Skip to main content

MHC-II Ubiquitination

  • Protocol
  • First Online:
Antigen Processing

Part of the book series: Methods in Molecular Biology™ ((MIMB,volume 960))

Abstract

Ubiquitinated protein detection is often troublesome since in most cases this modification reduces the half-life of targeted proteins, inducing their degradation. Furthermore, ubiquitination is reversible thanks to the action of highly specific deubiquitinases present in all eukaryotic cells. MHC molecules ubiquitination has been demonstrated to be a key event in the regulation of the potent immunostimulatory properties of activated human dendritic cells.

This is a preview of subscription content, log in via an institution to check access.

Access this chapter

Protocol
USD 49.95
Price excludes VAT (USA)
  • Available as PDF
  • Read on any device
  • Instant download
  • Own it forever
eBook
USD 139.00
Price excludes VAT (USA)
  • Available as EPUB and PDF
  • Read on any device
  • Instant download
  • Own it forever
Softcover Book
USD 179.00
Price excludes VAT (USA)
  • Compact, lightweight edition
  • Dispatched in 3 to 5 business days
  • Free shipping worldwide - see info
Hardcover Book
USD 219.99
Price excludes VAT (USA)
  • Durable hardcover edition
  • Dispatched in 3 to 5 business days
  • Free shipping worldwide - see info

Tax calculation will be finalised at checkout

Purchases are for personal use only

Institutional subscriptions

References

  1. Pierre P et al (1997) Developmental regulation of MHC class II transport in mouse dendritic cells. Nature 388(6644):787–792

    Article  CAS  PubMed  Google Scholar 

  2. de Gassart A et al (2008) MHC class II stabilization at the surface of human dendritic cells is the result of maturation-dependent MARCH1 down-regulation. Proc Natl Acad Sci 105(9):3491–3496

    Article  PubMed  PubMed Central  Google Scholar 

  3. Shin J-S et al (2006) Surface expression of MHC class II in dendritic cells is controlled by regulated ubiquitination. Nature 444(7115):115–118

    Article  CAS  PubMed  Google Scholar 

  4. van Niel G et al (2006) Dendritic cells regulate exposure of MHC class II at their plasma membrane by oligoubiquitination. Immunity 25(6):885–894

    Article  PubMed  Google Scholar 

  5. Komander D (2009) The emerging complexity of protein ubiquitination. Biochem Soc Trans 37(Pt 5):937–953

    Article  CAS  PubMed  Google Scholar 

  6. Baravalle G et al (2011) Ubiquitination of CD86 is a key mechanism in regulating antigen presentation by dendritic cells. J Immunol 187(6):2966–2973

    Article  CAS  PubMed  PubMed Central  Google Scholar 

  7. Bartee E et al (2004) Downregulation of major histocompatibility complex class I by human ubiquitin ligases related to viral immune evasion proteins. J Virol 78(3):1109–1120

    Article  CAS  PubMed  PubMed Central  Google Scholar 

  8. Goto E et al (2003) c-MIR, a human E3 ubiquitin ligase, is a functional homolog of herpesvirus proteins MIR1 and MIR2 and has similar activity. J Biol Chem 278(17):14657–14668

    Article  CAS  PubMed  Google Scholar 

  9. Ishido S et al (2009) E3 ubiquitin ligases for MHC molecules. Curr Opin Immunol 21(1):78–83

    Article  CAS  PubMed  Google Scholar 

  10. Toyomoto M et al (2011) Anti-arthritic effect of E3 ubiquitin ligase, c-MIR, expression in the joints. Int Immunol 23(3):177–183

    Article  CAS  PubMed  Google Scholar 

  11. Bania J et al (2003) Human cathepsin S, but not cathepsin L, degrades efficiently MHC class II-associated invariant chain in nonprofessional APCs. Proc Natl Acad Sci U S A 100(11):6664–6669

    Article  CAS  PubMed  PubMed Central  Google Scholar 

  12. Roche PA et al (1990) Invariant chain association with HLA-DR molecules inhibits immunogenic peptide binding. Nature 345(6276):615–618

    Article  CAS  PubMed  Google Scholar 

  13. Radka SF et al (1984) Analysis of monoclonal antibodies reactive with human class II beta chains by two-dimensional electrophoresis and Western blotting. Hum Immunol 10(3):177–186

    Article  CAS  PubMed  Google Scholar 

Download references

Author information

Authors and Affiliations

Authors

Corresponding author

Correspondence to Evelina Gatti .

Editor information

Editors and Affiliations

Rights and permissions

Reprints and permissions

Copyright information

© 2013 Springer Science+Business Media, LLC

About this protocol

Cite this protocol

De Gassart, A., De Angelis Rigotti, F., Gatti, E. (2013). MHC-II Ubiquitination. In: van Endert, P. (eds) Antigen Processing. Methods in Molecular Biology™, vol 960. Humana Press, Totowa, NJ. https://doi.org/10.1007/978-1-62703-218-6_38

Download citation

  • DOI: https://doi.org/10.1007/978-1-62703-218-6_38

  • Published:

  • Publisher Name: Humana Press, Totowa, NJ

  • Print ISBN: 978-1-62703-217-9

  • Online ISBN: 978-1-62703-218-6

  • eBook Packages: Springer Protocols

Publish with us

Policies and ethics