulation is implicated in neurodegenerative diseases due to impaired protein quality control.
Antibodies targeting RFFL are essential tools for studying its expression, localization, and molecular interactions. They enable applications like Western blotting, immunoprecipitation, and immunohistochemistry, aiding in the exploration of RFFL's functional mechanisms and therapeutic potential. Commercial RFFL antibodies are typically validated for specificity against conserved epitopes, though challenges remain in distinguishing isoforms or post-translationally modified variants. Continued research aims to clarify RFFL's context-dependent roles and its viability as a diagnostic or therapeutic target.