Tapasin and other chaperones: models of the MHC class I loading complex
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| 024 | 7 | 0 | |a 10.1515/BC.2004.100 |2 doi |
| 035 | |a (NATIONALLICENCE)gruyter-10.1515/BC.2004.100 | ||
| 245 | 0 | 0 | |a Tapasin and other chaperones: models of the MHC class I loading complex |h [Elektronische Daten] |c [Cynthia Anne Wright, Patrycja Kozik, Martin Zacharias, Sebastian Springer] |
| 520 | 3 | |a MHC (major histocompatibility complex) class I molecules bind intracellular virus-derived peptides in the endoplasmic reticulum (ER) and present them at the cell surface to cytotoxic T lymphocytes. Peptide-free class I molecules at the cell surface, however, could lead to aberrant T cell killing. Therefore, cells ensure that class I molecules bind high-affinity ligand peptides in the ER, and restrict the export of empty class I molecules to the Golgi apparatus. For both of these safeguard mechanisms, the MHC class I loading complex (which consists of the peptide transporter TAP, the chaperones tapasin and calreticulin, and the protein disulfide isomerase ERp57) plays a central role. This article reviews the actions of accessory proteins in the biogenesis of class I molecules, specifically the functions of the loading complex in high-affinity peptide binding and localization of class I molecules, and the known connections between these two regulatory mechanisms. It introduces new models for the mode of action of tapasin, the role of the class I loading complex in peptide editing, and the intracellular localization of class I molecules. | |
| 540 | |a © Walter de Gruyter | ||
| 690 | 7 | |a Biochemistry |2 nationallicence | |
| 690 | 7 | |a Molecular biology |2 nationallicence | |
| 690 | 7 | |a Cellular biology |2 nationallicence | |
| 690 | 7 | |a calreticulin |2 nationallicence | |
| 690 | 7 | |a ERp57 |2 nationallicence | |
| 690 | 7 | |a major histocompatibility complex molecules |2 nationallicence | |
| 690 | 7 | |a peptide binding |2 nationallicence | |
| 690 | 7 | |a TAP |2 nationallicence | |
| 690 | 7 | |a tapasin |2 nationallicence | |
| 700 | 1 | |a Wright |D Cynthia Anne |u Biochemistry and Cell Biology, International University Bremen, D-28759 Bremen, Germany |4 aut | |
| 700 | 1 | |a Kozik |D Patrycja |u Biochemistry and Cell Biology, International University Bremen, D-28759 Bremen, Germany |4 aut | |
| 700 | 1 | |a Zacharias |D Martin |u Bioinformatics and Computational Biology, International University Bremen, D-28759 Bremen, Germany |4 aut | |
| 700 | 1 | |a Springer |D Sebastian |u Biochemistry and Cell Biology, International University Bremen, D-28759 Bremen, Germany |4 aut | |
| 773 | 0 | |t Biological Chemistry |d Walter de Gruyter |g 385/9(2004-09-01), 763-778 |x 1431-6730 |q 385:9<763 |1 2004 |2 385 |o bchm | |
| 856 | 4 | 0 | |u https://doi.org/10.1515/BC.2004.100 |q text/html |z Onlinezugriff via DOI |
| 908 | |D 1 |a research article |2 jats | ||
| 950 | |B NATIONALLICENCE |P 856 |E 40 |u https://doi.org/10.1515/BC.2004.100 |q text/html |z Onlinezugriff via DOI | ||
| 950 | |B NATIONALLICENCE |P 700 |E 1- |a Wright |D Cynthia Anne |u Biochemistry and Cell Biology, International University Bremen, D-28759 Bremen, Germany |4 aut | ||
| 950 | |B NATIONALLICENCE |P 700 |E 1- |a Kozik |D Patrycja |u Biochemistry and Cell Biology, International University Bremen, D-28759 Bremen, Germany |4 aut | ||
| 950 | |B NATIONALLICENCE |P 700 |E 1- |a Zacharias |D Martin |u Bioinformatics and Computational Biology, International University Bremen, D-28759 Bremen, Germany |4 aut | ||
| 950 | |B NATIONALLICENCE |P 700 |E 1- |a Springer |D Sebastian |u Biochemistry and Cell Biology, International University Bremen, D-28759 Bremen, Germany |4 aut | ||
| 950 | |B NATIONALLICENCE |P 773 |E 0- |t Biological Chemistry |d Walter de Gruyter |g 385/9(2004-09-01), 763-778 |x 1431-6730 |q 385:9<763 |1 2004 |2 385 |o bchm | ||
| 900 | 7 | |b CC0 |u http://creativecommons.org/publicdomain/zero/1.0 |2 nationallicence | |
| 898 | |a BK010053 |b XK010053 |c XK010000 | ||
| 949 | |B NATIONALLICENCE |F NATIONALLICENCE |b NL-gruyter | ||