Wdr26, also known as WD repeat-containing protein 26, is a core component of the carboxy-terminal to LisH (CTLH) E3 ubiquitin ligase complex. It is involved in multiple biological pathways, including substrate recognition in the context of the CTLH E3 ligase for non-canonical substrates, and has significance in processes like prodrug metabolism, cell development, and chromatin regulation [1,5,6].

Loss-of-function studies have provided insights into its role. In zebrafish, loss of Wdr26 induces anemia, and in mouse erythroblasts, it causes enucleation defects due to impaired nuclear condensation. As part of the glucose-induced degradation-deficient ubiquitin ligase complex, it regulates the ubiquitination and degradation of nuclear proteins such as lamin B [3]. In mammalian cells, Wdr26 knockout leads to over 2000 differentially expressed genes and over 32,000 differentially accessible chromatin regions, affecting genes regulated by AP-1 and NF-1 transcription factors [6].

In conclusion, Wdr26 is crucial for multiple biological functions. Its role in regulating nuclear condensation during erythropoiesis and chromatin accessibility has been revealed through model-based research. Additionally, its potential as a therapeutic target in multiple myeloma and its association with Skraban-Deardorff syndrome, an intellectual disability syndrome, highlight its significance in disease-related research [2,4,5].