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Science 27 May 1994:
Vol. 264. no. 5163, pp. 1322 - 1326
DOI: 10.1126/science.8191286
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Articles

Science, Vol 264, Issue 5163, 1322-1326
Copyright © 1994 by American Association for the Advancement of Science

articles

Interaction of MHC class I molecules with the transporter associated with antigen processing

WK Suh, MF Cohen-Doyle, K Fruh, K Wang, PA Peterson, and DB Williams

Department of Biochemistry, University of Toronto, Ontario, Canada.

The transporter associated with antigen processing (TAP) delivers cytosolic peptides into the endoplasmic reticulum (ER) where they bind to nascent class 1 histocompatibility molecules. Class 1-peptide complexes are then displayed at the cell surface for recognition by cytotoxic T lymphocytes. Immunoprecipitation of either TAP or class 1 molecules revealed an association between the transporter and diverse class 1 products. TAP bound preferentially to heterodimers of the class 1 heavy chain and beta 2-microglobulin, and the complex subsequently dissociated in parallel with transport of class 1 molecules from the ER to the Golgi apparatus. The TAP-class 1 complexes could also be dissociated in vitro by the addition of class 1-binding peptides. The association of class 1 molecules with TAP likely promotes efficient capture of peptides before their exposure to the lumen of the ER.


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C. J. Luckey, G. M. King, J. A. Marto, S. Venketeswaran, B. F. Maier, V. L. Crotzer, T. A. Colella, J. Shabanowitz, D. F. Hunt, and V. H. Engelhard (1998)
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A Soluble Major Histocompatibility Complex Class I Peptide-binding Platform Undergoes a Conformational Change in Response to Peptide Epitopes.
E. Rigney, M. Kojima, A. Glithero, and T. Elliott (1998)
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Interaction of HLA-E with Peptides and the Peptide Transporter In Vitro: Implications for its Function in Antigen Presentation.
M. Ulbrecht, S. Modrow, R. Srivastava, P. A. Peterson, and E. H. Weiss (1998)
J. Immunol. 160, 4375-4385
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Physical and Functional Association of the Major Histocompatibility Complex Class I Heavy Chain alpha 3 Domain with the Transporter Associated with Antigen Processing.
K. Kulig, D. Nandi, I. Bacik, J. J. Monaco, and S. Vukmanovic (1998)
J. Exp. Med. 187, 865-874
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The Class I Antigen-processing Pathway for the Membrane Protein Tyrosinase Involves Translation in the Endoplasmic Reticulum and Processing in the Cytosol.
C. A. Mosse, L. Meadows, C. J. Luckey, D. J. Kittlesen, E. L. Huczko, C. L. Slingluff Jr., J. Shabanowitz, D. F. Hunt, and V. H. Engelhard (1998)
J. Exp. Med. 187, 37-48
   Abstract »    Full Text »    PDF »
Reduced Cell Surface Expression of HLA-C Molecules Correlates with Restricted Peptide Binding and Stable TAP Interaction.
A. Neisig, C. J. M. Melief, and J. Neefjes (1998)
J. Immunol. 160, 171-179
   Abstract »    Full Text »    PDF »
Introduction of a Glycosylation Site into a Secreted Protein Provides Evidence for an Alternative Antigen Processing Pathway: Transport of Precursors of Major Histocompatability Complex Class I-Restricted Peptides from the Endoplasmic Reticulum to the Cytosol.
I. Bacik, H. L. Snyder, L. C. Anton, G. Russ, W. Chen, J. R. Bennink, L. Urge, L. Otvos, B. Dudkowska, L. Eisenlohr, et al. (1997)
J. Exp. Med. 186, 479-487
   Abstract »    Full Text »    PDF »
Cloning and functional characterization of a subunit of the transporter associated with antigen processing.
S. Li, H.-O. Sjogren, U. Hellman, R. F. Pettersson, and P. Wang (1997)
PNAS 94, 8708-8713
   Abstract »    Full Text »    PDF »
Influences of Transporter Associated with Antigen Processing (TAP) on the Repertoire of Peptides Associated with the Endoplasmic Reticulum-resident Stress Protein gp96.
D. Arnold, C. Wahl, S. Faath, H.-G. Rammensee, and H. Schild (1997)
J. Exp. Med. 186, 461-466
   Abstract »    Full Text »    PDF »
The three-dimensional structure of an H-2Ld-peptide complex explains the unique interaction of Ld with beta-2 microglobulin and peptide.
G. K. Balendiran, J. C. Solheim, A. C. M. Young, T. H. Hansen, S. G. Nathenson, and J. C. Sacchettini (1997)
PNAS 94, 6880-6885
   Abstract »    Full Text »    PDF »
Membrane Topology of the ATP-binding Cassette Transporter Associated with Antigen Presentation (Tap1) Expressed in Escherichia coli.
U. Gileadi and C. F. Higgins (1997)
J. Biol. Chem. 272, 11103-11108
   Abstract »    Full Text »    PDF »
Intermediates in the Assembly and Degradation of Class I Major Histocompatibility Complex (MHC) Molecules Probed with Free Heavy Chain-specific Monoclonal Antibodies.
R. P. Machold and H. L. Ploegh (1996)
J. Exp. Med. 184, 2251-2260
   Abstract »    Full Text »    PDF »
Deglucosylation of N-linked glycans is an important step in the dissociation of calreticulin-class I-TAP complexes.
J. E. M. Van Leeuwen and K. P. Kearse (1996)
PNAS 93, 13997-14001
   Abstract »    Full Text »    PDF »
Binding of H-2Kb-specific Peptides to TAP and Major Histocompatibility Complex Class I in Microsomes from Wild-type, TAP1, and beta 2-Microglobulin Mutant Mice.
P. Wang, C. Raynoschek, K. Svensson, and H.-G. Ljunggren (1996)
J. Biol. Chem. 271, 24830-24835
   Abstract »    Full Text »    PDF »
In Vivo Assembly of the Proteasomal Complexes, Implications for Antigen Processing.
Y. Yang, K. Früh, K. Ahn, and P. A. Peterson (1995)
J. Biol. Chem. 270, 27687-27694
   Abstract »    Full Text »    PDF »
Dependence of Peptide Binding by MHC Class I Molecules on Their Interaction with TAP.
A. G. Grandea III, T. Spies, M. J. Androlewicz, R. S. Athwal, and D. E. Geraghty (1995)
Science 270, 105-108
   Abstract »    PDF »
Calnexin Influences Folding of Human Class I Histocompatibility Proteins but Not Their Assembly with beta(2)-Microglobulin.
M. Tector and R. D. Salter (1995)
J. Biol. Chem. 270, 19638-19642
   Abstract »    Full Text »    PDF »
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
   Abstract »    Full Text »    PDF »
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
   Abstract »    Full Text »    PDF »
Assembly and Intracellular Transport of MHC Class I and Class II Molecules.
M.R. Jackson, K. Fruh, L. Karlsson, L. Teyton, Y. Yang, and P.A. Peterson (1995)
Cold Spring Harb Symp Quant Biol 60, 249-261
   Abstract »    PDF »
Assembly, Peptide Loading, and Transport of MHC Class I Molecules in a Calnexin-negative Cell Line.
B.K. Sadasivan, A. Cariappa, G.L. Waneck, and P. Cresswell (1995)
Cold Spring Harb Symp Quant Biol 60, 267-275
   Abstract »    PDF »
Heat Shock Protein-chaperoned Peptides but Not Free Peptides Introduced into the Cytosol Are Presented Efficiently by Major Histocompatibility Complex I Molecules.
R. J. Binder, N. E. Blachere, and P. K. Srivastava (2001)
J. Biol. Chem. 276, 17163-17171
   Abstract »    Full Text »    PDF »
The Lectin Chaperone Calnexin Utilizes Polypeptide-based Interactions to Associate with Many of Its Substrates in Vivo.
U. G. Danilczyk and D. B. Williams (2001)
J. Biol. Chem. 276, 25532-25540
   Abstract »    Full Text »    PDF »


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