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Nucleotide-Induced Membrane-Proximal Proteolysis Controls the Substrate Specificity of T Cell Ecto-ADP-Ribosyltransferase ARTC2.2

Standard

Nucleotide-Induced Membrane-Proximal Proteolysis Controls the Substrate Specificity of T Cell Ecto-ADP-Ribosyltransferase ARTC2.2. / Menzel, Stephan; Rissiek, Björn; Bannas, Peter; Jakoby, Thomas; Miksiewicz, Maria; Schwarz, Nicole; Nissen, Marion; Haag, Friedrich; Tholey, Andreas; Nolte, Friedrich.

in: J IMMUNOL, Jahrgang 195, Nr. 5, 01.09.2015, S. 2057-2066.

Publikationen: SCORING: Beitrag in Fachzeitschrift/Zeitung › SCORING: Zeitschriftenaufsatz › Forschung › Begutachtung

Harvard

Menzel, S, Rissiek, B, Bannas, P, Jakoby, T, Miksiewicz, M, Schwarz, N, Nissen, M, Haag, F, Tholey, A & Nolte, F 2015, 'Nucleotide-Induced Membrane-Proximal Proteolysis Controls the Substrate Specificity of T Cell Ecto-ADP-Ribosyltransferase ARTC2.2', J IMMUNOL, Jg. 195, Nr. 5, S. 2057-2066. https://doi.org/10.4049/jimmunol.1401677

APA

Menzel, S., Rissiek, B., Bannas, P., Jakoby, T., Miksiewicz, M., Schwarz, N., Nissen, M., Haag, F., Tholey, A., & Nolte, F. (2015). Nucleotide-Induced Membrane-Proximal Proteolysis Controls the Substrate Specificity of T Cell Ecto-ADP-Ribosyltransferase ARTC2.2. J IMMUNOL, 195(5), 2057-2066. https://doi.org/10.4049/jimmunol.1401677

Vancouver

Menzel S, Rissiek B, Bannas P, Jakoby T, Miksiewicz M, Schwarz N et al. Nucleotide-Induced Membrane-Proximal Proteolysis Controls the Substrate Specificity of T Cell Ecto-ADP-Ribosyltransferase ARTC2.2. J IMMUNOL. 2015 Sep 1;195(5):2057-2066. https://doi.org/10.4049/jimmunol.1401677

Bibtex

@article{2a6f16dee69c4ac597cd68787ef71efc,
title = "Nucleotide-Induced Membrane-Proximal Proteolysis Controls the Substrate Specificity of T Cell Ecto-ADP-Ribosyltransferase ARTC2.2",
abstract = "ARTC2.2 is a toxin-related, GPI-anchored ADP-ribosyltransferase expressed by murine T cells. In response to NAD(+) released from damaged cells during inflammation, ARTC2.2 ADP-ribosylates and thereby gates the P2X7 ion channel. This induces ectodomain shedding of metalloprotease-sensitive cell surface proteins. In this study, we show that ARTC2.2 itself is a target for P2X7-triggered ectodomain shedding. We identify the metalloprotease cleavage site 3 aa upstream of the predicted GPI anchor attachment site of ARTC2.2. Intravenous injection of NAD(+) increased the level of enzymatically active ARTC2.2 in serum, indicating that this mechanism is operative also under inflammatory conditions in vivo. Radio-ADP-ribosylation assays reveal that shedding refocuses the target specificity of ARTC2.2 from membrane proteins to secretory proteins. Our results uncover nucleotide-induced membrane-proximal proteolysis as a regulatory mechanism to control the substrate specificity of ARTC2.2.",
author = "Stephan Menzel and Bj{\"o}rn Rissiek and Peter Bannas and Thomas Jakoby and Maria Miksiewicz and Nicole Schwarz and Marion Nissen and Friedrich Haag and Andreas Tholey and Friedrich Nolte",
note = "Copyright {\textcopyright} 2015 by The American Association of Immunologists, Inc.",
year = "2015",
month = sep,
day = "1",
doi = "10.4049/jimmunol.1401677",
language = "English",
volume = "195",
pages = "2057--2066",
journal = "J IMMUNOL",
issn = "0022-1767",
publisher = "American Association of Immunologists",
number = "5",

}

RIS

TY - JOUR

T1 - Nucleotide-Induced Membrane-Proximal Proteolysis Controls the Substrate Specificity of T Cell Ecto-ADP-Ribosyltransferase ARTC2.2

AU - Menzel, Stephan

AU - Rissiek, Björn

AU - Bannas, Peter

AU - Jakoby, Thomas

AU - Miksiewicz, Maria

AU - Schwarz, Nicole

AU - Nissen, Marion

AU - Haag, Friedrich

AU - Tholey, Andreas

AU - Nolte, Friedrich

N1 - Copyright © 2015 by The American Association of Immunologists, Inc.

PY - 2015/9/1

Y1 - 2015/9/1

N2 - ARTC2.2 is a toxin-related, GPI-anchored ADP-ribosyltransferase expressed by murine T cells. In response to NAD(+) released from damaged cells during inflammation, ARTC2.2 ADP-ribosylates and thereby gates the P2X7 ion channel. This induces ectodomain shedding of metalloprotease-sensitive cell surface proteins. In this study, we show that ARTC2.2 itself is a target for P2X7-triggered ectodomain shedding. We identify the metalloprotease cleavage site 3 aa upstream of the predicted GPI anchor attachment site of ARTC2.2. Intravenous injection of NAD(+) increased the level of enzymatically active ARTC2.2 in serum, indicating that this mechanism is operative also under inflammatory conditions in vivo. Radio-ADP-ribosylation assays reveal that shedding refocuses the target specificity of ARTC2.2 from membrane proteins to secretory proteins. Our results uncover nucleotide-induced membrane-proximal proteolysis as a regulatory mechanism to control the substrate specificity of ARTC2.2.

AB - ARTC2.2 is a toxin-related, GPI-anchored ADP-ribosyltransferase expressed by murine T cells. In response to NAD(+) released from damaged cells during inflammation, ARTC2.2 ADP-ribosylates and thereby gates the P2X7 ion channel. This induces ectodomain shedding of metalloprotease-sensitive cell surface proteins. In this study, we show that ARTC2.2 itself is a target for P2X7-triggered ectodomain shedding. We identify the metalloprotease cleavage site 3 aa upstream of the predicted GPI anchor attachment site of ARTC2.2. Intravenous injection of NAD(+) increased the level of enzymatically active ARTC2.2 in serum, indicating that this mechanism is operative also under inflammatory conditions in vivo. Radio-ADP-ribosylation assays reveal that shedding refocuses the target specificity of ARTC2.2 from membrane proteins to secretory proteins. Our results uncover nucleotide-induced membrane-proximal proteolysis as a regulatory mechanism to control the substrate specificity of ARTC2.2.

U2 - 10.4049/jimmunol.1401677

DO - 10.4049/jimmunol.1401677

M3 - SCORING: Journal article

C2 - 26209623

VL - 195

SP - 2057

EP - 2066

JO - J IMMUNOL

JF - J IMMUNOL

SN - 0022-1767

IS - 5

ER -