Two open states of P2X receptor channels
Apstrakt
The occupancy of the orthosteric ligand binding sites of P2X receptor (P2XR) channels causes the rapid opening of a small cation-permeable pore, followed by a gradual dilation that renders the pore permeable to large organic cations. Electrophysiologically, this phenomenon was shown using whole-cell current recording on P2X2R-, P2X2/X5R-, P2X4R- and P2X7R-expressing cells that were bathed in N-methyl-D-glucamine (NMDG(+))-containing buffers in the presence and/or absence of small monovalent and divalent cations. The pore dilation of P2X4R and P2X7R caused a secondary current growth, whereas that of P2X2R showed a sustained kinetic coupling of dilation and desensitization, leading to receptor channel closure. The pore size of the P2X7R open and dilated states was estimated to be approximately 0.85 nm and greater than 1 nm, respectively. The P2XR pore dilation was also observed in intact cells by measurement of fluorescent dye uptake/release, application of polyethylene glycols of differ...ent sizes, and atomic force microscopy. However, pore dilation was not observed at the single channel level. Structural data describing the dilated state are not available, and the relevance of orthosteric and allosteric ligand interactions to pore dilation was not studied.
Ključne reči:
YO-PRO-1 / purinergic receptor channels / pore opening / pore dilation / NMDG / gating / ATPIzvor:
Frontiers in Cellular Neuroscience, 2013, 7Izdavač:
- Frontiers Media Sa, Lausanne
Finansiranje / projekti:
- Intramural Research Program of the National Institute of Child Health and Human Development
- EUNICE KENNEDY SHRIVER NATIONAL INSTITUTE OF CHILD HEALTH & HUMAN DEVELOPMENT [ZIAHD000195] Funding Source: NIH RePORTER
DOI: 10.3389/fncel.2013.00215
ISSN: 1662-5102
WoS: 000327850200001
Scopus: 2-s2.0-84888189345
Institucija/grupa
Institut za molekularnu genetiku i genetičko inženjerstvoTY - JOUR AU - Rokić, Miloš AU - Stojilković, Stanko S. PY - 2013 UR - https://imagine.imgge.bg.ac.rs/handle/123456789/700 AB - The occupancy of the orthosteric ligand binding sites of P2X receptor (P2XR) channels causes the rapid opening of a small cation-permeable pore, followed by a gradual dilation that renders the pore permeable to large organic cations. Electrophysiologically, this phenomenon was shown using whole-cell current recording on P2X2R-, P2X2/X5R-, P2X4R- and P2X7R-expressing cells that were bathed in N-methyl-D-glucamine (NMDG(+))-containing buffers in the presence and/or absence of small monovalent and divalent cations. The pore dilation of P2X4R and P2X7R caused a secondary current growth, whereas that of P2X2R showed a sustained kinetic coupling of dilation and desensitization, leading to receptor channel closure. The pore size of the P2X7R open and dilated states was estimated to be approximately 0.85 nm and greater than 1 nm, respectively. The P2XR pore dilation was also observed in intact cells by measurement of fluorescent dye uptake/release, application of polyethylene glycols of different sizes, and atomic force microscopy. However, pore dilation was not observed at the single channel level. Structural data describing the dilated state are not available, and the relevance of orthosteric and allosteric ligand interactions to pore dilation was not studied. PB - Frontiers Media Sa, Lausanne T2 - Frontiers in Cellular Neuroscience T1 - Two open states of P2X receptor channels VL - 7 DO - 10.3389/fncel.2013.00215 ER -
@article{ author = "Rokić, Miloš and Stojilković, Stanko S.", year = "2013", abstract = "The occupancy of the orthosteric ligand binding sites of P2X receptor (P2XR) channels causes the rapid opening of a small cation-permeable pore, followed by a gradual dilation that renders the pore permeable to large organic cations. Electrophysiologically, this phenomenon was shown using whole-cell current recording on P2X2R-, P2X2/X5R-, P2X4R- and P2X7R-expressing cells that were bathed in N-methyl-D-glucamine (NMDG(+))-containing buffers in the presence and/or absence of small monovalent and divalent cations. The pore dilation of P2X4R and P2X7R caused a secondary current growth, whereas that of P2X2R showed a sustained kinetic coupling of dilation and desensitization, leading to receptor channel closure. The pore size of the P2X7R open and dilated states was estimated to be approximately 0.85 nm and greater than 1 nm, respectively. The P2XR pore dilation was also observed in intact cells by measurement of fluorescent dye uptake/release, application of polyethylene glycols of different sizes, and atomic force microscopy. However, pore dilation was not observed at the single channel level. Structural data describing the dilated state are not available, and the relevance of orthosteric and allosteric ligand interactions to pore dilation was not studied.", publisher = "Frontiers Media Sa, Lausanne", journal = "Frontiers in Cellular Neuroscience", title = "Two open states of P2X receptor channels", volume = "7", doi = "10.3389/fncel.2013.00215" }
Rokić, M.,& Stojilković, S. S.. (2013). Two open states of P2X receptor channels. in Frontiers in Cellular Neuroscience Frontiers Media Sa, Lausanne., 7. https://doi.org/10.3389/fncel.2013.00215
Rokić M, Stojilković SS. Two open states of P2X receptor channels. in Frontiers in Cellular Neuroscience. 2013;7. doi:10.3389/fncel.2013.00215 .
Rokić, Miloš, Stojilković, Stanko S., "Two open states of P2X receptor channels" in Frontiers in Cellular Neuroscience, 7 (2013), https://doi.org/10.3389/fncel.2013.00215 . .