MARCH9‐mediated ubiquitination regulates ...
Document type :
Compte-rendu et recension critique d'ouvrage
DOI :
Title :
MARCH9‐mediated ubiquitination regulates MHC I export from the TGN
Author(s) :
de Angelis Rigotti, Francesca [Auteur]
Centre d'Immunologie de Marseille - Luminy [CIML]
de Gassart, Aude [Auteur]
Centre d'Immunologie de Marseille - Luminy [CIML]
Pforr, Carina [Auteur]
Centre d'Immunologie de Marseille - Luminy [CIML]
Cano, Florencia [Auteur]
N'Guessan, Prudence [Auteur]
Centre d'Immunologie de Marseille - Luminy [CIML]
Combes, Alexis [Auteur]
Centre d'Immunologie de Marseille - Luminy [CIML]
Camossetto, Voahirana [Auteur]
Centre d'Immunologie de Marseille - Luminy [CIML]
Lehner, Paul [Auteur]
Centre Interuniversitaire de Recherche en Education de Lille - ULR 4354 [CIREL]
Gatti, Evelina [Auteur]
Centre d'Immunologie de Marseille - Luminy [CIML]
Pierre, Philippe [Auteur]
Centre d'Immunologie de Marseille - Luminy [CIML]
Rigotti, Angelis [Auteur]
Centre d'Immunologie de Marseille - Luminy [CIML]
Centre d'Immunologie de Marseille - Luminy [CIML]
de Gassart, Aude [Auteur]
Centre d'Immunologie de Marseille - Luminy [CIML]
Pforr, Carina [Auteur]
Centre d'Immunologie de Marseille - Luminy [CIML]
Cano, Florencia [Auteur]
N'Guessan, Prudence [Auteur]
Centre d'Immunologie de Marseille - Luminy [CIML]
Combes, Alexis [Auteur]
Centre d'Immunologie de Marseille - Luminy [CIML]
Camossetto, Voahirana [Auteur]
Centre d'Immunologie de Marseille - Luminy [CIML]
Lehner, Paul [Auteur]
![refId](/themes/Mirage2//images/idref.png)
Centre Interuniversitaire de Recherche en Education de Lille - ULR 4354 [CIREL]
Gatti, Evelina [Auteur]
Centre d'Immunologie de Marseille - Luminy [CIML]
Pierre, Philippe [Auteur]
Centre d'Immunologie de Marseille - Luminy [CIML]
Rigotti, Angelis [Auteur]
Centre d'Immunologie de Marseille - Luminy [CIML]
Journal title :
Immunology and Cell Biology
Pages :
753-764
Publisher :
Nature Publishing Group
Publication date :
2017-10
ISSN :
0818-9641
English keyword(s) :
ubiquitin ligase
HLA
antigen presentation
dendritic cells
HLA
antigen presentation
dendritic cells
HAL domain(s) :
Sciences du Vivant [q-bio]
English abstract : [en]
Given the heterogeneous nature of antigens, MHC-I intracellular transport intersects with multiple degradation pathways for efficient peptide loading and presentation to cytotoxic T cells. MHC-I loading with peptides in ...
Show more >Given the heterogeneous nature of antigens, MHC-I intracellular transport intersects with multiple degradation pathways for efficient peptide loading and presentation to cytotoxic T cells. MHC-I loading with peptides in the endoplasmic reticulum (ER) is a tightly regulated process, while postER intracellular transport is considered to occur by default, leading to peptide-bearing MHC-I delivery to the plasma membrane. We show here that MHC-I traffic is submitted to a previously uncharacterized sorting step at the trans Golgi network (TGN), dependent on the ubiquitination of its cytoplasmic tail lysine residues. MHC-I ubiquitination is mediated by the E3 ligase MARCH9 and allows MHC-I access to syntaxin 6 (Stx6)positive endosomal compartments. We further show that MARCH9 can also target the human MHC I-like lipid antigen presentation molecule CD1a. MARCH9 expression is modulated by microbial patterns exposure in dendritic cells (DC), thus revealing the role of this ubiquitin E3 ligase in coordinating MHC-I access to endosomes and DC activation for efficient antigen cross-presentation.Show less >
Show more >Given the heterogeneous nature of antigens, MHC-I intracellular transport intersects with multiple degradation pathways for efficient peptide loading and presentation to cytotoxic T cells. MHC-I loading with peptides in the endoplasmic reticulum (ER) is a tightly regulated process, while postER intracellular transport is considered to occur by default, leading to peptide-bearing MHC-I delivery to the plasma membrane. We show here that MHC-I traffic is submitted to a previously uncharacterized sorting step at the trans Golgi network (TGN), dependent on the ubiquitination of its cytoplasmic tail lysine residues. MHC-I ubiquitination is mediated by the E3 ligase MARCH9 and allows MHC-I access to syntaxin 6 (Stx6)positive endosomal compartments. We further show that MARCH9 can also target the human MHC I-like lipid antigen presentation molecule CD1a. MARCH9 expression is modulated by microbial patterns exposure in dendritic cells (DC), thus revealing the role of this ubiquitin E3 ligase in coordinating MHC-I access to endosomes and DC activation for efficient antigen cross-presentation.Show less >
Language :
Anglais
Popular science :
Non
ANR Project :
Source :
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