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In animals, gender is determined by the number and type of sex chromosome. For example, human females have two X chromosomes, and males have one X and one Y chromosome, whereas C.elegans with one X chromosome is a male, and the one with two X chromosomes is a hermaphrodite.
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Many cellular signals are hydrophilic and therefore cannot pass through the plasma membrane. However, small or hydrophobic signaling molecules can cross the hydrophobic core of the plasma membrane and bind to internal, or intracellular, receptors that reside within the cell. Many mammalian steroid hormones use this mechanism of cell signaling, as does nitric oxide (NO) gas.
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Related Experiment Video

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Detecting the Ligand-binding Domain Dimerization Activity of Estrogen Receptor Alpha Using the Mammalian Two-Hybrid Assay
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DDX3X functionally and physically interacts with Estrogen Receptor-alpha.

Jyotsna Pardeshi1, Niamh McCormack1, Lili Gu1

  • 1Biology Department, Kathleen Lonsdale Institute for Human Health Research, Maynooth University, Maynooth, Co. Kildare, Ireland.

Biochimica Et Biophysica Acta. Gene Regulatory Mechanisms
|February 5, 2022
PubMed
Summary
This summary is machine-generated.

DEAD-box protein 3X (DDX3X) interacts with Estrogen Receptor alpha (ERα), enhancing its activity and promoting breast cancer cell growth. This discovery reveals a new mechanism for DDX3X

Keywords:
Breast cancerDEAD-box helicaseEstrogen receptorIKKεTamoxifen resistance

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Profiling of Estrogen-regulated MicroRNAs in Breast Cancer Cells
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Area of Science:

  • * Molecular and Cellular Biology
  • * Oncology
  • * Biochemistry

Background:

  • * DEAD-box protein 3X (DDX3X) is involved in RNA metabolism and signaling pathways.
  • * DDX3X functions as an adaptor molecule in innate immune signaling, interacting with IKB-kinase-epsilon (IKKε).
  • * Both DDX3X and IKKε are implicated as oncogenes in breast cancer, with IKKε potentially phosphorylating Estrogen Receptor alpha (ERα).

Purpose of the Study:

  • * To investigate the novel interaction between DDX3X and ERα.
  • * To elucidate the role of DDX3X in ERα activation and breast cancer progression.
  • * To determine if DDX3X contributes to estrogen-independent ERα activity.

Main Methods:

  • * Co-immunoprecipitation and pulldown assays to confirm physical interaction between DDX3X and ERα.
  • * DDX3X knockdown and overexpression experiments in ER+ breast cancer cell lines.
  • * Measurement of ERα phosphorylation, Estrogen Response Element (ERE)-controlled reporter gene expression, and ERα target gene expression.

Main Results:

  • * A novel physical interaction between DDX3X and ERα was identified.
  • * DDX3X knockdown reduced ERα phosphorylation, ERE-driven transcription, target gene expression, and cell proliferation.
  • * DDX3X overexpression enhanced ERα phosphorylation and activity.

Conclusions:

  • * DDX3X physically binds to ERα and positively regulates its activation.
  • * DDX3X acts as an adaptor to facilitate IKKε-mediated ERα activation, similar to its role in innate immunity.
  • * This mechanism contributes to the oncogenic role of DDX3X in breast cancer and may be linked to endocrine therapy resistance.