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Science 6 August 1993:
Vol. 261. no. 5122, pp. 769 - 771
DOI: 10.1126/science.8342042

Articles

Science, Vol 261, Issue 5122, 769-771
Copyright © 1993 by American Association for the Advancement of Science


articles

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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A. Craiu, T. Akopian, A. Goldberg, and K. L. Rock (1997)
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A. G. Grandea III, T. Spies, M. J. Androlewicz, R. S. Athwal, and D. E. Geraghty (1995)
Science 270, 105-108
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Assembly, Intracellular Localization, and Nucleotide Binding Properties of the Human Peptide Transporters TAP1 and TAP2 Expressed by Recombinant Vaccinia Viruses.
G. Russ, F. Esquivel, J. W. Yewdell, P. Cresswell, T. Spies, and J. R. Bennink (1995)
J. Biol. Chem. 270, 21312-21318
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Requirements for Peptide Binding to the Human Transporter Associated with Antigen Processing Revealed by Peptide Scans and Complex Peptide Libraries.
S. Uebel, T. H. Meyer, W. Kraas, S. Kienle, G. Jung, K.-H. Wiesmller, and R. Tamp (1995)
J. Biol. Chem. 270, 18512-18516
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Presentation without Proteolytic Cleavage of Endogenous Precursors in the MHC Class I Antigen Processing Pathway.
D. Buchholz, P. Scott, and N. Shastri (1995)
J. Biol. Chem. 270, 6515-6522
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