![]() Regulation of MHC class I transport by the molecular chaperone, calnexin (p88, IP90). Jackson MR, Cohen-Doyle MF, Peterson PA et al. Enhanced catalysis of ribonuclease B folding by the interaction of calnexin or calreticulin with ERp57. The role of ERp57 in disulfide bond formation during the assembly of major histocompatibility complex class I in a synchronized semipermeabilized cell translation system. Calnexin influences folding of human class I histocompatibility proteins but not their assembly with beta 2-microglobulin. Mechanisms of MHC class I-restricted antigen processing. This process is experimental and the keywords may be updated as the learning algorithm improves. These keywords were added by machine and not by the authors. Studies of a calreticulin-deficient cell line has demonstrated its critical role in the peptide loading of class I molecules. Calreticulin, on the other hand, is involved in the later stages of class I assembly. In addition, assembly of class I HC with β2m is reduced in the absence of calnexin suggesting a direct involvement of calnexin in the assembly of HC with β2m. Recent findings suggest calnexin is important in early stages of class I assembly where it recruits Erp57 to facilitate disulphide bond formation in class I HC and protects class I HC from degradation prior to their assembly with β2m. ![]() Calnexin and calreticulin are two major chaperones involved in the assembly of class I. Assembly of Major Histocompatibility Complex (MHC) class I heavy chain (HC) with β2-microglobulin (β2m) and subsequent acquisition of optimal peptides is necessary for class 1 antigen presentation to cytotoxic T cells (CTLs). ![]()
0 Comments
Leave a Reply. |
Details
AuthorWrite something about yourself. No need to be fancy, just an overview. ArchivesCategories |