Membrane topology of the transporter associated with antigen processing (TAP1) within an assembled functional peptide-loading complex

doi:10.1074/jbc.M509784200

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Papers In Press, published online ahead of print January 5, 2006
J. Biol. Chem, 10.1074/jbc.M509784200
Submitted on September 6, 2005
Revised on December 2, 2005
Accepted on January 5, 2006

Membrane topology of the transporter associated with antigen processing (TAP1) within an assembled functional peptide-loading complex

Susanne Schrodt, Joachim Koch, and Robert Tampé

Insitute of Biochemsitry, Biocenter, Goethe-University Frankfurt, Frankfurt/M. D-60439

Corresponding Author: tampe{at}em.uni-frankfurt.de

The transporter associated with antigen processing (TAP) translocates antigenic peptides from the cytosol into the ER-lumen for subsequent loading onto MHC class I molecules. These peptide-MHC complexes are inspected at the cell surface by cytotoxic T-lymphocytes. Assembly of the functional peptide transport and loading complex depends on intra- and intermolecular packing of transmembrane helices (TMs). Here we examined the membrane topology of human TAP1 within an assembled and functional transport complex by cysteine-scanning mutagenesis. The accessibility of single cysteine residues facing the cytosol or ER-lumen was probed by a minimal invasive approach using membrane-impermeable, thiol-specific fluorophors in semi-permeabilized ‘living’ cells. TAP1 contains ten transmembrane segments placing the N- and C-terminus in the cytosol. The transmembrane domain consists of a translocation core of six TMs, a building block conserved among most ABC transporters, and a unique additional N-terminal domain of four TMs, essential for tapasin binding and assembly of the peptide-loading complex. This study provides a first map of the structural organization of the functional TAP complex.

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