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Ribosylation of the CD8αβ heterodimer permits binding of the nonclassical major histocompatibility molecule, H2-Q10
The CD8αβ heterodimer plays a crucial role in the stabilization between major histocompatibility complex class I molecules (MHC-I) and the T cell receptor (TCR). The interaction between CD8 and MHC-I can be regulated by posttranslational modifications, which are proposed to play an important role in...
Autores principales: | , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
American Society for Biochemistry and Molecular Biology
2021
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8517849/ https://www.ncbi.nlm.nih.gov/pubmed/34478713 http://dx.doi.org/10.1016/j.jbc.2021.101141 |
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author | Goodall, Katharine Jennifer Nguyen, Angela Andrews, Daniel Mark Sullivan, Lucy Catherine |
author_facet | Goodall, Katharine Jennifer Nguyen, Angela Andrews, Daniel Mark Sullivan, Lucy Catherine |
author_sort | Goodall, Katharine Jennifer |
collection | PubMed |
description | The CD8αβ heterodimer plays a crucial role in the stabilization between major histocompatibility complex class I molecules (MHC-I) and the T cell receptor (TCR). The interaction between CD8 and MHC-I can be regulated by posttranslational modifications, which are proposed to play an important role in the development of CD8 T cells. One modification that has been proposed to control CD8 coreceptor function is ribosylation. Utilizing NAD(+), the ecto-enzyme adenosine diphosphate (ADP) ribosyl transferase 2.2 (ART2.2) catalyzes the addition of ADP-ribosyl groups onto arginine residues of CD8α or β chains and alters the interaction between the MHC and TCR complexes. To date, only interactions between modified CD8 and classical MHC-I (MHC-Ia), have been investigated and the interaction with non-classical MHC (MHC-Ib) has not been explored. Here, we show that ADP-ribosylation of CD8 facilitates the binding of the liver-restricted nonclassical MHC, H2-Q10, independent of the associated TCR or presented peptide, and propose that this highly regulated binding imposes an additional inhibitory leash on the activation of CD8-expressing cells in the presence of NAD(+). These findings highlight additional important roles for nonclassical MHC-I in the regulation of immune responses. |
format | Online Article Text |
id | pubmed-8517849 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2021 |
publisher | American Society for Biochemistry and Molecular Biology |
record_format | MEDLINE/PubMed |
spelling | pubmed-85178492021-10-21 Ribosylation of the CD8αβ heterodimer permits binding of the nonclassical major histocompatibility molecule, H2-Q10 Goodall, Katharine Jennifer Nguyen, Angela Andrews, Daniel Mark Sullivan, Lucy Catherine J Biol Chem Research Article The CD8αβ heterodimer plays a crucial role in the stabilization between major histocompatibility complex class I molecules (MHC-I) and the T cell receptor (TCR). The interaction between CD8 and MHC-I can be regulated by posttranslational modifications, which are proposed to play an important role in the development of CD8 T cells. One modification that has been proposed to control CD8 coreceptor function is ribosylation. Utilizing NAD(+), the ecto-enzyme adenosine diphosphate (ADP) ribosyl transferase 2.2 (ART2.2) catalyzes the addition of ADP-ribosyl groups onto arginine residues of CD8α or β chains and alters the interaction between the MHC and TCR complexes. To date, only interactions between modified CD8 and classical MHC-I (MHC-Ia), have been investigated and the interaction with non-classical MHC (MHC-Ib) has not been explored. Here, we show that ADP-ribosylation of CD8 facilitates the binding of the liver-restricted nonclassical MHC, H2-Q10, independent of the associated TCR or presented peptide, and propose that this highly regulated binding imposes an additional inhibitory leash on the activation of CD8-expressing cells in the presence of NAD(+). These findings highlight additional important roles for nonclassical MHC-I in the regulation of immune responses. American Society for Biochemistry and Molecular Biology 2021-08-31 /pmc/articles/PMC8517849/ /pubmed/34478713 http://dx.doi.org/10.1016/j.jbc.2021.101141 Text en © 2021 The Authors https://creativecommons.org/licenses/by-nc-nd/4.0/This is an open access article under the CC BY-NC-ND license (http://creativecommons.org/licenses/by-nc-nd/4.0/). |
spellingShingle | Research Article Goodall, Katharine Jennifer Nguyen, Angela Andrews, Daniel Mark Sullivan, Lucy Catherine Ribosylation of the CD8αβ heterodimer permits binding of the nonclassical major histocompatibility molecule, H2-Q10 |
title | Ribosylation of the CD8αβ heterodimer permits binding of the nonclassical major histocompatibility molecule, H2-Q10 |
title_full | Ribosylation of the CD8αβ heterodimer permits binding of the nonclassical major histocompatibility molecule, H2-Q10 |
title_fullStr | Ribosylation of the CD8αβ heterodimer permits binding of the nonclassical major histocompatibility molecule, H2-Q10 |
title_full_unstemmed | Ribosylation of the CD8αβ heterodimer permits binding of the nonclassical major histocompatibility molecule, H2-Q10 |
title_short | Ribosylation of the CD8αβ heterodimer permits binding of the nonclassical major histocompatibility molecule, H2-Q10 |
title_sort | ribosylation of the cd8αβ heterodimer permits binding of the nonclassical major histocompatibility molecule, h2-q10 |
topic | Research Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8517849/ https://www.ncbi.nlm.nih.gov/pubmed/34478713 http://dx.doi.org/10.1016/j.jbc.2021.101141 |
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