ArticleThe Journal of experimental medicine1997
Potential immunocompetence of proteolytic fragments produced by proteasomes before evolution of the vertebrate immune system.
Article in The Journal of experimental medicine, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed, 83 citations in OpenAlex.
- Cell Clearing Systems Bridging Neuro-Immunity and Synaptic Plasticity.International journal of molecular sciences · 2019Review
- A Sentinel in the Crosstalk Between the Nervous and Immune System: The (Immuno)-Proteasome.Frontiers in immunology · 2019Review
- Structure and Dynamics of Antigenic Peptides in Complex with TAP.Frontiers in immunology · 2017Review
- Computational prediction of cleavage using proteasomal in vitro digestion and MHC I ligand data.Journal of Zhejiang University. Science. B · 2013Article
- Proteasome allostery as a population shift between interchanging conformers.Proceedings of the National Academy of Sciences of the United States of America · 2012Article
- PA28 and the proteasome immunosubunits play a central and independent role in the production of MHC class I-binding peptides in vivo.European journal of immunology · 2011Article
- The ubiquitin-proteasome system.Journal of biosciences · 2006Review
- Bioinformatic analysis of functional differences between the immunoproteasome and the constitutive proteasome.Immunogenetics · 2003Article
- Differential influence on cytotoxic T lymphocyte epitope presentation by controlled expression of either proteasome immunosubunits or PA28.The Journal of experimental medicine · 2000Article
- Efficient generation of a hepatitis B virus cytotoxic T lymphocyte epitope requires the structural features of immunoproteasomes.The Journal of experimental medicine · 2000Article
- Cytotoxic T lymphocyte epitopes of HIV-1 Nef: Generation of multiple definitive major histocompatibility complex class I ligands by proteasomes.The Journal of experimental medicine · 2000Article
- The proteasome activator 11 S REG (PA28) and class I antigen presentation.The Biochemical journal · 2000Review
- Follicle cell proteasome activity and acid extract from the egg vitelline coat prompt the onset of self-sterility in Ciona intestinalis oocytes.Proceedings of the National Academy of Sciences of the United States of America · 1999Article
- Retention of empty MHC class I molecules by tapasin is essential to reconstitute antigen presentation in invertebrate cells.The EMBO journal · 1999Article
- Cleavage motifs of the yeast 20S proteasome beta subunits deduced from digests of enolase 1.Proceedings of the National Academy of Sciences of the United States of America · 1998Article
- The sequence alteration associated with a mutational hotspot in p53 protects cells from lysis by cytotoxic T lymphocytes specific for a flanking peptide epitope.The Journal of experimental medicine · 1998Article
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Authors and funding
11 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
To generate peptides for presentation by major histocompatibility complex (MHC) class I molecules to T lymphocytes, the immune system of vertebrates has recruited the proteasomes, phylogenetically ancient multicatalytic high molecular weight endoproteases. We have previously shown that many of the proteolytic fragments generated by vertebrate proteasomes have structural features in common with peptides eluted from MHC class I molecules, suggesting that many MHC class I ligands are direct products of proteasomal proteolysis. Here, we report that the processing of polypeptides by proteasomes is conserved in evolution, not only among vertebrate species, but including invertebrate eukaryotes such as insects and yeast. Unexpectedly, we found that several high copy ligands of MHC class I molecules, in particular, self-ligands, are major products in digests of source polypeptides by invertebrate proteasomes. Moreover, many major dual cleavage peptides produced by invertebrate proteasomes have the length and the NH2 and COOH termini preferred by MHC class I. Thus, the ability of proteasomes to generate potentially immunocompetent peptides evolved well before the vertebrate immune system. We demonstrate with polypeptide substrates that interferon gamma induction in vivo or addition of recombinant proteasome activator 28alpha in vitro alters proteasomal proteolysis in such a way that the generation of peptides with the structural features of MHC class I ligands is optimized. However, these changes are quantitative and do not confer qualitatively novel characteristics to proteasomal proteolysis. The data suggest that proteasomes may have influenced the evolution of MHC class I molecules.
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