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Tullett, Kirsteen M; Tan, Peck Szee; Park, Hae-Young; Schittenhelm, Ralf B; Michael, Nicole; Li, Rong; Policheni, Antonia N; Gruber, Emily; Huang, Cheng; Fulcher, Alex J; Danne, Jillian C; Czabotar, Peter E; Wakim, Linda M; Mintern, Justine D; Ramm, Georg; Radford, Kristen J; Caminschi, Irina; O'Keeffe, Meredith; Villadangos, Jose A; Wright, Mark D; Blewitt, Marnie E; Heath, William R; Shortman, Ken; Purcell, Anthony W; Nicola, Nicos A; Zhang, Jian-Guo; Lahoud, Mireille H
eLife, 12/2020, Letnik: 9Journal Article
The dendritic cell receptor Clec9A facilitates processing of dead cell-derived antigens for cross-presentation and the induction of effective CD8 T cell immune responses. Here, we show that this process is regulated by E3 ubiquitin ligase RNF41 and define a new ubiquitin-mediated mechanism for regulation of Clec9A, reflecting the unique properties of Clec9A as a receptor specialized for delivery of antigens for cross-presentation. We reveal RNF41 is a negative regulator of Clec9A and the cross-presentation of dead cell-derived antigens by mouse dendritic cells. Intriguingly, RNF41 regulates the downstream fate of Clec9A by directly binding and ubiquitinating the extracellular domains of Clec9A. At steady-state, RNF41 ubiquitination of Clec9A facilitates interactions with ER-associated proteins and degradation machinery to control Clec9A levels. However, Clec9A interactions are altered following dead cell uptake to favor antigen presentation. These findings provide important insights into antigen cross-presentation and have implications for development of approaches to modulate immune responses.
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in: SICRIS
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