Assembly and antigen-presenting function of MHC class I molecules in cells lacking the ER chaperone calreticulin.
MHC class I molecules expressed in a calreticulin-deficient cell line (K42) assembled with beta 2-microglobulin (beta2-m) normally, but their subsequent loading with optimal peptides was defective. Suboptimally loaded class I molecules were released into the secretory pathway. This occurred despite...
Main Authors: | Gao, B, Adhikari, R, Howarth, M, Nakamura, K, Gold, M, Hill, AB, Knee, R, Michalak, M, Elliott, T |
---|---|
Format: | Journal article |
Language: | English |
Published: |
2002
|
Similar Items
-
The role of calnexin, calreticulin and heavy chain glycosylation in MHC class I assembly
by: Adhikari, R, et al.
Published: (2002) -
The ins and outs of calreticulin: from the ER lumen to the extracellular space.
by: Johnson, S, et al.
Published: (2001) -
Chaperone function in antigen presentation by MHC class I molecules—tapasin in the PLC and TAPBPR beyond
by: David H. Margulies, et al.
Published: (2023-06-01) -
Chaperone-mediated MHC-I peptide exchange in antigen presentation
by: Jiansheng Jiang, et al.
Published: (2024-05-01) -
Calreticulin and the Heart
by: Jody Groenendyk, et al.
Published: (2022-05-01)