iProXProteomicsJin BaiHomo Sapienshttp://www.iprox.org/page/project.html?id=IPX0012195000bj@xzhmu.edu.cnXuZhou Medical UniversityiProXThe FOX transcription factor family plays a pivotal role in the malignant progression of tumors. We propose a hypothesis that FOXQ1 recruits p300 and BRD4 to super-enhancer regions. Our findings indicate that p300 acetylates Lys190 of FOXQ1, resulting in its recognition and binding by BRD4. Subsequently, BRD4 recruits RNA-Pol II to form a "FOXQ1-p300-BRD4-RNA Pol II" complex, which then binds to the super-enhancers of target genes. Meanwhile, acetylation at Lys190 of FOXQ1 directly enhances its binding affinity to super-enhancers. Consequently, more target oncogenes can be transcribed to promote CRC proliferation and metastasis. Our results suggest that FOXQ1 acts as a key regulator of super-enhancers, providing insights into its role in CRC and highlighting its potential as a therapeutic target.P300-dependent acetylation of the FOXQ1 complex activates super-enhancers to promote colorectal cancer proliferation and metastasis.Yang Wen-Dong WD, Zhang Zhi-Heng ZH, Zhao Man-Yi MY, Shao Ke K, Ma Yan-Feng YF, Shen Qi Q, Lu Meng-Ru MR, Shao Zhi-Ying ZY, Xu Jia-Yu JY, Cao Meng-Han MH, Meng Seng S, Chu Su-Fang SF, Yong Hong-Mei HM, Ding Jin J, Bai Jin JfalseThe potential binding proteins of FOXQ1 were detected by mass spectrometry technology, laying the foundation for the subsequent in-depth study of its molecular mechanismFirst, Flag-FOXQ1 was overexpressed in HCT-116 cells. Subsequently, the Flag-FOXQ1 complex was enriched via immunoprecipitation (IP) technology. The complex was then washed four times with phosphate-buffered saline (PBS), denatured in loading buffer by boiling, and separated via gel electrophoresis to obtain the protein components of the complex. Finally, mass spectrometry analysis was performed for identification.Mon Jun 09 00:00:00 GMT+01:00 2025PXD064807960640624346