A sequential model for peptide binding and transport by the transporters associated with antigen processing

Endert, Peter Van; Tampé, Robert; Meyer, Thomas; Tisch, Roland; Bach, Jean François; McDevitt, Hugh O.

doi:10.1016/1074-7613(94)90091-4

Cited by 283 publications

(259 citation statements)

References 24 publications

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“…The transmembrane domain harbors also the peptide-binding site, which was localized to the last cytosolic loop and a region of 15 amino acids after the last transmembrane helix of each TAP subunit [69]. Notably, both TAP subunits are required for peptide binding [90].…”

Section: Structural Organization Of the Tap Complexmentioning

confidence: 99%

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Intracellular peptide transporters in human – compartmentalization of the “peptidome”

Herget

Tampé

2006

Pflugers Arch - Eur J Physiol

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In the human genome, the five adenosine triphosphate (ATP)-binding cassette (ABC) half transporters ABCB2 (TAP1), ABCB3 (TAP2), ABCB9 (TAP-like), and in part, also ABCB8 and ABCB10 are closely related with regard to their structural and functional properties. Although targeted to different cellular compartments such as the endoplasmic reticulum (ER), lysosomes, and mitochondria, they are involved in intracellular peptide trafficking across membranes. The transporter associated with antigen processing (TAP1 and TAP2) constitute a key machinery in the major histocompatibility complex (MHC) class I-mediated cellular immune defense against infected or malignantly transformed cells. TAP translocates the cellular "peptidome" derived primarily from cytosolic proteasomal degradation into the ER lumen for presentation by MHC class I molecules. The homodimeric ABCB9 (TAP-like) complex located in lysosomal compartments shares structural and functional similarities to TAP; however, its biological role seems to be different from the MHC I antigen processing. ABCB8 and ABCB10 are targeted to the inner mitochondrial membrane. MDL1, the yeast homologue of ABCB10, is involved in the export of peptides derived from proteolysis of inner-membrane proteins into the intermembrane space. As such peptides are presented as minor histocompatibility antigens on the surface of mammalian cells, a physiological role of ABCB10 in the antigen processing can be accounted.

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Section: Structural Organization Of the Tap Complexmentioning

confidence: 99%

“…Peptide binding is ATP-independent [88,90], whereas, peptide translocation requires ATP hydrolysis [3,61,65,79]. Peptide binding is composed of a fast association step followed by a slow structural reorganization of the TAP complex [68].…”

Section: Chemo-mechanical Coupling Of Atp Hydrolysis and Peptide Tranmentioning

confidence: 99%

Intracellular peptide transporters in human – compartmentalization of the “peptidome”

Herget

Tampé

2006

Pflugers Arch - Eur J Physiol

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“…TAP1 and TAP2 have 10 and 9 transmembrane helices, respectively, where the 6 C-terminal helices from each subunit build together to form the so called 6+6 TM core complex which has been shown to be essential and sufficient for ER targeting, assembly of the heterodimer, binding of peptide and peptide translocation (Koch, Guntrum et al 2004). The translocation is a multistep process, beginning with association of peptides with TAP in an ATP-independent manner (Androlewicz, Anderson et al 1993;van Endert, Tampe et al 1994;Neumann and Tampe 1999). Peptides with a length of 8-16 amino acids are preferentially bound to TAP (van Endert, Tampe et al 1994).…”

Section: Tap Transports Cytosolic Peptides Into the Er And Supports Mmentioning

confidence: 99%

MHC Class I Quality Control

Røder

Ulfsson²,

Follin³

et al. 2012

Histocompatibility

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“…Immunodetection of LMP and TAP proteins was performed using enhanced chemiluminescence (ECL; Amersham, Buckinghamshire, UK) according to the manufacturer's instruction. For the detection of TAP1 and TAP2 proteins, the membranes were incubated overnight at room temperature with either anti-TAP1 mAb 148.3 (1:10 dilution of hybridoma supernatant) 68 or anti-TAP2 mAb 429.3 (1:20 dilution of hybridoma supernatant), 69 followed by a 1 h incubation with a 1:8000 dilution of horseradish peroxidase-conjugated goat anti-mouse polyclonal antibody (A4416; Sigma) at room temperature. After ECL detection the membrane was stripped of bound antibodies by incubation in a solution containing 60 mm Tris-HCl, 2% SDS, 100 mm ␤-mercaptoethanol, pH 6.7 at 50°C for 30 min.…”

Section: Indirect Immunofluorescencementioning

confidence: 99%

Gene transfer of human interferon gamma complementary DNA into a renal cell carcinoma line enhances MHC-restricted cytotoxic T lymphocyte recognition but suppresses non-MHC-restricted effector cell activity

et al. 2000

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Even though renal cell carcinomas (RCC) are thought to be immunogenic, many tumors express variations in surface molecules and intracellular proteins that hinder induction of optimal antitumor responses. Interferon gamma (IFN␥) stimulation can correct some of these deficiencies. Therefore, we introduced the complementary DNA (cDNA) encoding human IFN␥ into a well-characterized RCC line that has been selected for development of an allogeneic tumor cell vaccine for treatment of patients with metastatic disease. Studies were performed to determine how endogenous IFN␥ expression influences tumor cell immunogenicity. IFN␥ transductants showed minimal increases in surface expression of MHC class I and adhesion molecules but

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A sequential model for peptide binding and transport by the transporters associated with antigen processing

Cited by 283 publications

References 24 publications

Intracellular peptide transporters in human – compartmentalization of the “peptidome”

Intracellular peptide transporters in human – compartmentalization of the “peptidome”

MHC Class I Quality Control

Gene transfer of human interferon gamma complementary DNA into a renal cell carcinoma line enhances MHC-restricted cytotoxic T lymphocyte recognition but suppresses non-MHC-restricted effector cell activity

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