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Interactions formed by individually expressed TAP1 and TAP2 polypeptide subunits

Interactions formed by individually expressed TAP1 and TAP2 polypeptide subunits
Interactions formed by individually expressed TAP1 and TAP2 polypeptide subunits
The transporter associated with antigen processing (TAP) supplies peptides into the lumen of the endoplasmic reticulum (ER) for binding by major histocompatibility complex (MHC) class I molecules. TAP comprises two polypeptides, TAP1 and TAP2, each a 'half-transporter' encoding a transmembrane domain and a nucleotide-binding domain. Immunoprecipitation of rat TAP1 and TAP2 expressed individually in the human TAP-deficient cell line, T2, revealed that both bound the endogenously expressed HLA-A2 and -B51 class I molecules. Using HLA-encoding recombinant vaccinia viruses HLA-A*2501, -B*2704, -B*3501 and -B*4402, alleles also associated with both TAP1 and TAP2. Thus, TAP1 and TAP2 do not appear to differ in their ability to interact with MHC class I alleles. Single TAP polypeptide subunits also formed MHC class I peptide-loading complexes, and their nucleotide-binding domains retained the ability to interact with ATP, and may permit the release of peptide-loaded MHC class I molecules in the absence of a peptide transport cycle. It is also demonstrated by chemical cross-linking that TAP2, but not TAP1, has the ability to form a homodimer complex both in whole cells and in detergent lysates. Together these data indicate that single TAP polypeptide subunits possess many of the features of the TAP heterodimer, demonstrating them to be useful models in the study of ATP-binding cassette (ABC) transporters.
0019-2805
182-189
Antoniou, Antony N.
3d711a3b-f688-46f9-823e-5bb925d10ea8
Ford, Stuart
911cc21c-13b6-42ff-bb0b-ba0d01ba1a42
Pilley, Elizabeth S.
1f140b4f-c51a-4f01-b2da-35e322a3eba4
Blake, Neil
5a18e7b9-8bcc-41be-b447-95d915fc0dfd
Powis, Simon J.
1bdcdc68-9097-459d-9675-7bb408316bf9
Antoniou, Antony N.
3d711a3b-f688-46f9-823e-5bb925d10ea8
Ford, Stuart
911cc21c-13b6-42ff-bb0b-ba0d01ba1a42
Pilley, Elizabeth S.
1f140b4f-c51a-4f01-b2da-35e322a3eba4
Blake, Neil
5a18e7b9-8bcc-41be-b447-95d915fc0dfd
Powis, Simon J.
1bdcdc68-9097-459d-9675-7bb408316bf9

Antoniou, Antony N., Ford, Stuart, Pilley, Elizabeth S., Blake, Neil and Powis, Simon J. (2002) Interactions formed by individually expressed TAP1 and TAP2 polypeptide subunits. Immunology, 106 (2), 182-189. (doi:10.1046/j.1365-2567.2002.01415.x).

Record type: Article

Abstract

The transporter associated with antigen processing (TAP) supplies peptides into the lumen of the endoplasmic reticulum (ER) for binding by major histocompatibility complex (MHC) class I molecules. TAP comprises two polypeptides, TAP1 and TAP2, each a 'half-transporter' encoding a transmembrane domain and a nucleotide-binding domain. Immunoprecipitation of rat TAP1 and TAP2 expressed individually in the human TAP-deficient cell line, T2, revealed that both bound the endogenously expressed HLA-A2 and -B51 class I molecules. Using HLA-encoding recombinant vaccinia viruses HLA-A*2501, -B*2704, -B*3501 and -B*4402, alleles also associated with both TAP1 and TAP2. Thus, TAP1 and TAP2 do not appear to differ in their ability to interact with MHC class I alleles. Single TAP polypeptide subunits also formed MHC class I peptide-loading complexes, and their nucleotide-binding domains retained the ability to interact with ATP, and may permit the release of peptide-loaded MHC class I molecules in the absence of a peptide transport cycle. It is also demonstrated by chemical cross-linking that TAP2, but not TAP1, has the ability to form a homodimer complex both in whole cells and in detergent lysates. Together these data indicate that single TAP polypeptide subunits possess many of the features of the TAP heterodimer, demonstrating them to be useful models in the study of ATP-binding cassette (ABC) transporters.

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Published date: 2002

Identifiers

Local EPrints ID: 26196
URI: http://eprints.soton.ac.uk/id/eprint/26196
ISSN: 0019-2805
PURE UUID: b9863837-d287-4be6-ac54-889b61672372

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Date deposited: 20 Apr 2006
Last modified: 15 Jul 2019 19:14

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Contributors

Author: Antony N. Antoniou
Author: Stuart Ford
Author: Elizabeth S. Pilley
Author: Neil Blake
Author: Simon J. Powis

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