WDR26, 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, such as ubiquitination-mediated protein degradation, which is crucial for maintaining cellular protein homeostasis. WDR26 is also associated with important biological processes like erythropoiesis, cardiac cell response to hypoxia, and the regulation of canonical Wnt signaling pathway, highlighting its overall biological importance [1,2,3,4]. Genetic models, especially knockout (KO) mouse models, can provide insights into its function.

In a KO mouse model, loss of Wdr26 induced anemia in zebrafish and enucleation defects in mouse erythroblasts due to impaired nuclear condensation. As part of the glucose-induced degradation-deficient ubiquitin ligase complex, Wdr26 regulates the ubiquitination and degradation of nuclear proteins like lamin B. Failure of lamin B degradation blocks nuclear opening formation, leading to impaired clearance of nuclear proteins and delayed nuclear condensation [2]. Unbiased genetic forward screening in a genetically engineered mouse model of human multiple myeloma led to the discovery of WDR26 as a novel myeloma gene, suggesting its role in plasma cell neoplasia [1].

In conclusion, WDR26 is essential for processes such as erythroblast nuclear condensation and may be involved in the development of multiple myeloma. The study of WDR26 using KO mouse models has provided valuable insights into its role in these specific biological processes and disease conditions, enhancing our understanding of related biological functions and disease mechanisms.