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Related Concept Videos

Internal Receptors01:31

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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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Nuclear protein sorting regulates nucleus composition and gene expression, crucial for determining the fate of a eukaryotic cell. Hence, the entry and exit of molecules across the nuclear envelope is a tightly controlled process. Nuclear protein sorting can be inhibited by one of the following ways: 1) masking cargo signal sequences, 2) modifying the nuclear receptor's affinity for cargo, 3) controlling the nuclear pore size, 4) retaining the cargo during its transit to the cytosol or the...
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Multivesicular bodies (MVBs) are mature endosomes that sort ubiquitinated proteins and then fuse with lysosomes to degrade the sorted proteins. Epidermal growth factor (EGF) and its receptor (EGFR) form a complex that can be internalized through endocytosis, sorted into an MVB, and later degraded.
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Multiprotein signaling complexes are formed in a dynamic process involving protein-protein interactions at the cytoplasmic domain of transmembrane receptors or enzymatic and non-enzymatic proteins associated with the receptor. These complexes ensure the activation and propagation of intracellular signals that regulate cell functions.
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Related Experiment Video

Updated: Mar 17, 2026

Detecting the Ligand-binding Domain Dimerization Activity of Estrogen Receptor Alpha Using the Mammalian Two-Hybrid Assay
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Memo interacts with c-Src to control Estrogen Receptor alpha sub-cellular localization.

Anna Frei1,2, Gwen MacDonald1, Ingrid Lund3

  • 1Friedrich Miescher Institute for Biomedical Research, Maulbeerstrasse, Basel, Switzerland.

Oncotarget
|July 30, 2016
PubMed
Summary

Memo protein links heregulin and estrogen signaling in breast cancer, impacting cell migration and proliferation. This discovery offers new therapeutic targets for endocrine resistance.

Keywords:
ER alphaMemo1c-Srcestrogenheregulin

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Systems Biology of Metabolic Regulation by Estrogen Receptor Signaling in Breast Cancer
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Area of Science:

  • Oncology
  • Molecular Biology
  • Cell Signaling

Background:

  • Growth factor and steroid hormone signaling are crucial in breast cancer progression and therapy resistance.
  • The crosstalk between these pathways, particularly concerning endocrine resistance, is not fully understood.
  • Memo protein was previously identified as a regulator of heregulin-mediated breast cancer cell migration.

Purpose of the Study:

  • To investigate the role of Memo protein at the intersection of heregulin and estrogen signaling pathways in breast cancer.
  • To elucidate the molecular mechanisms by which Memo influences Estrogen Receptor alpha (ERα) function.
  • To determine Memo's impact on breast cancer cell migration and proliferation.

Main Methods:

  • Investigated Memo's interaction with heregulin and estrogen signaling pathways.
  • Assessed Memo's effect on Estrogen Receptor alpha (ERα) sub-cellular localization and phosphorylation.
  • Examined Memo's role in facilitating ERα and c-Src interaction and ERα Y537 phosphorylation.
  • Evaluated Memo's control over ERα extra-nuclear localization.

Main Results:

  • Memo protein acts as a key mediator between heregulin and estrogen signaling pathways in breast cancer cells.
  • Memo controls Estrogen Receptor alpha (ERα) sub-cellular localization, phosphorylation, and function downstream of heregulin and estrogen.
  • Memo facilitates the interaction between ERα and c-Src, promoting ERα Y537 phosphorylation.
  • Memo influences ERα's extra-nuclear localization, affecting breast cancer cell migration and proliferation.

Conclusions:

  • Memo is identified as a critical mediator linking heregulin and estrogen signaling in breast cancer.
  • Memo's regulation of ERα function is a key mechanism contributing to breast cancer cell migration and proliferation.
  • Targeting Memo may offer novel therapeutic strategies to overcome endocrine resistance in breast cancer.