Dcaf11, also known as Ddb1-and Cul4-associated factor 11, is an E3 ligase substrate adaptor that plays crucial roles in multiple biological processes. It is involved in pathways such as ubiquitin-proteasome-mediated proteolysis, which is essential for regulating protein levels in cells. This gene is important for maintaining chromosome stability, cell cycle progression, and redox homeostasis [1,2,3,4].

In early embryos and embryonic stem cells, deletion of Dcaf11 leads to reduced telomere sister-chromatid exchange and impairs telomere lengthening. Dcaf11-deficient mice exhibit gradual telomere erosion over successive generations, and hematopoietic stem cell activity is greatly compromised. Mechanistically, Dcaf11 targets Kap1 for ubiquitination-mediated degradation, activating the Zscan4 downstream enhancer and removing heterochromatic H3K9me3 at telomere/subtelomere regions [1]. In human osteosarcoma cells, knocking down components of the CRL4BDCAF11 complex (including DCAF11) attenuates the ubiquitination level of p21Cip1, inhibits cell proliferation, leads to cell cycle arrest at S phase, and decreases colony formation rate [3].

In conclusion, Dcaf11 is vital for telomere elongation in early embryos and stem cells, as well as for regulating cell cycle progression in osteosarcoma cells. Studies using Dcaf11-deficient mouse models have provided valuable insights into its role in maintaining chromosome stability and cell-cycle-related diseases, helping to understand the underlying molecular mechanisms and potentially paving the way for new therapeutic strategies.