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Related Concept Videos

Assembly of Signaling Complexes01:30

Assembly of Signaling Complexes

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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Receptor tyrosine kinases or RTKs are membrane-bound receptors that phosphorylate specific tyrosine on protein substrates. RTKs regulate cellular growth, differentiation, survival, and migration. They contain an extracellular ligand binding domain, a transmembrane domain, and a cytosolic tail with intrinsic kinase activity. Several extracellular signaling molecules activate RTKs in one or more ways and relay the signal downstream. Ligands such as platelet-derived growth factor (PDGF) or...
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G protein-coupled receptor (GPCR) signaling plays a crucial role in cell functioning. GPCR desensitization is an equally essential process. It allows cells to respond to changing environments and regain sensitivity to new stimuli while preventing unnecessary stimulation when no longer needed. Prolonged exposure to stimuli leads to GPCR desensitization. It involves blocking the receptors from binding and activating additional G proteins. This inhibits activation of downstream effectors, thereby...
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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

Updated: May 25, 2026

Detecting the Ligand-binding Domain Dimerization Activity of Estrogen Receptor Alpha Using the Mammalian Two-Hybrid Assay
09:07

Detecting the Ligand-binding Domain Dimerization Activity of Estrogen Receptor Alpha Using the Mammalian Two-Hybrid Assay

Published on: December 19, 2018

Stepwise androgen receptor dimerization.

Martin E van Royen1, Wiggert A van Cappellen, Carola de Vos

  • 1Department of Pathology, Josephine Nefkens Institute, Erasmus University Medical Center, Rotterdam, The Netherlands.

Journal of Cell Science
|February 14, 2012
PubMed
Summary
This summary is machine-generated.

Androgen receptor (AR) homodimerization involves intramolecular and intermolecular interactions, occurring before DNA binding. These distinct AR forms regulate gene expression differently, offering new therapeutic targets.

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Area of Science:

  • Molecular Biology
  • Cellular Signaling
  • Genetics

Background:

  • Androgen receptor (AR) function is crucial for gene expression, regulated by ligand binding, DNA binding, and protein-protein interactions.
  • Key AR interactions include DNA-binding domain (D-box) mediated homodimerization and N-terminal/ligand-binding domain (N/C) interactions.

Purpose of the Study:

  • To investigate the dynamics of AR homodimerization and the role of specific AR interactions.
  • To understand the spatiotemporal organization of AR intra- and inter-molecular interactions during gene regulation.

Main Methods:

  • Quantitative imaging techniques were employed to study AR interactions.
  • AR-regulated reporter assays were utilized to assess gene expression specificity.

Main Results:

  • Ligand binding induces an initial intramolecular AR N/C interaction in the cytoplasm.
  • This is followed by a D-box dimerization-dependent transition to intermolecular N/C interactions in nuclear AR.
  • Homodimerization steps precede DNA binding, with evidence of both nuclear AR homodimers and monomers.

Conclusions:

  • AR homodimers and monomers exhibit distinct roles in regulating gene expression via specific domain interactions.
  • The study elucidates critical spatiotemporal steps in AR intra- and inter-molecular interactions.