P2X1 receptor mobility and trafficking; regulation by receptor insertion and activation
Related Experiment Video
Updated: Jun 14, 2026

Proteomics to Identify Proteins Interacting with P2X2 Ligand-Gated Cation Channels
Published on: May 18, 2009
Ulyana Lalo1, Rebecca C Allsopp, Martyn P Mahaut-Smith
1Department of Cell Physiology & Pharmacology, Henry Wellcome Building, University of Leicester, Leicester, UK.
Abstract:
P2X1 receptors for ATP contribute to signalling in a variety of cell types and following stimulation undergo rapid desensitisation (within 1 s), and require approximately 5 min to recover. In HEK293 cells P2X1 receptors C-terminally tagged with enhanced green fluorescent protein (P2X1-eGFP) were predominantly expressed at the cell surface. Following > 90% photo-bleaching of P2X1-eGFP within a 6 microm(2) circle at the cell surface fluorescence recovery after photo-bleaching (FRAP) was fit with a time constant of approximately 60 s and recovered to approximately 75% of pre-bleach levels. Following activation of the P2X1 receptor with alpha,beta-methylene ATP the associated calcium influx doubled the FRAP recovery rate. The protein synthesis inhibitor cycloheximide had only a small effect on repeated FRAP and indicated a limited contribution of new P2X1 receptors to the FRAP. Inhibition of trafficking with brefeldin A reduced recovery and this effect could be reversed following receptor activation. In contrast, the dynamin inhibitor dynasore had no effect on FRAP under unstimulated conditions but reduced the level of recovery following agonist stimulation. In functional studies both brefeldin A and dynasore increased the recovery time from desensitisation. Taken together these studies demonstrate for the first time an important role of receptor recycling on P2X1 receptor responsiveness.
Insights
P2X1 receptors rapidly desensitize but recover via recycling. Calcium influx accelerates recovery, while protein synthesis plays a minor role. Receptor recycling is crucial for P2X1 receptor responsiveness.
Area of Science:
- Cell biology
- Neuroscience
- Biochemistry
Background:
- P2X1 receptors mediate ATP signaling and desensitize rapidly.
- Understanding P2X1 receptor recovery mechanisms is vital for cellular signaling research.
Purpose of the Study:
- To investigate the role of receptor recycling in P2X1 receptor recovery from desensitization.
- To elucidate the mechanisms influencing P2X1 receptor responsiveness.
Main Methods:
- Utilized fluorescence recovery after photobleaching (FRAP) in HEK293 cells expressing P2X1-eGFP.
- Applied pharmacological inhibitors (cycloheximide, brefeldin A, dynasore) to assess protein synthesis and trafficking.
- Measured functional recovery from desensitization.
Main Results:
- P2X1-eGFP FRAP recovery occurred with a time constant of ~60 s, reaching ~75% of pre-bleach levels.
- Calcium influx doubled FRAP recovery rate; cycloheximide had minimal impact.
- Brefeldin A reduced FRAP recovery, reversible upon activation, while dynasore affected recovery post-stimulation.
- Both inhibitors prolonged functional recovery time from desensitization.
Conclusions:
- Receptor recycling significantly contributes to P2X1 receptor recovery and responsiveness.
- Calcium influx enhances receptor recycling dynamics.
- Trafficking pathways, particularly dynamin-dependent endocytosis, are involved in agonist-stimulated recovery.
Related Concept Videos
Regulation of Nuclear Protein Sorting
Receptor-mediated Endocytosis
Receptor-mediated Endocytosis
Clathrin-Mediated Endocytosis of LDL
One well-characterized example of receptor-mediated endocytosis is the...
Receptor-Mediated Endocytosis
Clathrin-Mediated Endocytosis of LDL
One well-characterized example of receptor-mediated endocytosis is the...
GPCR Desensitization
Insertion of Multi-pass Transmembrane Proteins in the RER
The multipass transmembrane proteins are the type IV integral membrane proteins with multiple topogenic sequences determining their spatial arrangement in the ER membrane. Nearly all multipass proteins lack a cleavable signal sequence and use...

