Related Experiment Video
Updated: Jun 25, 2026
07:48
Tracking Drug-induced Changes in Receptor Post-internalization Trafficking by Colocalizational Analysis
Published on: July 3, 2015
Modulation of opioid receptor function by protein-protein interactions
Konstantinos Alfaras-Melainis1, Ivone Gomes, Raphael Rozenfeld
1Department of Pharmacology and Systems Therapeutics, Mount Sinai School of Medicine, New York, NY, USA.
Frontiers in Bioscience (Landmark Edition)
|March 11, 2009
Summary
Opioid receptors (MORP, DORP, KORP) are crucial for physiological functions and addiction. Protein interactions significantly influence their function, trafficking, signaling, and dimerization, impacting opiate analgesia.
Area of Science:
- Neuroscience
- Pharmacology
- Molecular Biology
Background:
- Opioid receptors (mu, delta, kappa) are G protein-coupled receptors (GPCRs) regulating vital physiological processes.
- Opioid alkaloids induce analgesia, euphoria, and addiction, linked to altered opioid receptor function.
- Protein-protein interactions are increasingly recognized as critical for opioid receptor regulation.
Purpose of the Study:
- To review protein interactions affecting opioid receptor biogenesis, trafficking, and signal transduction.
- To examine protein interactions that modulate opioid receptor endocytosis, degradation, and dimerization.
- To provide a comprehensive overview of protein-protein interactions in opioid receptor pharmacology.
Main Methods:
- Literature review of studies on opioid receptor protein interactions.
- Analysis of research on GPCRs, focusing on opioid receptor family A.
- Synthesis of findings related to receptor function, trafficking, signaling, and dimerization.
Main Results:
- Identified protein interactions crucial for opioid receptor biogenesis and trafficking.
- Summarized interactions affecting signal transduction pathways upon receptor activation.
- Highlighted protein roles in modulating receptor endocytosis, degradation, and dimerization.
- Discussed the significance of homo- and heterodimerization in opioid receptor function.
Conclusions:
- Protein-protein interactions are essential regulators of opioid receptor function and responsiveness.
- These interactions influence key processes from receptor synthesis to degradation and dimerization.
- Understanding these interactions is vital for comprehending opiate analgesia and addiction mechanisms.
More Related Videos
16:02Demonstration of the Sequence Alignment to Predict Across Species Susceptibility Tool for Rapid Assessment of Protein Conservation
Published on: February 10, 2023
09:09Preparation and Delivery of Protein Microcrystals in Lipidic Cubic Phase for Serial Femtosecond Crystallography
Published on: September 20, 2016
Related Concept Videos
01:22Opioid Receptors: Overview
Opioid receptors, including the mu (μ, MOR), delta (δ, DOR), and kappa (κ, KOR) types, belong to the rhodopsin family of G protein-coupled receptors. These receptors are located throughout the central and peripheral nervous systems and in non-neuronal tissues such as macrophages and astrocytes. Opioid receptor ligands can be categorized into agonists or antagonists. Highly selective agonists include [d-Ala2, MePhe4, Gly(ol)5]-enkephalin or DAMGO for MOR, [D-Pen2, D-Pen5]-enkephalin or DPDPE for...
01:25Analgesia and Pain Management
Pain is critical to various clinical pathologies, provoking an urgent need for effective management. Pain, whether acute or chronic, is a complex neurochemical process. Its alleviation depends on the type, with nonopioid analgesics effective for mild to moderate pain, such as musculoskeletal or inflammatory pain, while neuropathic pain responds best to anticonvulsants, tricyclic antidepressants, or serotonin/norepinephrine reuptake inhibitors. For severe acute or chronic pain, opioids may be...
01:20Opioid Analgesics: Morphine and Other Natural Cogeners
Opioids are a class of drugs that mimic endogenous opioid peptides and act on opioid receptors, and help in pain relief. These compounds are classified as natural, synthetic, or semi-synthetic. Natural opioids, like morphine, codeine, and thebaine, are derived from the opium poppy plant (Papaver somniferum or Papaver album) and are termed opiates. Synthetic opioids are artificial, while semi-synthetic opioids combine natural and synthetic compounds. Morphine, a prototypical opioid, possesses a...
01:29Drug-Receptor Interactions
Drug-receptor interaction describes the binding of receptors by drugs, but not all drug-receptor interactions result in activation and tissue response. For instance, the binding of agonists activates the receptor to generate a cellular reaction, while antagonists bind to receptors without causing their activation.
Several parameters, such as the drug's affinity for its receptor and its efficacy, which is its ability to activate the receptor, determine the drug's effect on the tissue.
Several parameters, such as the drug's affinity for its receptor and its efficacy, which is its ability to activate the receptor, determine the drug's effect on the tissue.
01:29The Two-State Receptor Model
The two-state receptor model explains a drug's interaction with receptors, such as G protein-coupled receptors and ligand-gated ion channels, to induce or inhibit a biological response. When no natural ligands are present, a receptor exists in an equilibrium of inactive (Ri) and active (Ra) conformations. The inactive form does not produce a response, while the active form generates a basal effect known as constitutive activity.
The binding affinity of a drug determines its interaction with one...
The binding affinity of a drug determines its interaction with one...
01:58Cooperative Allosteric Transitions
Cooperative allosteric transitions can occur in multimeric proteins, where each subunit of the protein has its own ligand-binding site. When a ligand binds to any of these subunits, it triggers a conformational change that affects the binding sites in the other subunits; this can change the affinity of the other sites for their respective ligands. The ability of the protein to change the shape of its binding site is attributed to the presence of a mix of flexible and stable segments in the...