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Internal Receptors

Internal Receptors

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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Allosteric proteins have more than one ligand binding site; the binding of a ligand to any of these sites influences the binding of ligands to the other sites. When a protein is allosteric, its binding sites are called coupled or linked. In the case of enzymes, the site that binds to the substrate is known as the active site and the other site is known as the regulatory site. When a ligand binds to the regulatory site, this leads to conformational changes in the protein that can influence...

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The Equilibrium Binding Constant and Binding Strength

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Updated: Feb 15, 2026

A "Dual-Addition" Calcium Fluorescence Assay for the High-Throughput Screening of Recombinant G Protein-Coupled Receptors

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A Dual Binding Receptor for ER-phagy.

Noboru Mizushima¹

¹Department of Biochemistry and Molecular Biology, Graduate School and Faculty of Medicine, The University of Tokyo, Tokyo 113-0033, Japan.

Developmental Cell

|February 6, 2018

Summary

This summary is machine-generated.

Researchers identified CCPG1 as a receptor for ER-phagy, a process that degrades the endoplasmic reticulum (ER). This discovery is crucial for maintaining protein homeostasis, particularly in pancreatic cells.

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Area of Science:

Cell biology
Molecular biology
Autophagy research

Background:

Selective autophagy, specifically ER-phagy, is essential for cellular health.
Multiple receptors are known to mediate ER-phagy.
Maintaining endoplasmic reticulum (ER) protein homeostasis is critical for cell function.

Purpose of the Study:

To identify novel receptors involved in ER-phagy.
To elucidate the molecular mechanisms underlying ER-phagy.
To understand the role of ER-phagy in maintaining protein homeostasis in specific cell types.

Main Methods:

Investigated the function of ER membrane protein CCPG1 in ER-phagy.
Examined the interaction between CCPG1 and autophagy-related proteins (GABARAPs, FIP200).
Assessed the impact of CCPG1 on ER protein homeostasis, particularly in pancreatic acinar cells.

Main Results:

Identified CCPG1 as a novel ER-phagy receptor.
Demonstrated that CCPG1 interacts with GABARAPs and FIP200.
Showed that CCPG1 plays a role in maintaining ER protein homeostasis in pancreatic acinar cells.

Conclusions:

CCPG1 is a key receptor mediating ER-phagy.
The CCPG1-GABARAP-FIP200 complex is involved in selective ER degradation.
This pathway is important for cellular function, especially in pancreatic acinar cells.