NSFL1C

NSFL1C refers to a protein encoded by the NSFL1C gene (also known as p47, NSF1C, or VCIP135) in humans. This protein is a critical component of the cellular machinery involved in membrane fusion events. Specifically, NSFL1C functions as a cofactor of N-ethylmaleimide-sensitive factor (NSF), an ATPase essential for vesicular transport, Golgi reassembly, and other membrane-related processes.

NSFL1C's primary role is to bind to NSF and modulate its activity. The NSFL1C-NSF complex is then recruited to specific membrane fusion sites, where it facilitates the disassembly of SNARE (soluble NSF attachment protein receptor) complexes. SNAREs are proteins that mediate the docking and fusion of vesicles with their target membranes. After fusion, the SNARE proteins form a stable complex that must be disassembled to allow the SNAREs to participate in further rounds of fusion. The NSF-NSFL1C complex provides the energy for this disassembly process, freeing the SNAREs and enabling continued membrane trafficking.

Defects in the NSFL1C gene have been linked to several human diseases, including congenital dyserythropoietic anemia type II (CDA II), a rare inherited disorder characterized by abnormalities in red blood cell formation. Mutations in NSFL1C disrupt the normal trafficking and processing of proteins involved in erythropoiesis, leading to the characteristic features of CDA II, such as multinucleated erythroblasts in the bone marrow. Research continues to investigate the precise mechanisms by which NSFL1C mutations cause CDA II and to explore potential therapeutic strategies for this condition.