WDR1 (WD repeat domain 1) is a cytoskeletal regulatory protein that primarily functions to induce actin filament disassembly in conjunction with ADF/cofilin family proteins 1. The protein preferentially promotes disassembly of ADF/cofilin-decorated actin filaments while exhibiting minimal effects on bare actin filaments, serving as more than just an ancillary co-factor but as a major regulator of actin dynamics 1. WDR1 mediates its effects through direct protein interactions, including binding to YAP protein via its N-terminal domain, which inhibits YAP phosphorylation and promotes YAP transcriptional activity 2. The protein plays critical roles in cellular processes including cytokinesis, cell migration, and cytoskeletal remodeling 3. Disease relevance includes periodic fever, immunodeficiency, and thrombocytopenia syndrome (PFIT), where homozygous WDR1 mutations cause impaired actin dynamics, increased inflammasome activity, and elevated IL-18 secretion 4. WDR1 has also been implicated in cancer progression, serving as a therapeutic target in glioma where small molecule inhibitors can disrupt WDR1-dependent cytoskeletal remodeling 5, and in pancreatic cancer metastasis through exosome-mediated mechanisms 2. Additionally, WDR1 polymorphisms correlate with metabolic parameters in certain populations 6.