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Surface expression of MHC class II in dendritic cells is controlled by regulated ubiquitination

Author

Listed:
  • Jeoung-Sook Shin

    (Yale University School of Medicine)

  • Melanie Ebersold

    (Yale University School of Medicine)

  • Marc Pypaert

    (Yale University School of Medicine)

  • Lelia Delamarre

    (Yale University School of Medicine)

  • Adam Hartley

    (Yale University School of Medicine)

  • Ira Mellman

    (Yale University School of Medicine)

Abstract

Dendritic cells have a unique function in the immune response owing to their ability to stimulate immunologically naive T lymphocytes1. In response to microbial and inflammatory stimuli, dendritic cells enhance their capacity for antigen presentation by a process of terminal differentiation, termed maturation2,3. The conversion of immature to mature dendritic cells is accompanied by a marked cellular reorganization, including the redistribution of major histocompatibility complex class II molecules (MHC II) from late endosomal and lysosomal compartments to the plasma membrane4,5,6,7 and the downregulation of some forms of endocytosis, which has been thought to slow the clearance of MHC II from the surface8,9,10,11. The relative extent to which these or other mechanisms contribute to the regulation of surface MHC II remains unclear, however. Here we find that the MHC II β-chain cytoplasmic tail is ubiquitinated in mouse immature dendritic cells. Although only partly required for the sequestration of MHC II in multivesicular bodies, this modification is essential for endocytosis. Notably, ubiquitination of MHC II ceased upon maturation, resulting in the accumulation of MHC II at the cell surface. Dendritic cells thus exhibit a unique ability to regulate MHC II surface expression by selectively controlling MHC II ubiquitination.

Suggested Citation

  • Jeoung-Sook Shin & Melanie Ebersold & Marc Pypaert & Lelia Delamarre & Adam Hartley & Ira Mellman, 2006. "Surface expression of MHC class II in dendritic cells is controlled by regulated ubiquitination," Nature, Nature, vol. 444(7115), pages 115-118, November.
  • Handle: RePEc:nat:nature:v:444:y:2006:i:7115:d:10.1038_nature05261
    DOI: 10.1038/nature05261
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    Cited by:

    1. Haiyin Liu & Kayla R. Wilson & Ashley M. Firth & Christophe Macri & Patrick Schriek & Annabelle B. Blum & Javiera Villar & Samuel Wormald & Mitch Shambrook & Bangyan Xu & Hui Jing Lim & Hamish E. G. M, 2022. "Ubiquitin-like protein 3 (UBL3) is required for MARCH ubiquitination of major histocompatibility complex class II and CD86," Nature Communications, Nature, vol. 13(1), pages 1-15, December.

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