Activation of the P2X7 ion channel by soluble and covalently bound ligands.

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Activation of the P2X7 ion channel by soluble and covalently bound ligands. / Schwarz, Nicole; Fliegert, Ralf; Adriouch, Sahil; Seman, Michel; Guse, Andreas H.; Haag, Friedrich; Koch Nolte, Friedrich.

in: PURINERG SIGNAL, Jahrgang 5, Nr. 2, 2, 2009, S. 139-149.

Publikationen: SCORING: Beitrag in Fachzeitschrift/ZeitungSCORING: ZeitschriftenaufsatzForschungBegutachtung

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Schwarz N, Fliegert R, Adriouch S, Seman M, Guse AH, Haag F et al. Activation of the P2X7 ion channel by soluble and covalently bound ligands. PURINERG SIGNAL. 2009;5(2):139-149. 2.

Bibtex

@article{36c1f2d090174c0a89cf438af57f7b24,
title = "Activation of the P2X7 ion channel by soluble and covalently bound ligands.",
abstract = "The homotrimeric P2X7 purinergic receptor has sparked interest because of its capacity to sense adenosine triphosphate (ATP) and nicotinamide adenine dinucleotide (NAD) released from cells and to induce calcium signaling and cell death. Here, we examine the response of arginine mutants of P2X7 to soluble and covalently bound ligands. High concentrations of ecto-ATP gate P2X7 by acting as a soluble ligand and low concentrations of ecto-NAD gate P2X7 following ADP-ribosylation at R125 catalyzed by toxin-related ecto-ADP-ribosyltransferase ART2.2. R125 lies on a prominent cysteine-rich finger at the interface of adjacent receptor subunits, and ADP-ribosylation at this site likely places the common adenine nucleotide moiety into the ligand-binding pocket of P2X7.",
author = "Nicole Schwarz and Ralf Fliegert and Sahil Adriouch and Michel Seman and Guse, {Andreas H.} and Friedrich Haag and {Koch Nolte}, Friedrich",
year = "2009",
language = "Deutsch",
volume = "5",
pages = "139--149",
journal = "PURINERG SIGNAL",
issn = "1573-9538",
publisher = "Springer Netherlands",
number = "2",

}

RIS

TY - JOUR

T1 - Activation of the P2X7 ion channel by soluble and covalently bound ligands.

AU - Schwarz, Nicole

AU - Fliegert, Ralf

AU - Adriouch, Sahil

AU - Seman, Michel

AU - Guse, Andreas H.

AU - Haag, Friedrich

AU - Koch Nolte, Friedrich

PY - 2009

Y1 - 2009

N2 - The homotrimeric P2X7 purinergic receptor has sparked interest because of its capacity to sense adenosine triphosphate (ATP) and nicotinamide adenine dinucleotide (NAD) released from cells and to induce calcium signaling and cell death. Here, we examine the response of arginine mutants of P2X7 to soluble and covalently bound ligands. High concentrations of ecto-ATP gate P2X7 by acting as a soluble ligand and low concentrations of ecto-NAD gate P2X7 following ADP-ribosylation at R125 catalyzed by toxin-related ecto-ADP-ribosyltransferase ART2.2. R125 lies on a prominent cysteine-rich finger at the interface of adjacent receptor subunits, and ADP-ribosylation at this site likely places the common adenine nucleotide moiety into the ligand-binding pocket of P2X7.

AB - The homotrimeric P2X7 purinergic receptor has sparked interest because of its capacity to sense adenosine triphosphate (ATP) and nicotinamide adenine dinucleotide (NAD) released from cells and to induce calcium signaling and cell death. Here, we examine the response of arginine mutants of P2X7 to soluble and covalently bound ligands. High concentrations of ecto-ATP gate P2X7 by acting as a soluble ligand and low concentrations of ecto-NAD gate P2X7 following ADP-ribosylation at R125 catalyzed by toxin-related ecto-ADP-ribosyltransferase ART2.2. R125 lies on a prominent cysteine-rich finger at the interface of adjacent receptor subunits, and ADP-ribosylation at this site likely places the common adenine nucleotide moiety into the ligand-binding pocket of P2X7.

M3 - SCORING: Zeitschriftenaufsatz

VL - 5

SP - 139

EP - 149

JO - PURINERG SIGNAL

JF - PURINERG SIGNAL

SN - 1573-9538

IS - 2

M1 - 2

ER -