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/Zeitung › SCORING: Zeitschriftenaufsatz › Forschung › Begutachtung
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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 -