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Science 6 August 1993: Vol. 261. no. 5122, pp. 769 - 771 DOI: 10.1126/science.8342042
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Articles
Science, Vol 261, Issue 5122, 769-771
Copyright © 1993 by American Association for the Advancement of Science
Selective and ATP-dependent translocation of peptides by the MHC-encoded transporter
JJ Neefjes,
F Momburg,
and
GJ Hammerling
The Netherlands Cancer Institute, Amsterdam.
Major histocompatibility complex (MHC) class I molecules present peptides derived from nuclear and cytosolic proteins to CD8+ T cells. These peptides are translocated into the lumen of the endoplasmic reticulum (ER) to associate with class I molecules. Two MHC-encoded putative transporter proteins, TAP1 and TAP2, are required for efficient assembly of class I molecules and presentation of endogenous peptides. Expression of TAP1 and TAP2 in a mutant cell line resulted in the delivery of an 11-amino acid oligomer model peptide to the ER. Peptide translocation depended on the sequence of the peptide, was adenosine triphosphate (ATP)-dependent, required ATP hydrolysis, and was inhibited in a concentration-dependent manner.
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