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Does Cyclic ADP-Ribose (cADPR) Activate the Non-selective Cation Channel TRPM2?

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Does Cyclic ADP-Ribose (cADPR) Activate the Non-selective Cation Channel TRPM2? / Fliegert, Ralf; Riekehr, Winnie M; Guse, Andreas H.

In: FRONT IMMUNOL, Vol. 11, 2018, 2020.

Research output: SCORING: Contribution to journal › SCORING: Review article › Research

Harvard

Fliegert, R, Riekehr, WM & Guse, AH 2020, 'Does Cyclic ADP-Ribose (cADPR) Activate the Non-selective Cation Channel TRPM2?', FRONT IMMUNOL, vol. 11, 2018. https://doi.org/10.3389/fimmu.2020.02018

APA

Fliegert, R., Riekehr, W. M., & Guse, A. H. (2020). Does Cyclic ADP-Ribose (cADPR) Activate the Non-selective Cation Channel TRPM2? FRONT IMMUNOL, 11, [2018]. https://doi.org/10.3389/fimmu.2020.02018

Vancouver

Fliegert R, Riekehr WM, Guse AH. Does Cyclic ADP-Ribose (cADPR) Activate the Non-selective Cation Channel TRPM2? FRONT IMMUNOL. 2020;11. 2018. https://doi.org/10.3389/fimmu.2020.02018

Bibtex

@article{90531139179d48d590f37bf2347f7a7b,
title = "Does Cyclic ADP-Ribose (cADPR) Activate the Non-selective Cation Channel TRPM2?",
abstract = "TRPM2 is a non-selective, Ca2+-permeable cation channel widely expressed in immune cells. It is firmly established that the channel can be activated by intracellular adenosine 5'-diphosphoribose (ADPR). Until recent cryo-EM structures have exhibited an additional nucleotide binding site in the N-terminus of the channel, this activation was thought to occur via binding to a C-terminal domain of the channel that is highly homologous to the ADPR pyrophosphatase NudT9. Over the years it has been controversially discussed whether the Ca2+ mobilizing second messenger cyclic ADP ribose (cADPR) might also directly activate Ca2+ entry via TRPM2. Here we will review the status of this discussion.",
author = "Ralf Fliegert and Riekehr, {Winnie M} and Guse, {Andreas H}",
note = "Copyright {\textcopyright} 2020 Fliegert, Riekehr and Guse.",
year = "2020",
doi = "10.3389/fimmu.2020.02018",
language = "English",
volume = "11",
journal = "FRONT IMMUNOL",
issn = "1664-3224",
publisher = "Lausanne : Frontiers Research Foundation",

}

RIS

TY - JOUR

T1 - Does Cyclic ADP-Ribose (cADPR) Activate the Non-selective Cation Channel TRPM2?

AU - Fliegert, Ralf

AU - Riekehr, Winnie M

AU - Guse, Andreas H

N1 - Copyright © 2020 Fliegert, Riekehr and Guse.

PY - 2020

Y1 - 2020

N2 - TRPM2 is a non-selective, Ca2+-permeable cation channel widely expressed in immune cells. It is firmly established that the channel can be activated by intracellular adenosine 5'-diphosphoribose (ADPR). Until recent cryo-EM structures have exhibited an additional nucleotide binding site in the N-terminus of the channel, this activation was thought to occur via binding to a C-terminal domain of the channel that is highly homologous to the ADPR pyrophosphatase NudT9. Over the years it has been controversially discussed whether the Ca2+ mobilizing second messenger cyclic ADP ribose (cADPR) might also directly activate Ca2+ entry via TRPM2. Here we will review the status of this discussion.

AB - TRPM2 is a non-selective, Ca2+-permeable cation channel widely expressed in immune cells. It is firmly established that the channel can be activated by intracellular adenosine 5'-diphosphoribose (ADPR). Until recent cryo-EM structures have exhibited an additional nucleotide binding site in the N-terminus of the channel, this activation was thought to occur via binding to a C-terminal domain of the channel that is highly homologous to the ADPR pyrophosphatase NudT9. Over the years it has been controversially discussed whether the Ca2+ mobilizing second messenger cyclic ADP ribose (cADPR) might also directly activate Ca2+ entry via TRPM2. Here we will review the status of this discussion.

U2 - 10.3389/fimmu.2020.02018

DO - 10.3389/fimmu.2020.02018

M3 - SCORING: Review article

C2 - 32903769

VL - 11

JO - FRONT IMMUNOL

JF - FRONT IMMUNOL

SN - 1664-3224

M1 - 2018

ER -