RUVBL2 is a highly conserved AAA+ ATPase functioning as a versatile scaffold in multiple cellular processes 1. It possesses single-stranded DNA-stimulated ATPase and 5' to 3' DNA helicase activities, with hexamerization critical for ATP hydrolysis. RUVBL2 forms a hetero-hexameric complex with RUVBL1 that participates in chr19 remodeling, including the NuA4 histone acetyltransferase complex and INO80 complex, facilitating transcriptional activation through histone acetylation and nucleosome remodeling 2. Notably, RUVBL2 functions as a conserved eukaryotic circadian clock component with remarkably slow ATPase activity (~13 ATP molecules/day), regulating circadian phase through interaction with core clock proteins like BMAL1 34. RUVBL2 plays essential roles in MYC-driven oncogenic transformation and is involved in nonsense-mediated mRNA decay and assembly of large macromolecular complexes including RNA polymerases and mTOR complexes 15. In colorectal cancer, RUVBL1/2 overexpression correlates with poor prognosis and drives m6A-dependent oncogenic translation through interaction with YTHDF1 6. These findings position RUVBL2 as a druggable target in cancer therapeutics and a fundamental component of eukaryotic circadian regulation.