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| Content Provider | PubMed Central |
|---|---|
| Author | Simone, Laura C. Wang, Xiaojian Tuli, Amit Solheim, Joyce C. |
| Abstract | Major histocompatibility complex (MHC) class I heavy chain/β2m heterodimers assemble with antigenic peptides via interactions with peptide-loading complex proteins, including tapasin and ERp57. In human cells, a cysteine residue within tapasin (C95) has been shown to form a covalent bond with ERp57. In this study, we focused on the effect of this tapasin amino acid residue in mouse cells expressing the MHC class I molecule H2-Kd. We demonstrated that a large disulfide-bonded complex was present in the mouse cells that included ERp57, tapasin, and Kd. Furthermore, in mouse cells, unlike human cells, we found that tapasin mutated at C95 can participate in a non-covalent complex with ERp57. Comparison of our findings to earlier findings with a human molecule (HLA-B*4402) also revealed that a tapasin C95 mutation has a stronger effect on the maturation and stability of Kd than HLA-B*4402. Overall, our results characterize the influence of this tapasin cysteine residue on the stable surface expression of a mouse MHC class I molecule, and reveal differences in tapasin C95 interactions and effects between mouse and human systems. |
| Related Links | http://dx.doi.org/10.1038/icb.2009.59 |
| Ending Page | 62 |
| Page Count | 6 |
| Starting Page | 57 |
| File Format | |
| ISSN | 08189641 |
| e-ISSN | 14401711 |
| Journal | Immunology and cell biology |
| Issue Number | 1 |
| Volume Number | 88 |
| Language | English |
| Publisher Date | 2010-01-01 |
| Access Restriction | Open |
| Subject Keyword | Immunology Cell Biology Research in Higher Education |
| Content Type | Text |
| Resource Type | Article |
| Subject | Cell Biology Immunology and Allergy Immunology |
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