{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,2]],"date-time":"2026-10-02T20:15:20Z","timestamp":1790972120072,"version":"4.1.0"},"reference-count":43,"publisher":"National Academy of Sciences","issue":"14","content-domain":{"domain":["www.pnas.org"],"crossmark-restriction":true},"short-container-title":["Proc. Natl. Acad. Sci. U.S.A."],"published-print":{"date-parts":[[2003,7,8]]},"abstract":"<jats:p>\n                    The\n                    <jats:italic>MLL<\/jats:italic>\n                    (\n                    <jats:italic>mixed-lineage leukemia<\/jats:italic>\n                    ) gene is involved in many\n chromosomal translocations associated with acute myeloid and lymphoid\n leukemia. We previously identified a transcriptional repression domain in MLL,\n which contains a region with homology to DNA methyltransferase. In chromosomal\n translocations, the MLL repression domain is retained in the leukemogenic\n fusion protein and is required for transforming activity of MLL fusion\n proteins. We explored the mechanism of action of the MLL repression domain.\n Histone deacetylase 1 interacts with the MLL repression domain, partially\n mediating its activity; binding of Cyp33 to the adjacent MLL-PHD domain\n potentiates this binding. Because the MLL repression domain activity was only\n partially relieved with the histone deacetylase inhibitor trichostatin A, we\n explored other protein interactions with this domain. Polycomb group proteins\n HPC2 and BMI-1 and the corepressor C-terminal-binding protein also bind the\n MLL repression domain. Expression of exogenous BMI-1 potentiates MLL\n repression domain activity. Functional antagonism between Mll and Bmi-1 has\n been shown genetically in murine knockout models for\n                    <jats:italic>Mll<\/jats:italic>\n                    and\n                    <jats:italic>Bmi-1<\/jats:italic>\n                    . Our new data suggest a model whereby recruitment of BMI-1 to\n the MLL protein may be able to modulate its function. Furthermore, repression\n mediated by histone deacetylases and that mediated by polycomb group proteins\n may act either independently or together for MLL function\n                    <jats:italic>in\n vivo<\/jats:italic>\n                    .\n                  <\/jats:p>","DOI":"10.1073\/pnas.1436338100","type":"journal-article","created":{"date-parts":[[2003,7,8]],"date-time":"2003-07-08T15:18:15Z","timestamp":1057677495000},"page":"8342-8347","update-policy":"https:\/\/doi.org\/10.1073\/pnas.cm10313","source":"Crossref","is-referenced-by-count":165,"title":["MLL repression domain interacts with histone deacetylases, the polycomb group proteins HPC2 and BMI-1, and the corepressor C-terminal-binding protein"],"prefix":"10.1073","volume":"100","author":[{"given":"Zhen-Biao","family":"Xia","sequence":"first","affiliation":[{"name":"Department of Medicine, Molecular Oncology Program, Cardinal Bernardin\r Cancer Center, Loyola University Medical Center, Maywood, IL 60153"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Melanie","family":"Anderson","sequence":"additional","affiliation":[{"name":"Department of Medicine, Molecular Oncology Program, Cardinal Bernardin\r Cancer Center, Loyola University Medical Center, Maywood, IL 60153"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Manuel O.","family":"Diaz","sequence":"additional","affiliation":[{"name":"Department of Medicine, Molecular Oncology Program, Cardinal Bernardin\r Cancer Center, Loyola University Medical Center, Maywood, IL 60153"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Nancy J.","family":"Zeleznik-Le","sequence":"additional","affiliation":[{"name":"Department of Medicine, Molecular Oncology Program, Cardinal Bernardin\r Cancer Center, Loyola University Medical Center, Maywood, IL 60153"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"341","published-online":{"date-parts":[[2003,6,26]]},"reference":[{"key":"e_1_3_2_1_2","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.88.23.10735"},{"key":"e_1_3_2_2_2","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.89.24.11794"},{"key":"e_1_3_2_3_2","doi-asserted-by":"publisher","DOI":"10.1038\/ng1092-113"},{"key":"e_1_3_2_4_2","doi-asserted-by":"publisher","DOI":"10.1016\/0092-8674(92)90602-9"},{"key":"e_1_3_2_5_2","doi-asserted-by":"publisher","DOI":"10.1016\/0092-8674(92)90603-A"},{"key":"e_1_3_2_6_2","doi-asserted-by":"publisher","DOI":"10.1056\/NEJM199309233291302"},{"key":"e_1_3_2_7_2","first-page":"59","volume":"36","year":"1999","unstructured":"Rowley, J. 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