Ubiquitin-Like 4A (UBL4A), also known as GDX, is a protein that contains a ubiquitin-like domain. This protein plays a critical role in various cellular processes, including protein degradation and regulation of essential cellular functions. UBL4A is involved in post-translational modifications, which are crucial for maintaining cellular homeostasis.
UBL4A is a small protein with a molecular weight of approximately 18.8 kDa. It is composed of 157 amino acids and is often expressed with a C-terminal His-tag for purification purposes. The recombinant form of UBL4A is typically produced in Escherichia coli (E. coli) and purified using conventional chromatography techniques .
UBL4A is involved in targeting cellular proteins for degradation. This process is essential for the regulation of protein levels within the cell and for the removal of damaged or misfolded proteins. In mammals, UBL4A plays a significant role during late spermiogenesis, a stage in sperm development where transcription is halted due to genome compaction. This creates a need for robust post-transcriptional regulation, which UBL4A helps to achieve .
Recent studies have highlighted the role of UBL4A in cancer, particularly in pancreatic ductal adenocarcinoma (PDAC). UBL4A has been found to inhibit autophagy-mediated proliferation and metastasis of cancer cells by targeting lysosome-associated membrane protein 1 (LAMP1). This interaction disrupts lysosomal function, leading to impaired autophagic degradation and accumulation of autophagosomes. High levels of UBL4A are associated with a favorable prognosis in PDAC patients, suggesting its potential as a therapeutic target .