| First Author | Paulsson K | Year | 2003 |
| Journal | Biochim Biophys Acta | Volume | 1641 |
| Issue | 1 | Pages | 1-12 |
| PubMed ID | 12788224 | Mgi Jnum | J:341409 |
| Mgi Id | MGI:7539455 | Doi | 10.1016/s0167-4889(03)00048-x |
| Citation | Paulsson K, et al. (2003) Chaperones and folding of MHC class I molecules in the endoplasmic reticulum. Biochim Biophys Acta 1641(1):1-12 |
| abstractText | In this review we discuss the influence of chaperones on the general phenomena of folding as well as on the specific folding of an individual protein, MHC class I. MHC class I maturation is a highly sophisticated process in which the folding machinery of the endoplasmic reticulum (ER) is heavily involved. Understanding the MHC class I maturation per se is important since peptides loaded onto MHC class I molecules are the base for antigen presentation generating immune responses against virus, intracellular bacteria as well as tumours. This review discusses the early stages of MHC class I maturation regarding BiP and calnexin association, and differences in MHC class I heavy chain (HC) interaction with calnexin and calreticulin are highlighted. Late stage MHC class I maturation with focus on the dedicated chaperone tapasin is also discussed. |
