P2X1 receptor currents after disruption of the PKC site and its surroundings by dominant negative mutations in HEK293 cells

Liu, Guo Jun; Brockhausen, Jennifer; Bennett, Maxwell R.

doi:10.1016/s1566-0702(03)00154-1

Cited by 15 publications

(20 citation statements)

References 13 publications

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“…The threonine residue is also part of a conserved consensus sequence for protein kinase C, and there is evidence that both P2X1 and P2X2 receptors are basally phosphorylated (41, 54). Mutation of the threonine residue led to speeding in desensitization for both P2X1 and P2X2 receptors, indicating the importance of this region of the receptor in the regulation of channel behavior (41, 54, 55).…”

Section: Discussionmentioning

confidence: 99%

The Intracellular Amino Terminus Plays a Dominant Role in Desensitization of ATP-gated P2X Receptor Ion Channels

Allsopp

Evans

2011

Journal of Biological Chemistry

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Background: P2X receptors show marked variation in the time-course of responses.Results: Amino-terminal chimeric and mutant P2X1 and -2 receptors had reciprocal effects on desensitization.Conclusion: The intracellular amino terminus plays a dominant role in regulation of the time-course of ATP currents.Significance: The P2X receptor channel pore region formed by the transmembrane segments is regulated by the amino terminus.

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Section: Discussionmentioning

confidence: 99%

The Intracellular Amino Terminus Plays a Dominant Role in Desensitization of ATP-gated P2X Receptor Ion Channels

Allsopp

Evans

2011

Journal of Biological Chemistry

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“…At first, mutation of the N-terminal Thr 18 residue of rP2X2R was found to dramatically affect receptor desensitization, and the addition of the PKC activator phorbol 12-myristate 13-acetate recovers the desensitization profile in chimeric receptors (Boué-Grabot et al, 2000). Mutation of the respective threonine residues resulted in a receptor with either significantly smaller amplitudes or an absence of P2X1R-and P2X3R-gated currents (Liu et al, 2003;Franklin et al, 2007). However, there is no biochemical evidence of direct phosphorylation of P2X2R and at this residue (Franklin et al, 2007;Vial et al, 2004 Brown andYule, 2007).…”

Section: E Roles Of Protein Kinases In Regulation Of P2x Receptor Fumentioning

confidence: 99%

Activation and Regulation of Purinergic P2X Receptor Channels

et al. 2011

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“…The ATP-induced currents of P2X1R and P2X3R are potentiated by PMA, suggesting again the phosphorylation of the TXR/K motif by PKC /139, 177/. In this case, mutation of the respective threonine residues resulted in receptors with either significantly smaller amplitudes or absence of P2X1R and P2X3R-gated currents, respectively /64, 109/. Finally, biochemical experiments discarded that these threonine residues are directly phosphorylated /64, 177/.…”

Section: Modulation Of P2xrs By Endogenous Proteinsmentioning

confidence: 92%

Allosteric modulation of ATP-gated P2X receptor channels

2011

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Seven mammalian purinergic receptor subunits, denoted P2X1 to P2X7, and several spliced forms of these subunits have been cloned. When heterologously expressed, these cDNAs encode ATP-gated non-selective cation channels organized as trimers. All activated receptors produce cell depolarization and promote Ca2+ influx through their pores and indirectly by activating voltage-gated calcium channels. However, the biophysical and pharmacological properties of these receptors differ considerably, and the majority of these subunits are also capable of forming heterotrimers with other members of the P2X receptor family, which confers further different properties. These channels have three ATP binding domains, presumably located between neighboring subunits, and occupancy of at least two binding sites is needed for their activation. In addition to the orthosteric binding sites for ATP, these receptors have additional allosteric sites that modulate the agonist action at receptors, including sites for trace metals, protons, neurosteroids, reactive oxygen species and phosphoinositides. The allosteric regulation of P2X receptors is frequently receptor-specific and could be a useful tool to identify P2X members in native tissues and their roles in signaling. The focus of this review is on common and receptor-specific allosteric modulation of P2X receptors and the molecular base accounting for allosteric binding sites.

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P2X1 receptor currents after disruption of the PKC site and its surroundings by dominant negative mutations in HEK293 cells

Cited by 15 publications

References 13 publications

The Intracellular Amino Terminus Plays a Dominant Role in Desensitization of ATP-gated P2X Receptor Ion Channels

The Intracellular Amino Terminus Plays a Dominant Role in Desensitization of ATP-gated P2X Receptor Ion Channels

Activation and Regulation of Purinergic P2X Receptor Channels

Allosteric modulation of ATP-gated P2X receptor channels

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