{"database":"iProX","file_versions":[],"scores":null,"additional":{"omics_type":["Proteomics"],"submitter":["Jin Bai"],"species":["Homo Sapiens"],"full_dataset_link":["http://www.iprox.org/page/project.html?id=IPX0012195000"],"submitter_email":["bj@xzhmu.edu.cn"],"submitter_affiliation":["XuZhou Medical University"],"sample_protocol":[""],"repository":["iProX"],"data_protocol":[""],"pubmed_abstract":["The 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."],"pubmed_title":["P300-dependent acetylation of the FOXQ1 complex activates super-enhancers to promote colorectal cancer proliferation and metastasis."],"pubmed_authors":["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 J"],"additional_accession":[]},"is_claimable":false,"name":"The potential binding proteins of FOXQ1 were detected by mass spectrometry technology, laying the foundation for the subsequent in-depth study of its molecular mechanism","description":"First, 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.","dates":{"publication":"Mon Jun 09 00:00:00 GMT+01:00 2025"},"accession":"PXD064807","cross_references":{"TAXONOMY":["9606"],"pubmed":["40624346"]}}