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Physiological Reviews, Vol. 82, No. 1, January 2002, pp. 187-204; 10.1152/physrev.00025.2001.
Copyright ©2002 by the American Physiological Society
Institut für Physiologische Chemie, Philipps-Universität Marburg, Marburg, Germany
Lankat-Buttgereit, Brigitte and
Robert Tampé.
The Transporter Associated With Antigen Processing: Function
and Implications in Human Diseases. Physiol. Rev. 82: 187-204, 2002.
The adaptive immune systems have
evolved to protect the organism against pathogens encountering the
host. Extracellular occurring viruses or bacteria are mainly bound by
antibodies from the humoral branch of the immune response, whereas
infected or malignant cells are identified and eliminated by the
cellular immune system. To enable the recognition, proteins are cleaved
into peptides in the cytosol and are presented on the cell surface by
class I molecules of the major histocompatibility complex (MHC). The
transport of the antigenic peptides into the lumen of the endoplasmic
reticulum (ER) and loading onto the MHC class I molecules is an
essential process for the presentation to cytotoxic T lymphocytes. The
delivery of these peptides is performed by the transporter associated
with antigen processing (TAP). TAP is a heterodimer of TAP1 and TAP2, each subunit containing transmembrane domains and an ATP-binding motif. Sequence homology analysis revealed that TAP belongs to the
superfamily of ATP-binding cassette transporters. Loss of TAP
function leads to a loss of cell surface expression of MHC class I
molecules. This may be a strategy for tumors and virus-infected cells to escape immune surveillance. Structure and function of the TAP
complex as well as the implications of loss or downregulation of TAP is
the topic of this review.
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