Ubiquitin recognition factor in ER-associated degradation protein 1 (UFD1 (also referred to as UFD1L in human gene context))

Ubiquitin recognition factor in ER-associated degradation protein 1 (UFD1, also known as UFD1L in human genetic nomenclature) is an essential adapter protein that forms a ternary complex with NPL4 and the AAA-ATPase VCP/p97. This complex plays a critical role in the export of misfolded proteins from the endoplasmic reticulum (ER) to the cytosol for proteasomal degradation, a process known as ER-associated degradation (ERAD)[2][1][3]. UFD1 is also involved in cell cycle progression, regulating the stability of the cell-cycle protein Skp2 to enable proper cell cycle arrest under ER stress[1]. In addition, the UFD1-NPL4-VCP complex is essential for spindle disassembly and formation of the nuclear envelope after mitosis, and it acts as a negative regulator of type I interferon production by targeting proteins such as DDX58/RIG-I for ubiquitin-mediated degradation[2]. Mutations in the human UFD1L gene are linked to severe developmental disorders, including cardiac and craniofacial abnormalities in 22q11.2 deletion syndrome (Catch 22 syndrome)[3]. While UFD1 is vital for cellular homeostasis, it is not currently a direct therapeutic target; no drugs are known to directly modulate its activity, but its function is of high interest in diseases involving protein folding, cancer, and development[3][2][1].

Other names

Ubiquitin fusion degradation protein 1Ufd1UFD1L (in humans)Ubiquitin fusion degradation protein 1 homolog (in certain databases)