Functional regulation of immunoproteasomes and transporter associated with antigen processing.
Immunol Res
; 24(3): 245-72, 2001.
Article
em En
| MEDLINE
| ID: mdl-11817324
ABSTRACT
The central event in the cellular immune response to invading pathogens is the presentation of non-self antigenic peptides by major histocompatibility complex (MHC) class I molecules to cytotoxic T lymphocytes (CTLs). As peptide binding and transport proteins, MHC class I molecules have evolved distinct biochemical and cellular strategies for acquiring antigenic peptides, providing CTLs an extracellular representation of the intracellular antigen content. Whereas efficient generation of MHC class I binding peptides depends on the intracellular, immunoproteasome-mediated proteolysis machinery, translocation of peptides into the lumen of the endoplasmic reticulum requires the endoplasmic reticulum-resident, adenosine 5'-triphosphate (ATP) binding cassette transporter associated with antigen processing (TAP). Here we show, for the first time, that immunoproteasomes, TAP complexes, and MHC class I molecules are physically associated, providing an effective means of transporting MHC class I binding peptides from their sites of generation into the lumen of the endoplasmic reticulum for loading onto MHC class I molecules. In this review, we assess the current understanding of the functional regulation of immunoproteasomes and transporter associated with antigen processing.
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Base de dados:
MEDLINE
Assunto principal:
Cisteína Endopeptidases
/
Apresentação de Antígeno
/
Transportadores de Cassetes de Ligação de ATP
/
Complexos Multienzimáticos
Idioma:
En
Ano de publicação:
2001
Tipo de documento:
Article