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Deubiquitinating Enzyme UCH-L1 Promotes Dendritic Cell Antigen Cross-Presentation by Favoring Recycling of MHC Class I Molecules

Standard

Deubiquitinating Enzyme UCH-L1 Promotes Dendritic Cell Antigen Cross-Presentation by Favoring Recycling of MHC Class I Molecules. / Reinicke, Anna T; Raczkowski, Friederike; Mühlig, Malte; Schmucker, Pina; Lischke, Timo; Reichelt, Julia; Schneider, Enja; Zielinski, Stephanie; Sachs, Marlies; Jurack, Elisabeth; Tolosa, Eva; Kurts, Christian; Mittrücker, Hans-Willi; Meyer-Schwesinger, Catherine.

in: J IMMUNOL, Jahrgang 203, Nr. 7, 01.10.2019, S. 1730-1742.

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

Harvard

Reinicke, AT, Raczkowski, F, Mühlig, M, Schmucker, P, Lischke, T, Reichelt, J, Schneider, E, Zielinski, S, Sachs, M, Jurack, E, Tolosa, E, Kurts, C, Mittrücker, H-W & Meyer-Schwesinger, C 2019, 'Deubiquitinating Enzyme UCH-L1 Promotes Dendritic Cell Antigen Cross-Presentation by Favoring Recycling of MHC Class I Molecules', J IMMUNOL, Jg. 203, Nr. 7, S. 1730-1742. https://doi.org/10.4049/jimmunol.1801133

APA

Reinicke, A. T., Raczkowski, F., Mühlig, M., Schmucker, P., Lischke, T., Reichelt, J., Schneider, E., Zielinski, S., Sachs, M., Jurack, E., Tolosa, E., Kurts, C., Mittrücker, H-W., & Meyer-Schwesinger, C. (2019). Deubiquitinating Enzyme UCH-L1 Promotes Dendritic Cell Antigen Cross-Presentation by Favoring Recycling of MHC Class I Molecules. J IMMUNOL, 203(7), 1730-1742. https://doi.org/10.4049/jimmunol.1801133

Vancouver

Reinicke AT, Raczkowski F, Mühlig M, Schmucker P, Lischke T, Reichelt J et al. Deubiquitinating Enzyme UCH-L1 Promotes Dendritic Cell Antigen Cross-Presentation by Favoring Recycling of MHC Class I Molecules. J IMMUNOL. 2019 Okt 1;203(7):1730-1742. https://doi.org/10.4049/jimmunol.1801133

Bibtex

@article{f4e8d930f71f40c792365e70b3ddc239,
title = "Deubiquitinating Enzyme UCH-L1 Promotes Dendritic Cell Antigen Cross-Presentation by Favoring Recycling of MHC Class I Molecules",
abstract = "The deubiquitinating enzyme ubiquitin C-terminal hydrolase-L1 (UCH-L1) is required for the maintenance of axonal integrity in neurons and is thought to regulate the intracellular pool of ubiquitin in the brain. In this study, we show that UCH-L1 has an immunological function in dendritic cell (DC) Ag cross-presentation. UCH-L1 is expressed in mouse kidney, spleen, and bone marrow-derived DCs, and its expression and activity are regulated by the immune stimuli LPS and IFN-γ. UCH-L1-deficient mice have significantly reduced ability to cross-prime CD8 T cells in vivo and in vitro because of a reduced ability of DCs to generate MHC class I (MHC I) peptide complexes for cross-presented Ags. Mechanistically, Ag uptake by phagocytosis and receptor-mediated endocytosis as well as phagosome maturation are unaffected by loss of UCH-L1 in DCs. Rather, MHC I recycling is reduced by loss of UCH-L1, which affects the colocalization of intracellular MHC I with late endosomal/lysosomal compartments necessary for cross-presentation of Ag. These results demonstrate a hitherto unrecognized role of the deubiquitinating enzyme UCH-L1 in DC Ag processing.",
author = "Reinicke, {Anna T} and Friederike Raczkowski and Malte M{\"u}hlig and Pina Schmucker and Timo Lischke and Julia Reichelt and Enja Schneider and Stephanie Zielinski and Marlies Sachs and Elisabeth Jurack and Eva Tolosa and Christian Kurts and Hans-Willi Mittr{\"u}cker and Catherine Meyer-Schwesinger",
note = "Copyright {\textcopyright} 2019 by The American Association of Immunologists, Inc.",
year = "2019",
month = oct,
day = "1",
doi = "10.4049/jimmunol.1801133",
language = "English",
volume = "203",
pages = "1730--1742",
journal = "J IMMUNOL",
issn = "0022-1767",
publisher = "American Association of Immunologists",
number = "7",

}

RIS

TY - JOUR

T1 - Deubiquitinating Enzyme UCH-L1 Promotes Dendritic Cell Antigen Cross-Presentation by Favoring Recycling of MHC Class I Molecules

AU - Reinicke, Anna T

AU - Raczkowski, Friederike

AU - Mühlig, Malte

AU - Schmucker, Pina

AU - Lischke, Timo

AU - Reichelt, Julia

AU - Schneider, Enja

AU - Zielinski, Stephanie

AU - Sachs, Marlies

AU - Jurack, Elisabeth

AU - Tolosa, Eva

AU - Kurts, Christian

AU - Mittrücker, Hans-Willi

AU - Meyer-Schwesinger, Catherine

N1 - Copyright © 2019 by The American Association of Immunologists, Inc.

PY - 2019/10/1

Y1 - 2019/10/1

N2 - The deubiquitinating enzyme ubiquitin C-terminal hydrolase-L1 (UCH-L1) is required for the maintenance of axonal integrity in neurons and is thought to regulate the intracellular pool of ubiquitin in the brain. In this study, we show that UCH-L1 has an immunological function in dendritic cell (DC) Ag cross-presentation. UCH-L1 is expressed in mouse kidney, spleen, and bone marrow-derived DCs, and its expression and activity are regulated by the immune stimuli LPS and IFN-γ. UCH-L1-deficient mice have significantly reduced ability to cross-prime CD8 T cells in vivo and in vitro because of a reduced ability of DCs to generate MHC class I (MHC I) peptide complexes for cross-presented Ags. Mechanistically, Ag uptake by phagocytosis and receptor-mediated endocytosis as well as phagosome maturation are unaffected by loss of UCH-L1 in DCs. Rather, MHC I recycling is reduced by loss of UCH-L1, which affects the colocalization of intracellular MHC I with late endosomal/lysosomal compartments necessary for cross-presentation of Ag. These results demonstrate a hitherto unrecognized role of the deubiquitinating enzyme UCH-L1 in DC Ag processing.

AB - The deubiquitinating enzyme ubiquitin C-terminal hydrolase-L1 (UCH-L1) is required for the maintenance of axonal integrity in neurons and is thought to regulate the intracellular pool of ubiquitin in the brain. In this study, we show that UCH-L1 has an immunological function in dendritic cell (DC) Ag cross-presentation. UCH-L1 is expressed in mouse kidney, spleen, and bone marrow-derived DCs, and its expression and activity are regulated by the immune stimuli LPS and IFN-γ. UCH-L1-deficient mice have significantly reduced ability to cross-prime CD8 T cells in vivo and in vitro because of a reduced ability of DCs to generate MHC class I (MHC I) peptide complexes for cross-presented Ags. Mechanistically, Ag uptake by phagocytosis and receptor-mediated endocytosis as well as phagosome maturation are unaffected by loss of UCH-L1 in DCs. Rather, MHC I recycling is reduced by loss of UCH-L1, which affects the colocalization of intracellular MHC I with late endosomal/lysosomal compartments necessary for cross-presentation of Ag. These results demonstrate a hitherto unrecognized role of the deubiquitinating enzyme UCH-L1 in DC Ag processing.

U2 - 10.4049/jimmunol.1801133

DO - 10.4049/jimmunol.1801133

M3 - SCORING: Journal article

C2 - 31492742

VL - 203

SP - 1730

EP - 1742

JO - J IMMUNOL

JF - J IMMUNOL

SN - 0022-1767

IS - 7

ER -