{
    "record_id": "pubmed.10409727", 
    "reference": {
        "url": "https://www.ncbi.nlm.nih.gov/pubmed/10409727", 
        "type": "PubMed", 
        "id": "10409727"
    }, 
    "title": "Purification and identification of p68 RNA helicase acting as a transcriptional coactivator specific for the activation function 1 of human estrogen receptor alpha.", 
    "mutagenesis": [], 
    "journal": "Mol. Cell. Biol.", 
    "abstract": "The estrogen receptor (ER) regulates the expression of target genes in a ligand-dependent manner. The ligand-dependent activation function AF-2 of the ER is located in the ligand binding domain (LBD), while the N-terminal A/B domain (AF-1) functions in a ligand-independent manner when isolated from the LBD. AF-1 and AF-2 exhibit cell type and promoter context specificity. Furthermore, the AF-1 activity of the human ERalpha (hERalpha) is enhanced through phosphorylation of the Ser(118) residue by mitogen-activated protein kinase (MAPK). From MCF-7 cells, we purified and cloned a 68-kDa protein (p68) which interacted with the A/B domain but not with the LBD of hERalpha. Phosphorylation of hERalpha Ser(118) potentiated the interaction with p68. We demonstrate that p68 enhanced the activity of AF-1 but not AF-2 and the estrogen-induced as well as the anti-estrogen-induced transcriptional activity of the full-length ERalpha in a cell-type-specific manner. However, it did not potentiate AF-1 or AF-2 of ERbeta, androgen receptor, retinoic acid receptor alpha, or mineralocorticoid receptor. We also show that the RNA helicase activity previously ascribed to p68 is dispensable for the ERalpha AF-1 coactivator activity and that p68 binds to CBP in vitro. Furthermore, the interaction region for p68 in the ERalpha A/B domain was essential for the full activity of hERalpha AF-1. Taken together, these findings show that p68 acts as a coactivator specific for the ERalpha AF-1 and strongly suggest that the interaction between p68 and the hERalpha A/B domain is regulated by MAPK-induced phosphorylation of Ser(118).", 
    "glycosylation": [], 
    "snv": [], 
    "referenced_glycans": [], 
    "phosphorylation": [], 
    "authors": "Maruyama K., Kobayashi Y., Hashimoto S., Kato S., Goto M., Endoh H., Yanagisawa J., Masuhiro Y., Metzger D., Tai H.", 
    "date": "1999", 
    "referenced_proteins": [
        "P17844-1", 
        "P03372-1"
    ], 
    "species": [
        {
            "common_name": "Human", 
            "taxid": 9606, 
            "name": "Homo sapiens", 
            "evidence": [
                {
                    "url": "https://www.uniprot.org/uniprot/P17844", 
                    "id": "P17844", 
                    "database": "UniProtKB"
                }
            ]
        }
    ], 
    "glycation": []
}