Anti-UFD1L antibody

Supplementary info

This supplementary information is collated from multiple sources and compiled automatically.

Activity summary

UFD1L also known as Ubiquitin Fusion Degradation 1 Like is a protein with a molecular mass of approximately 35 kDa. It is expressed throughout most human tissues with higher levels observed in the brain heart and skeletal muscle. UFD1L plays an active role in the process of protein degradation by interacting with other molecules in the cell. This protein is part of the ubiquitin proteasome pathway and it partners with NPL4 and VCP/p97 making up a critical component of the ubiquitin-dependent degradation machinery.

Biological function summary

UFD1L interacts with cellular mechanisms for quality control by forming a complex with NPL4 and the ATPase VCP/p97. It functions to recognize and bind misfolded proteins earmarked for degradation thereby regulating protein homeostasis. This UFD1L complex assists in the extraction of ubiquitinated substrates from membranes and chromatin ensuring that only properly folded proteins are allowed to accumulate in cells which is essential for maintaining cellular function.

Pathways

UFD1L is integrally involved in the ER-associated degradation (ERAD) and the ubiquitin-proteasome pathway. In the ERAD pathway UFD1L works closely with VCP/p97 facilitating the removal of misfolded or excess proteins from the endoplasmic reticulum. It contributes to the regulation of the cell cycle and stress responses by ensuring efficient ubiquitin-dependent protein turnover. Its interaction with these pathways highlights its connection to a tightly regulated network of proteins including those involved in proteostasis and cellular stress regulation.

Associated diseases and disorders

UFD1L has been implicated in the pathogenesis of neurodegenerative disorders such as amyotrophic lateral sclerosis (ALS) and Alzheimer's disease. The inappropriate function or expression of UFD1L and its associated proteins including VCP/p97 and NPL4 can lead to the accumulation of misfolded proteins a hallmark in these diseases. Further alterations in UFD1L are also associated with congenital disorders like DiGeorge syndrome linking it to critical developmental processes that go awry when protein degradation pathways are disrupted.