Molecular mechanisms of class I major histocompatibility complex antigen processing and presentation

被引:16
|
作者
Yang, Y
Sempe, P
Peterson, PA
机构
[1] The R.W. Johnson Pharmaceutical Research Institute, The Scripps Research Institute, La Jolla, 92037, Calif.
关键词
major histocompatibility complex; proteasomes; transporter associated with antigen processing; interferon; ubiquitination;
D O I
10.1007/BF02918250
中图分类号
R392 [医学免疫学]; Q939.91 [免疫学];
学科分类号
100102 ;
摘要
The presentation of antigenic peptides by class I major histocompatibility complex molecules plays a central role in the cellular immune response, since immune surveillance for detection of viral infections or malignant transformations is achieved by CD8+ T lymphocytes which inspect peptides, derived from intracellular proteins, bind to class I molecules on the surface of most cells. The transporter associated with antigen processing selectively translocates cytoplasmically derived peptides of appropriate sequence and length into the lumen of the endoplasmic reticulum where they associate with newly synthesized class I molecules. The translocated peptides are generated by multicatalytic and multisubunit proteasomes which degrade cytoplasmic proteins in a ATP-ubiquitin-dependent manner. This review discusses our current molecular understanding of class I antigen processing and presentation.
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页码:208 / 233
页数:26
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