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  • 1.
    Kalkat, Manpreet
    et al.
    Univ Toronto, Canada; Univ Hlth Network, Canada.
    Resetca, Diana
    Univ Toronto, Canada; Univ Hlth Network, Canada.
    Lourenco, Corey
    Univ Toronto, Canada; Univ Hlth Network, Canada.
    Chan, Pak-Kei
    Univ Hlth Network, Canada.
    Wei, Yong
    Univ Hlth Network, Canada; Struct Genom Consortium, Canada.
    Shiah, Yu-Jia
    Ontario Inst Canc Res, Canada.
    Vitkin, Natasha
    Univ Hlth Network, Canada.
    Tong, Yufeng
    Struct Genom Consortium, Canada; Univ Toronto, Canada.
    Sunnerhagen, Maria
    Linköping University, Department of Physics, Chemistry and Biology, Chemistry. Linköping University, Faculty of Science & Engineering.
    Done, Susan J.
    Univ Toronto, Canada; Univ Hlth Network, Canada.
    Boutros, Paul C.
    Univ Toronto, Canada; Ontario Inst Canc Res, Canada.
    Raught, Brian
    Univ Toronto, Canada; Univ Hlth Network, Canada.
    Penn, Linda Z.
    Univ Toronto, Canada; Univ Hlth Network, Canada.
    MYC Protein Interactome Profiling Reveals Functionally Distinct Regions that Cooperate to Drive Tumorigenesis2018In: Molecular Cell, ISSN 1097-2765, E-ISSN 1097-4164, Vol. 72, no 5, p. 836-+Article in journal (Refereed)
    Abstract [en]

    Transforming members of the MYC family (MYC, MYCL1, and MYCN) encode transcription factors containing six highly conserved regions, termed MYC homology boxes (MBs). By conducting proteomic profiling of the MB interactomes, we demonstrate that half of the MYC interactors require one or more MBs for binding. Comprehensive phenotypic analyses reveal that two MBs, MBO and MBII, are universally required for transformation. MBII mediates interactions with acetyltransferase-containing complexes, enabling histone acetylation, and is essential for MYC-dependent tumor initiation. By contrast, MBO mediates interactions with transcription elongation factors via direct binding to the general transcription factor TFIIF. MBO is dispensable for tumor initiation but is a major accelerator of tumor growth. Notably, the full transforming activity of MYC can be restored by co-expression of the non-transforming MBO and MBII deletion proteins, indicating that these two regions confer separate molecular functions, both of which are required for oncogenic MYC activity.

  • 2.
    Stender, Joshua D
    et al.
    Department of Cellular and Molecular Medicine, University of California, San Diego, La Jolla, CA 92093, USA.
    Nwachukwu, Jerome C
    Department of Cancer Biology, The Scripps Research Institute, 130 Scripps Way, Jupiter, FL 33458, USA.
    Kastrati, Irida
    Department of Physiology and Biophysics, University of Illinois at Chicago, Chicago, IL 60612, USA.
    Kim, Yohan
    Department of Pathology and Laboratory Medicine, Schulich School of Medicine and Dentistry, Western University, London, ON N6A 5C1, Canada.
    Strid, Tobias
    Department of Cellular and Molecular Medicine, University of California, San Diego, La Jolla, CA 92093, USA.
    Yakir, Maayan
    Department of Cellular and Molecular Medicine, University of California, San Diego, La Jolla, CA 92093, USA.
    Srinivasan, Sathish
    Department of Cancer Biology, The Scripps Research Institute, 130 Scripps Way, Jupiter, FL 33458, USA.
    Nowak, Jason
    Department of Cancer Biology, The Scripps Research Institute, 130 Scripps Way, Jupiter, FL 33458, USA.
    Izard, Tina
    Department of Cancer Biology, The Scripps Research Institute, 130 Scripps Way, Jupiter, FL 33458, USA.
    Rangarajan, Erumbi S
    Department of Cancer Biology, The Scripps Research Institute, 130 Scripps Way, Jupiter, FL 33458, USA.
    Carlson, Kathryn E
    Department of Chemistry, University of Illinois at Urbana-Champaign, 600 South Mathews Avenue, Urbana, IL 61801, USA.
    Katzenellenbogen, John A
    Department of Chemistry, University of Illinois at Urbana-Champaign, 600 South Mathews Avenue, Urbana, IL 61801, USA.
    Yao, Xin-Qiu
    Department of Computational Medicine and Bioinformatics, University of Michigan Medical School, Ann Arbor, MI 48109, USA.
    Grant, Barry J
    Department of Computational Medicine and Bioinformatics, University of Michigan Medical School, Ann Arbor, MI 48109, USA.
    Leong, Hon S
    Department of Surgery, Schulich School of Medicine and Dentistry, Western University, London, ON N6A 5C1, Canada.
    Lin, Chin-Yo
    Center for Nuclear Receptors and Cell Signaling, Department of Biology and Biochemistry, University of Houston, Houston, TX 77204, USA.
    Frasor, Jonna
    Department of Physiology and Biophysics, University of Illinois at Chicago, Chicago, IL 60612, USA.
    Nettles, Kendall W
    Department of Cancer Biology, The Scripps Research Institute, 130 Scripps Way, Jupiter, FL 33458, USA.
    Glass, Christopher K
    Department of Cellular and Molecular Medicine, University of California, San Diego, La Jolla, CA 92093, USA.
    Structural and Molecular Mechanisms of Cytokine-Mediated Endocrine Resistance in Human Breast Cancer Cells2017In: Molecular Cell, ISSN 1097-2765, E-ISSN 1097-4164, Vol. 65, no 6, p. 1122-1135.e5, article id S1097-2765(17)30122-3Article in journal (Refereed)
    Abstract [en]

    Human breast cancers that exhibit high proportions of immune cells and elevated levels of pro-inflammatory cytokines predict poor prognosis. Here, we demonstrate that treatment of human MCF-7 breast cancer cells with pro-inflammatory cytokines results in ERα-dependent activation of gene expression and proliferation, in the absence of ligand or presence of 4OH-tamoxifen (TOT). Cytokine activation of ERα and endocrine resistance is dependent on phosphorylation of ERα at S305 in the hinge domain. Phosphorylation of S305 by IKKβ establishes an ERα cistrome that substantially overlaps with the estradiol (E2)-dependent ERα cistrome. Structural analyses suggest that S305-P forms a charge-linked bridge with the C-terminal F domain of ERα that enables inter-domain communication and constitutive activity from the N-terminal coactivator-binding site, revealing the structural basis of endocrine resistance. ERα therefore functions as a transcriptional effector of cytokine-induced IKKβ signaling, suggesting a mechanism through which the tumor microenvironment controls tumor progression and endocrine resistance.

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