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Related Concept Videos

Transducer Mechanism: Nuclear Receptors01:31

Transducer Mechanism: Nuclear Receptors

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Nuclear receptors, or NRs, are unique transcription factors that regulate gene transcription and affect the cellular pathways involved in reproduction, development, or metabolism. Their ability to be stimulated by small lipophilic ligands and control vital cellular processes makes them ideal drug targets. Nearly 10-15% of currently prescribed drugs target these receptors.
About 48 different soluble family members of nuclear receptors are identified that can be divided into two main classes:
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Regulation of Nuclear Protein Sorting01:45

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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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Signal Transduction: Overview01:26

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Cells respond to many types of information, often through receptor proteins positioned on the membrane. They respond to chemical signals, such as hormones, neurotransmitters, and other signaling molecules, initiating a series of molecular reactions to produce an appropriate response. This is called signal transduction. Cells also coordinate different responses elicited by the same signaling molecule via mediators, allowing molecular cross-talk.
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Types of Receptors: Internal Receptors01:07

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Many cellular signals are hydrophilic and cannot pass through the plasma membrane. However, small or hydrophobic signaling molecules can cross the hydrophobic core of the plasma membrane and bind intracellular receptors that reside within the cell cytoplasm or nucleus. Many mammalian steroid hormones and nitric oxide (NO) gas use this cell signaling mechanism.
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Internal Receptors01:31

Internal Receptors

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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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Receptor Downregulation in MVBs01:15

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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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Related Experiment Video

Updated: Jan 3, 2026

Reverse Yeast Two-hybrid System to Identify Mammalian Nuclear Receptor Residues that Interact with Ligands and/or Antagonists
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Cell adhesion signals regulate the nuclear receptor activity.

Kotaro Sugimoto1, Naoki Ichikawa-Tomikawa1, Korehito Kashiwagi1

  • 1Department of Basic Pathology, Fukushima Medical University School of Medicine, 960-1295 Fukushima, Japan.

Proceedings of the National Academy of Sciences of the United States of America
|November 20, 2019
PubMed
Summary
This summary is machine-generated.

Cell adhesion protein claudin-6 (CLDN6) activates Src-family kinases (SFKs), initiating a signaling cascade that regulates nuclear receptor activity, impacting cell growth and differentiation.

Keywords:
claudinestrogen receptorretinoic acid receptorsignal transductiontight junction

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Area of Science:

  • Molecular biology
  • Cell biology
  • Biochemistry

Background:

  • Cell adhesion is crucial for tissue integrity and function in multicellular organisms.
  • Cell adhesion molecules regulate diverse cellular processes, but the molecular mechanisms are not fully understood.
  • Tight-junction proteins, like claudin-6 (CLDN6), play key roles in cell adhesion and signaling.

Purpose of the Study:

  • To elucidate the molecular basis of cell adhesion signaling initiated by CLDN6.
  • To identify how CLDN6 regulates nuclear receptor activity.
  • To investigate the signaling pathway linking CLDN6 to nuclear receptors.

Main Methods:

  • Investigated the interaction between CLDN6 and Src-family kinases (SFKs).
  • Analyzed the phosphorylation of CLDN6 by SFKs.
  • Examined the CLDN6/SFK/PI3K/AKT signaling pathway's effect on nuclear receptors, including retinoic acid receptor γ (RARγ) and estrogen receptor α (ERα).

Main Results:

  • CLDN6 recruits and activates SFKs, which then phosphorylate CLDN6.
  • The CLDN6/SFK/PI3K/AKT pathway stimulates RARγ and ERα activity by targeting conserved phosphorylation sites.
  • Identified conserved phosphorylation motifs in 14 out of 48 human nuclear receptors.

Conclusions:

  • CLDN6-initiated cell adhesion signaling directly regulates nuclear receptor activity.
  • A conserved mechanism links cell adhesion to nuclear receptor signaling, influencing physiological and pathological processes.
  • This finding provides a novel understanding of how cell adhesion impacts gene expression and cellular functions.