P2x2 Receptor
P2x2 Receptor - Related Videos
16:36
Proteomics to Identify Proteins Interacting with P2X2 Ligand-Gated Cation Channels
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Cited by 13 •
2009
We describe a simple protocol to identify brain proteins that bind to the full length C terminus of ATP-gated P2X2 receptors. The extension and systematic application of this approach to all P2X receptors is expected to lead to a better understanding of P2X receptor signaling.
12:03
Receptor Autoradiography Protocol for the Localized Visualization of Angiotensin II Receptors
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Cited by 14 •
2016
Here we present a protocol to describe the localization of angiotensin II Type 1 receptors in the rat brain by quantitative, densitometric, in vitro receptor autoradiography using an iodine-125 labeled analog of angiotensin II.
12:02
High-throughput Analysis of Mammalian Olfactory Receptors: Measurement of Receptor Activation via Luciferase Activity
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Cited by 16 •
2014
Olfactory receptor activation patterns encode odor identity, but the lack of published data identifying odorant ligands for mammalian olfactory receptors hinders the development of a comprehensive model of odor coding. This protocol describes a method to facilitate high-throughput identification of olfactory receptor ligands and quantification of receptor activation.
01:07
Types of Receptors: Internal Receptors
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2023
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. Similar to membrane-bound receptors, the binding of a ligand to the intracellular receptor of causes a conformational change in the...
06:01
Extracellular Protein Microarray Technology for High Throughput Detection of Low Affinity Receptor-Ligand Interactions
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Cited by 4 •
2019
Here, we present a protocol to screen extracellular protein microarrays for identification of novel receptor-ligand interactions in high throughput. We also describe a method to enhance detection of transient protein-protein interactions by using protein-microbead complexes.
FAQs
ATP binding to extracellular regions of the receptor promotes a conformational change that opens its trimeric membrane pore. This links recognition of an external chemical signal to ion movement across the membrane. The resulting change in ionic balance provides a direct mechanism through which extracellular ATP can influence electrical activity in responsive cells.
When the channel opens, sodium and calcium move into the cell while potassium moves out. These opposing ion movements alter the cell’s membrane potential and produce depolarization. Calcium entry also makes the channel’s response relevant to signaling processes beyond voltage change, particularly in cells where P2X2 activity contributes to neuronal communication or sensory responses.
The receptor forms a pore from three receptor subunits, so channel opening depends on coordinated behavior within a trimeric structure. Its extracellular ATP-binding regions and membrane-spanning pore connect signal detection with ion conduction. This organization helps explain how molecular events outside the cell can rapidly produce electrical effects across the membrane.
P2X2 receptor activity contributes to synaptic transmission, sensory signaling, and regulation of neuronal excitability. These roles reflect the receptor’s ability to convert extracellular ATP into changes in membrane voltage and intracellular ion composition. Studying these functions helps connect purinergic signaling with communication between neurons and with the way cells respond to sensory inputs.
Electrophysiology examines the electrical consequences of receptor activation, including the depolarization produced when the channel opens and ions cross the membrane. This approach can connect ATP-dependent receptor activity with changes in cellular excitability. In studies of nervous or sensory tissues, those measurements help assess how P2X2 signaling contributes to communication and responsiveness.
Molecular biology and pharmacological approaches complement electrical measurements by examining the receptor and testing how its activity relates to cellular signaling. Together, these methods help clarify the mechanisms of purinergic communication and the receptor’s roles in normal physiology. They also support investigation of how altered P2X2-related signaling may influence neurological and sensory disorders.