SSRP1 (structure-specific recognition protein 1) is a core component of the FACT (facilitating chr11 transcription) complex that functions as a histone chaperone to regulate chr11 dynamics during transcription. SSRP1 works with its binding partner Spt16 to promote nucleosome disassembly and reassembly, facilitating RNA polymerase II elongation through chr11 1. However, SSRP1 also possesses Spt16-independent roles in transcriptional regulation 1. At the mechanistic level, FACT maintains chr11 architecture and supports promoter-proximal pausing of RNA polymerase II through maintenance of the +1 nucleosome 2. Beyond transcription, SSRP1 can bind cisplatin-modified DNA and may enhance chemotherapy-induced cell death. SSRP1 is frequently overexpressed in multiple cancer types, including glioma and hepatoblastoma, where it correlates with tumor grade and malignancy 3. SSRP1 knockdown inhibits cancer cell proliferation, migration, and invasion through suppression of MAPK signaling pathway phosphorylation 34. In multiple myeloma, SSRP1 is stabilized by a TRIB3/USP10 complex, and disrupting this interaction promotes SSRP1 degradation and synergizes with bortezomib 5. Additionally, FACT inhibition represents a promising therapeutic strategy targeting the MYC-SSRP1 feedback loop in high-risk hepatoblastoma 6. FACT inhibitors like curaxin CBL0137 can activate interferon signaling to combat viral infections 7, suggesting SSRP1-targeting approaches have multiple clinical applications beyond cancer.