Phagosomal signalling of the C-type lectin receptor Dectin-1 is terminated by intramembrane proteolysis.
Journal
Nature communications
ISSN: 2041-1723
Titre abrégé: Nat Commun
Pays: England
ID NLM: 101528555
Informations de publication
Date de publication:
06 04 2022
06 04 2022
Historique:
received:
23
11
2020
accepted:
14
03
2022
entrez:
7
4
2022
pubmed:
8
4
2022
medline:
9
4
2022
Statut:
epublish
Résumé
Sensing of pathogens by pattern recognition receptors (PRR) is critical to initiate protective host defence reactions. However, activation of the immune system has to be carefully titrated to avoid tissue damage necessitating mechanisms to control and terminate PRR signalling. Dectin-1 is a PRR for fungal β-glucans on immune cells that is rapidly internalised after ligand-binding. Here, we demonstrate that pathogen recognition by the Dectin-1a isoform results in the formation of a stable receptor fragment devoid of the ligand binding domain. This fragment persists in phagosomal membranes and contributes to signal transduction which is terminated by the intramembrane proteases Signal Peptide Peptidase-like (SPPL) 2a and 2b. Consequently, immune cells lacking SPPL2b demonstrate increased anti-fungal ROS production, killing capacity and cytokine responses. The identified mechanism allows to uncouple the PRR signalling response from delivery of the pathogen to degradative compartments and identifies intramembrane proteases as part of a regulatory circuit to control anti-fungal immune responses.
Identifiants
pubmed: 35388002
doi: 10.1038/s41467-022-29474-3
pii: 10.1038/s41467-022-29474-3
pmc: PMC8987071
doi:
Substances chimiques
Lectins, C-Type
0
Ligands
0
Receptors, Pattern Recognition
0
dectin 1
0
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
1880Informations de copyright
© 2022. The Author(s).
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